NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18403838|ref|NP_564600|]
View 

actin binding protein family [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 138-349 5.80e-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: 55.83  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    138 ENEINRLRNTVRALRERERCLEDKLLEYYslKEQQKIAMELRS-RLKLNQMETKVFNFK--IKKLQAENEKLKAECFEHS 214
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELR--KELEELEEELEQlRKELEELSRQISALRkdLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    215 KVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQEE---------EIKAVLPDL--EADKMMQRLRDLESEI 283
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalrealdELRAELTLLneEAANLRERLESLERRI 833

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18403838    284 NELTDTNTRLQFENFELSEKLESVQiianskleepEEIETLREDCNRLRSENEELKKDVEQLQGDR 349
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLA----------AEIEELEELIEELESELEALLNERASLEEAL 889
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-349 5.80e-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: 55.83  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    138 ENEINRLRNTVRALRERERCLEDKLLEYYslKEQQKIAMELRS-RLKLNQMETKVFNFK--IKKLQAENEKLKAECFEHS 214
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELR--KELEELEEELEQlRKELEELSRQISALRkdLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    215 KVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQEE---------EIKAVLPDL--EADKMMQRLRDLESEI 283
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalrealdELRAELTLLneEAANLRERLESLERRI 833

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18403838    284 NELTDTNTRLQFENFELSEKLESVQiianskleepEEIETLREDCNRLRSENEELKKDVEQLQGDR 349
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLA----------AEIEELEELIEELESELEALLNERASLEEAL 889
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
246-347 4.38e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.47  E-value: 4.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 246 LSLKQRVARLQEEEIKAVLPDLEADK---------MMQRLRDLESEINELTDTNTRLQFE-------NFELSEKLESVQI 309
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKeheerelteEEEEIRRLEEQVERLEAEVEELEAEleekderIERLERELSEARS 455

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18403838 310 IANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEERERIEELKR 493
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-347 5.53e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  132 EEEADHENEINRLRNTVRALRERERCLEDKLleyyslKEQQKIAMELRSRLKlnQMETKVFNFK-IKKLQAENEKLKAEC 210
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKI------RELEERIEELKKEIE--ELEEKVKELKeLKEKAEEYIKLSEFY 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  211 FEHSKVLLELDMAKSQVQVLKKKLnintQQHVAQILSLKQRVARLQE--EEIKAVLPDLEAD-KMMQRLRDLESEINELT 287
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKklKELEKRLEELEERhELYEEAKAKKEELERLK 378

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  288 DTNTRLQFEnfELSEKLESVQiiaNSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:PRK03918 379 KRLTGLTPE--KLEKELEELE---KAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 138-341 7.67e-05

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: 45.88  E-value: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    138 ENEINRLRNTVRALRERERCLEDKLLEYYSLKEqqkiamelRSRLKLNQME-TKVFNFKIKKLQAENEKLKAECFEHSKV 216
Cdd:pfam15921  492 ESSERTVSDLTASLQEKERAIEATNAEITKLRS--------RVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKV 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    217 lleldmaksqVQVLKKKLNINTQ---QHVAQILSLKQRVARLqEEEIKAVLPDLEADKMMQRLRDleSEINELTDTNTRL 293
Cdd:pfam15921  564 ----------IEILRQQIENMTQlvgQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKDKKD--AKIRELEARVSDL 630

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 18403838    294 QFENFEL----SEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKD 341
Cdd:pfam15921  631 ELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-349 5.80e-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: 55.83  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    138 ENEINRLRNTVRALRERERCLEDKLLEYYslKEQQKIAMELRS-RLKLNQMETKVFNFK--IKKLQAENEKLKAECFEHS 214
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELR--KELEELEEELEQlRKELEELSRQISALRkdLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    215 KVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQEE---------EIKAVLPDL--EADKMMQRLRDLESEI 283
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalrealdELRAELTLLneEAANLRERLESLERRI 833

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18403838    284 NELTDTNTRLQFENFELSEKLESVQiianskleepEEIETLREDCNRLRSENEELKKDVEQLQGDR 349
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLA----------AEIEELEELIEELESELEALLNERASLEEAL 889
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-347 7.57e-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: 55.45  E-value: 7.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    136 DHENEINRLRNTVRALRERERCLEDKLLEY-YSLKEQQKIAMELRSRLKLNQMETKVFNFKIKKLQAENEKLKAECFEHS 214
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    215 KVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQE--EEIKAVLPDLEADKMMQRLRDLESEINELTDTNTR 292
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrrERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 18403838    293 LQFENFELSEKLESVQiiaNSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:TIGR02168  452 LQEELERLEEALEELR---EELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
246-347 4.38e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.47  E-value: 4.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 246 LSLKQRVARLQEEEIKAVLPDLEADK---------MMQRLRDLESEINELTDTNTRLQFE-------NFELSEKLESVQI 309
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKeheerelteEEEEIRRLEEQVERLEAEVEELEAEleekderIERLERELSEARS 455

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18403838 310 IANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEERERIEELKR 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-347 9.15e-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: 48.90  E-value: 9.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    117 ETPRSDITAPLAFPSEEEADHENEINRLRNTVRALRERERCLEDKL-LEYYSLKEQQKIAMELRSRLKLNQMETKVFNFK 195
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    196 IKKLQAENEKLKAECFEHSKVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQE--EEIKAVLPDLEA--DK 271
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqiEELSEDIESLAAeiEE 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    272 MMQRLRDLESEINELTD----TNTRLQFENFELSEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:TIGR02168  864 LEELIEELESELEALLNerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 85-356 1.99e-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: 47.76  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838     85 RRECDLDEKDVFLLPEFEEEAKKLDLLVCDDCETPRSDITAPLAFPSEEEADHENEINRLRNTVRALRERERCLE---DK 161
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkiKD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    162 LLEYYSLKEQQKIAmELRSRLKLNQMETKVFNFKIKKLQAENEKLKAEcfeHSKVLLELDMAKSQVQVLKKKLnintQQH 241
Cdd:TIGR02169  284 LGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAE---IDKLLAEIEELEREIEEERKRR----DKL 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    242 VAQILSLKQR----VARLQEEEIKAVLPDLEADKMMQRLRDLESEINELTDTNTRLQFENFELSEKLESVQiiansklee 317
Cdd:TIGR02169  356 TEEYAELKEEledlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN--------- 426

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 18403838    318 pEEIETLREDCNRLRSENEELKKDVEQLQGDRCTDLEQL 356
Cdd:TIGR02169  427 -AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-347 5.53e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  132 EEEADHENEINRLRNTVRALRERERCLEDKLleyyslKEQQKIAMELRSRLKlnQMETKVFNFK-IKKLQAENEKLKAEC 210
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKI------RELEERIEELKKEIE--ELEEKVKELKeLKEKAEEYIKLSEFY 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  211 FEHSKVLLELDMAKSQVQVLKKKLnintQQHVAQILSLKQRVARLQE--EEIKAVLPDLEAD-KMMQRLRDLESEINELT 287
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKklKELEKRLEELEERhELYEEAKAKKEELERLK 378

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  288 DTNTRLQFEnfELSEKLESVQiiaNSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:PRK03918 379 KRLTGLTPE--KLEKELEELE---KAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 138-341 7.67e-05

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: 45.88  E-value: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    138 ENEINRLRNTVRALRERERCLEDKLLEYYSLKEqqkiamelRSRLKLNQME-TKVFNFKIKKLQAENEKLKAECFEHSKV 216
Cdd:pfam15921  492 ESSERTVSDLTASLQEKERAIEATNAEITKLRS--------RVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKV 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    217 lleldmaksqVQVLKKKLNINTQ---QHVAQILSLKQRVARLqEEEIKAVLPDLEADKMMQRLRDleSEINELTDTNTRL 293
Cdd:pfam15921  564 ----------IEILRQQIENMTQlvgQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKDKKD--AKIRELEARVSDL 630

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 18403838    294 QFENFEL----SEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKD 341
Cdd:pfam15921  631 ELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 164-314 1.08e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 43.36  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838   164 EYYSlkEQQKIAMELRSRLKlNQMETkvfnfkIKKLQAENEKLKAECFEHSKVLLE-LDMAKSQVQVLKKKLnintQQHV 242
Cdd:pfam13851  15 NYYN--DITRNNLELIKSLK-EEIAE------LKKKEERNEKLMSEIQQENKRLTEpLQKAQEEVEELRKQL----ENYE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838   243 AQILSLKQRVARL--QEEEIKAVlpDLEADKMMQRLRDLESEINELTDTNT--------RLQFENFELSEKLESVQIIAN 312
Cdd:pfam13851  82 KDKQSLKNLKARLkvLEKELKDL--KWEHEVLEQRFEKVERERDELYDKFEaaiqdvqqKTGLKNLLLEKKLQALGETLE 159


                  ..
gi 18403838   313 SK 314
Cdd:pfam13851 160 KK 161
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-361 1.16e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 132 EEEADHENEINRLRNTVRALRERERcledklleyyslkeqqkiamELRSRLKLNQMETKVFNFKIKKLQAENEKLKAECF 211
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRR--------------------ELEERLEELEEELAELEEELEELEEELEELEEELE 347

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 212 EHSKVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQEEEIKAVLPDLEADkmmQRLRDLESEINELTDTNT 291
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEEELE 424

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 292 RLQFENFELSEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQGDRCTDLEQLVYLRW 361
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 134-347 2.57e-04

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: 43.94  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838   134 EADHENEINRLRNTVRALRERERCLEDKLLEYYSLKEQqkiamelrSRLKLNQMETKVfnfkikKLQAENEKLKAECFEH 213
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEE--------SRDKANQLEEKT------KLQDENLKELIEKKDH 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838   214 -SKVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQEEEIKA------VLPDLEAD--KMMQRLRDLESEIN 284
Cdd:pfam05483 294 lTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfVVTEFEATtcSLEELLRTEQQRLE 373

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18403838   285 ELTDTNTRLQFENFELSEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-354 4.25e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    138 ENEINRLRNTVRALRERERCLEDKLLEYYSlkEQQKIAMELRS--------RLKLNQMETKVFNFKIKKLQAENEKLKAE 209
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKS--ELKELEARIEEleedlhklEEALNDLEARLSHSRIPEIQAELSKLEEE 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    210 CFEHSKVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVA--RLQEEEIKAVLPDLEA--DKMMQRLRDLESEINE 285
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsiEKEIENLNGKKEELEEelEELEAALRDLESRLGD 886

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18403838    286 LTDTNTRLQFENFELSEKLEsvqiiansklEEPEEIETLREDCNRLRSENEELKKDVEQLQGDRCTDLE 354
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIE----------ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 131-346 5.08e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    131 SEEEADHENEINRLRNTVRALRERERCLEDKLLEYY-SLKEQQKIAMELRSRLKLNQMETKVFNFKIKKLQAENEKLKAE 209
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    210 CFEHSKVLLELDMAKSQvqvLKKKLNINTQQHVAQILSLKQRVARLQEEE---IKAVLPDLEAD--KMMQRLRDLESEIN 284
Cdd:TIGR02169  760 LKELEARIEELEEDLHK---LEEALNDLEARLSHSRIPEIQAELSKLEEEvsrIEARLREIEQKlnRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18403838    285 ELTDTNTRLQFENFELSEKLESVQIIANSKLEEPEEIETLREDcnrLRSENEELKKDVEQLQ 346
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD---LESRLGDLKKERDELE 895
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 133-355 5.97e-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: 42.80  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    133 EEADHENEINRLRNTVRALrERERCLEDKLLEYYSLKEQQKIAMELRSRLKLNQMETKVFNFKI---KKLQaENEKLKAE 209
Cdd:pfam15921  136 ESQSQEDLRNQLQNTVHEL-EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEasgKKIY-EHDSMSTM 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    210 CFEH-----SKVLLELDMAKS-----------QVQVLK----KKLNINTQQHVAQI-------------LSLKQRVARLQ 256
Cdd:pfam15921  214 HFRSlgsaiSKILRELDTEISylkgrifpvedQLEALKsesqNKIELLLQQHQDRIeqliseheveitgLTEKASSARSQ 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    257 EEEIKAVLPDLEADK------MMQRLRDLESEINELTDTNTRLQFENFELSEKLESVQIIANSKLEEPE-EIETLREDCN 329
Cdd:pfam15921  294 ANSIQSQLEIIQEQArnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARtERDQFSQESG 373

                          250       260
                   ....*....|....*....|....*.
gi 18403838    330 RLRSENEELKKDVEQLQGDRCTDLEQ 355
Cdd:pfam15921  374 NLDDQLQKLLADLHKREKELSLEKEQ 399
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
131-347 9.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 9.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  131 SEEEADHENEINRLRNTVRALRERERCLEDKLLEYYSLKEQQKIAMELRSrlklnqMETKVFNFKIKKLQAENEklkaec 210
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE------LEEKLKKYNLEELEKKAE------ 525

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  211 fEHSKVLLELDMAKSQVQVLKKKLNintqqhvaQILSLKQRVARLQEEeikavlpdleadkmmqrLRDLESEINELTDTN 290
Cdd:PRK03918 526 -EYEKLKEKLIKLKGEIKSLKKELE--------KLEELKKKLAELEKK-----------------LDELEEELAELLKEL 579

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18403838  291 TRLQFENF-ELSEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:PRK03918 580 EELGFESVeELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-347 1.47e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  132 EEEADHENEINRLRNTVRALRERERCLEDKLLEYYSLKEQQKIAMELRSRLKLNQME------------TKVFNFKIKKL 199
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEklekeleelekaKEEIEEEISKI 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  200 QAENEKLKAECFEHSKVLLELDMAKSQVQVLKKKLninTQQHVAQIL-SLKQRVARLQEEEIKAvlpDLEADKMMQRLRD 278
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKCPVCGREL---TEEHRKELLeEYTAELKRIEKELKEI---EEKERKLRKELRE 484

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18403838  279 LESEINELTDTNTRLQFENF--ELSEKLESVQIianSKLEEP-EEIETLREDCNRLRSENEELKKDVEQLQG 347
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQlkELEEKLKKYNL---EELEKKaEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
172-346 2.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 172 QKIAMELRSRLKLNQMETKVFNFKIKKLQAENEKLKAECFEHSKVLLELDMAKSQVQVLKKKLNiNTQQHVAQILSLKQR 251
Cdd:COG4717  49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 252 VARLQE-EEIKAVLPDLEA--DKMMQRLRDLESEINELTDTNTRLQFENFELSEKLESVQIIANSKLEE--------PEE 320
Cdd:COG4717 128 LPLYQElEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDlaeeleelQQR 207

                       170       180
                ....*....|....*....|....*.
gi 18403838 321 IETLREDCNRLRSENEELKKDVEQLQ 346
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLE 233
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 276-346 2.35e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 37.26  E-value: 2.35e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18403838 276 LRDLESEINELTDTNTRLQFENFELSEKlesvqiiaNSKLEEpeEIETLREDCNRLRSENEELKKDVEQLQ 346
Cdd:COG3074   6 LEELEAKVQQAVDTIELLQMEVEELKEK--------NEELEQ--ENEELQSENEELQSENEQLKTENAEWQ 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 132-346 2.35e-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: 40.81  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    132 EEEADHENEINRLRNTVRALRERERCLEDKLLEY-YSLKEQQKIAMELRSRLKLNQMETKVFNFKIKKLQAENEKLKAEC 210
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    211 FEHSKVLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVA---RLQEEEIKAVLPDLEADKMM--QRLRDLESEINE 285
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeySLTLEEAEALENKIEDDEEEarRRLKRLENKIKE 983

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18403838    286 LTDTNtrlqfenfelseklesvqiianskLEEPEEIETLREDCNRLRSENEELKKDVEQLQ 346
Cdd:TIGR02168  984 LGPVN------------------------LAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
131-346 2.61e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 131 SEEEADHENEINRLRNTVRALRERERCLEDKLLEYYSlKEQQKIA--MELRSRLKLNQMETKVFNFKIKKLQAENEKLKA 208
Cdd:COG1340   7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAE-KRDELNAqvKELREEAQELREKRDELNEKVKELKEERDELNE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 209 EcfehskvlleLDMAKSQVQVLKKKLNiNTQQHVAQILSLKQRVARLQEEEIKAVLPDLEADKMMQRLRDLESEI----- 283
Cdd:COG1340  86 K----------LNELREELDELRKELA-ELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELekakk 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18403838 284 -----NELTDTNTRLQFENFELSEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQ 346
Cdd:COG1340 155 aleknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQ 222
46 PHA02562
endonuclease subunit; Provisional
 168-360 3.10e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  168 LKEQQKIAMELRSRLKLNQMEtkvFNFKIKKLQAENEKLKAECFEHSKVLLELDMAKSQVQVLKKKLNINTQQHVAQILS 247
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIAR---KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQ 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  248 LkQRVARLQEE--EIKAVLPDL-EADKMMQRLRDLESEIN-ELTDTNTRLQfenfELSEKLESVQIIANSKLEEPEEIET 323
Cdd:PHA02562 274 F-QKVIKMYEKggVCPTCTQQIsEGPDRITKIKDKLKELQhSLEKLDTAID----ELEEIMDEFNEQSKKLLELKNKIST 348

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 18403838  324 LREDCNRLRSENEELKKDVEQLQGDRCTDLEQLVYLR 360
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 197-346 3.17e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 197 KKLQAENEKLKAECFehskvLLELDMAKSQVQVLKKKLNINTQQHVAQILSLKQRVARLQEEEIKAVLPDLEADKMMQRL 276
Cdd:COG1196 216 RELKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18403838 277 RDLESEINELT----DTNTRLQFENFELSEKLESVQIIANSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQ 346
Cdd:COG1196 291 YELLAELARLEqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 171-357 4.31e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 171 QQKIAMELRSRLKLNQmetkvfnfkiKKLQAENEKLKAECFEHSKVLLELDMAKSQVQVLKKKLN-INTQQHV--AQILS 247
Cdd:COG4942  18 QADAAAEAEAELEQLQ----------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRaLEQELAAleAELAE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838 248 LKQRVARL------QEEEIKAVLPDL-------------------EADKMMQRLRDL----ESEINELTDTNTRLQFENF 298
Cdd:COG4942  88 LEKEIAELraeleaQKEELAELLRALyrlgrqpplalllspedflDAVRRLQYLKYLaparREQAEELRADLAELAALRA 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18403838 299 ELSEKLESVQIIANSKLEEPEEIETLREDCN----RLRSENEELKKDVEQLQGDRcTDLEQLV 357
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQkllaRLEKELAELAAELAELQQEA-EELEALI 229
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-360 4.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  195 KIKKLQAENEKLKAECFEHSKVLLELDMAKSQVQVLKKKLN---------INTQQHVAQILSLKQRVARLQE-----EEI 260
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeIDVASAEREIAELEAELERLDAssddlAAL 690

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  261 KAVLPDLEAdkmmqRLRDLESEINELTDTNTRLQFENFELSEKLESVQII--ANSKLEEPEEIETLREDCNRLRSEN--- 335
Cdd:COG4913  691 EEQLEELEA-----ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleAAEDLARLELRALLEERFAAALGDAver 765

                        170       180
                 ....*....|....*....|....*...
gi 18403838  336 ---EELKKDVEQLQGDRCTDLEQLVYLR 360
Cdd:COG4913  766 elrENLEERIDALRARLNRAEEELERAM 793
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
136-348 4.48e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  136 DHENEINRLRNTVRALRERERCLEDKLLEYYSLKEQQKiamELRSRLKLNQMETKVFNFKIKKLQAENEKLKAECFEHSK 215
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK---EKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  216 VLLELDMAKSQVQVL---KKKLNINTQQHVAQILSLKQRVARLqeEEIKAVLPDLEADKmmQRLRDLESEINELTDTNTR 292
Cdd:PRK03918 236 LKEEIEELEKELESLegsKRKLEEKIRELEERIEELKKEIEEL--EEKVKELKELKEKA--EEYIKLSEFYEEYLDELRE 311

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18403838  293 LQFENFELSEKLESVQiiansklEEPEEIETLREDCNRLRSENEELKKDVEQLQGD 348
Cdd:PRK03918 312 IEKRLSRLEEEINGIE-------ERIKELEEKEERLEELKKKLKELEKRLEELEER 360
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 138-346 7.02e-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: 39.23  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838   138 ENEINRLRNTVRALRERERCLEDKLleyYSLKEQQKiamELRSRLKLNQMETKVFNFKIKKLQAENEKLKAECFEHSKvl 217
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQD---SVKELIIK---NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK-- 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838   218 lELDMAKSQVQVLKKKLNINTQQhvaqILSLKQRVARLqEEEIKavlpdleadKMMQRLRDLESEINELTDTNTRLQFEN 297
Cdd:TIGR04523 497 -ELKKLNEEKKELEEKVKDLTKK----ISSLKEKIEKL-ESEKK---------EKESKISDLEDELNKDDFELKKENLEK 561

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 18403838   298 felseklesvqiianSKLEEPEEIETLREDCNRLRSENEELKKDVEQLQ 346
Cdd:TIGR04523 562 ---------------EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 131-369 7.33e-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: 39.57  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    131 SEEEADHENEINRLRNTVRALRERERCLEDKLLEYYSLKEQQKIAMELRSRLKLNQMETKvfNFKIKKLQAENEKLKAEC 210
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE--YLLYLDYLKLNEERIDLL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    211 FEHSKVLLELDMAKSQVQVLKKKLNintqQHVAQILSLKQRVARLQEEEIKAVLPDLEADKmmQRLRDLESEINELTDTN 290
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKL----AQVLKENKEEEKEKKLQEEELKLLAKEEEELK--SELLKLERRKVDDEEKL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838    291 TRLQFENFELSEKLESVQIIANSKLEEPEEIETLR-------EDCNRLRSENEELKKDVEQLQGDRCTDLEQLVYLRWIN 363
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKReaeeeeeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396


                   ....*.
gi 18403838    364 ACLRYE 369
Cdd:pfam02463  397 LELKSE 402
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
114-356 9.51e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 9.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  114 DDCETPRSDITAPLAFPSEEEADHENEINRLRNTVRALRERERcLEDKLLEYYSLKEQQKIAMELRSRlklnqmetkvfn 193
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER-LEERREDLEELIAERRETIEEKRE------------ 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  194 fKIKKLQAENEKLKAECFEH----SKVLLELDMAKSQVQVLKKKLNINTQQ---------HVAQILSLKQRVARLQEE-E 259
Cdd:PRK02224 538 -RAEELRERAAELEAEAEEKreaaAEAEEEAEEAREEVAELNSKLAELKERieslerirtLLAAIADAEDEIERLREKrE 616

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18403838  260 IKAVLPDLEADKMM---QRLRDLESEINELTDTNTRLQFENFElsEKLESVQiianskleepEEIETLREDCNRLRS--- 333
Cdd:PRK02224 617 ALAELNDERRERLAekrERKRELEAEFDEARIEEAREDKERAE--EYLEQVE----------EKLDELREERDDLQAeig 684

                        250       260       270
                 ....*....|....*....|....*....|
gi 18403838  334 -------ENEELKKDVEQLQgDRCTDLEQL 356
Cdd:PRK02224 685 aveneleELEELRERREALE-NRVEALEAL 713
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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