|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
166-341 |
1.66e-53 |
|
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.
Pssm-ID: 461464 [Multi-domain] Cd Length: 169 Bit Score: 174.59 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 166 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 235
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 236 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 315
Cdd:pfam04880 81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
|
170 180
....*....|....*....|....*.
gi 578828127 316 NRtggpasgRSSKNRDGGERRPSSTS 341
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-218 |
4.64e-09 |
|
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: 58.14 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 137
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 210
Cdd:TIGR02168 818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
....*...
gi 578828127 211 ELAVQQKQ 218
Cdd:TIGR02168 898 ELSEELRE 905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-220 |
4.87e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELEtQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 137
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ----RLKDEARDLRQELA 213
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerleRLEEELEELEEALA 431
|
....*..
gi 578828127 214 VQQKQEK 220
Cdd:COG1196 432 ELEEEEE 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-219 |
4.96e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 135
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 136 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 215
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
....
gi 578828127 216 QKQE 219
Cdd:COG1196 430 LAEL 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-220 |
9.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGY 122
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 123 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 202
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170
....*....|....*...
gi 578828127 203 DEARDLRQELAVQQKQEK 220
Cdd:COG1196 460 ALLELLAELLEEAALLEA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-219 |
1.10e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 137
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
..
gi 578828127 218 QE 219
Cdd:COG1196 478 AL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-220 |
1.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSREYEAELET---QLQQIETRNRDLLSENNRLRMELETIKEKFEVQH---SEGYRQISALE 129
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 130 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLR 209
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELA 399
|
170
....*....|.
gi 578828127 210 QELAVQQKQEK 220
Cdd:COG1196 400 AQLEELEEAEE 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-219 |
2.08e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDDLAQTKA 137
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
..
gi 578828127 218 QE 219
Cdd:COG1196 485 EL 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-233 |
4.93e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYEAE-----LETQLQQIETRNRDLLSENNRLRMELETIKEK---FEVQHSE-GYRQISALE 129
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGnGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 130 DDLAQTKAIKDQLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN----LLESVQRLKDEA 205
Cdd:COG4913 345 REIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRREL 421
|
170 180
....*....|....*....|....*...
gi 578828127 206 RDLRQELAVQQKQekpRTPMPSSVEAER 233
Cdd:COG4913 422 RELEAEIASLERR---KSNIPARLLALR 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-237 |
5.09e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYeAELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYRQISALEDDLAQTKAI 138
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 139 KDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAF-----LESELDEKENLLESVQRLKDEARDLRQEL- 212
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLateeeLQDLAEELEELQQRLAELEEELEEAQEELe 223
|
170 180
....*....|....*....|....*
gi 578828127 213 AVQQKQEKPRTPMPSSVEAERTDTA 237
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEA 248
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-218 |
5.76e-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: 54.68 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 66 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKAIKDQL 142
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828127 143 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 218
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
62-220 |
7.57e-08 |
|
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: 54.26 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 62 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRL---RMELETIK-EKFEVQHSEGYRQISALEDDLAQTKA 137
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 216
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
....
gi 578828127 217 KQEK 220
Cdd:TIGR04523 405 KLNQ 408
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-220 |
1.03e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyrqisALEDDLAQTKA 137
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----------EAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
...
gi 578828127 218 QEK 220
Cdd:COG1196 443 ALE 445
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
80-220 |
1.08e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 80 AELETQLQQIETRNRDLLSENNRLRMELETIK---EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYI------RELE 150
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828127 151 QANDDLERAKRAtIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQ-RLKDEARDLRQELAVQQKQEK 220
Cdd:COG1579 93 ALQKEIESLKRR-ISDLEDEILELMERIEE---LEEELAELEAELAELEaELEEKKAELDEELAELEAELE 159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
80-232 |
1.17e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 80 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVqhSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 159
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828127 160 KR---ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAE 232
Cdd:COG4913 691 EEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
58-243 |
1.32e-07 |
|
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: 52.84 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR--QISALE--- 129
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 130 --DDLAQT-------KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLesvQR 200
Cdd:COG4942 127 spEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---AR 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578828127 201 LKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGS 243
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-213 |
2.86e-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: 52.75 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 137
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 205
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974
|
....*...
gi 578828127 206 RDLRQELA 213
Cdd:TIGR02168 975 KRLENKIK 982
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
56-218 |
3.39e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSREYE------------AELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYR 123
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPD--ALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 124 QISALEDDLAQTKA-IKDQLQKY------IRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLL 195
Cdd:COG3206 264 VIQQLRAQLAELEAeLAELSARYtpnhpdVIALRAQIAALRAQLQQEAqRILASLEAELEALQAREASLQAQLAQLEARL 343
|
170 180
....*....|....*....|...
gi 578828127 196 ESVQRLKDEARDLRQELAVQQKQ 218
Cdd:COG3206 344 AELPELEAELRRLEREVEVAREL 366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-213 |
3.65e-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: 52.37 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 51 KDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSegyrQISALED 130
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN----EIERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQtkaIKDQLQKYIRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLR 209
Cdd:TIGR02168 408 RLER---LEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
....
gi 578828127 210 QELA 213
Cdd:TIGR02168 485 AQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-205 |
4.74e-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: 51.99 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA-----------------ELETQLQQIETRNRDLLSENNRLRM 105
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 106 ELETIKEKFEVQHSEgyrqISALEDDLAQTKAIK------DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIE 179
Cdd:TIGR02169 918 RLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
170 180
....*....|....*....|....*.
gi 578828127 180 RNAFLESELDEKENLLESVQRLKDEA 205
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-219 |
5.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 137
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
..
gi 578828127 218 QE 219
Cdd:COG1196 502 DY 503
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
73-218 |
5.51e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 73 EGSREYEAELETQLQQIETRnrdLLSENNRLRMElETIKEKFE------------VQHSEGYRQISALEDDLAQTKAIKD 140
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 141 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:PRK04863 514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
.
gi 578828127 218 Q 218
Cdd:PRK04863 590 Q 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-220 |
5.90e-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: 51.61 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIK- 111
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 112 --------------EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQK-------YIRELE-------QANDDLERAKRAT 163
Cdd:TIGR02169 787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqeQRIDLKeqiksieKEIENLNGKKEEL 866
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828127 164 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 220
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-220 |
6.22e-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: 51.60 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGS-----REYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfEVQHSEGYRQISALEDDLA 133
Cdd:TIGR02168 213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 134 QTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL- 212
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELe 371
|
....*....
gi 578828127 213 -AVQQKQEK 220
Cdd:TIGR02168 372 sRLEELEEQ 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-223 |
7.54e-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: 51.21 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELET 109
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 110 IKEKFevqhSEGYRqiSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQrLNqaiERNAFLESELD 189
Cdd:TIGR02168 941 LQERL----SEEYS--LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE-LK---ERYDFLTAQKE 1010
|
170 180 190
....*....|....*....|....*....|....*...
gi 578828127 190 E----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 223
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
58-285 |
7.68e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlSENNRLRMELETIKEkfevqhSEGyrqISALEDDLAQTKA 137
Cdd:COG3883 57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-YRSGGSVSYLDVLLG------SES---FSDFLDRLSALSK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828127 218 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 285
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
51-220 |
8.10e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 50.06 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 51 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKEkfevqhsegyrQISAL 128
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 129 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLL 195
Cdd:cd22656 192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLL 269
|
170 180
....*....|....*....|....*
gi 578828127 196 ESVQRlkDEARDLRQELAVQQKQEK 220
Cdd:cd22656 270 EDDIS--KIPAAILAKLELEKAIEK 292
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-213 |
9.87e-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: 50.84 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYEA--------ELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALED 130
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGyellkekeALERQKEAIERQ-----------LASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQ-TKAIKD-------QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EK 191
Cdd:TIGR02169 273 LLEElNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRR 352
|
170 180
....*....|....*....|..
gi 578828127 192 ENLLESVQRLKDEARDLRQELA 213
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELE 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-219 |
1.07e-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: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLRMELETIKEKF----------E 115
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEElrlevseleeEIEELQKELYALANEISRLEQQKQILRERLanlerqleelE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 116 VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQAND-------DLERAKRATIMSLEDFEQRLNQAIERNAFLESEL 188
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190
....*....|....*....|....*....|....*
gi 578828127 189 ----DEKENLLESVQRLKDEARDLRQELAVQQKQE 219
Cdd:TIGR02168 403 erleARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
79-223 |
1.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 79 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEgYRQisaLEDDLAQTKAIKDQLQKYIRELEQANDDLER 158
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE-YAE---LQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828127 159 AKRA--TIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRT 223
Cdd:COG4717 124 LLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-220 |
2.22e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 57 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSEN---NRLRMELETIKEKFEVQHS---EGYRQISALED 130
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealDELRAELTLLNEEAANLRErleSLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 210
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
170
....*....|
gi 578828127 211 ELAVQQKQEK 220
Cdd:TIGR02168 919 ELREKLAQLE 928
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-228 |
3.14e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYE---------AELETQLQQIETRNRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALE 129
Cdd:COG4913 634 EALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELK 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 130 DDLAQTKAIKDQLQkyiRELEQANDDLERA-KRATIMSLEDFEQRLNQAIERNAflesELDEKENLLESVQRLKDEARDL 208
Cdd:COG4913 713 GEIGRLEKELEQAE---EELDELQDRLEAAeDLARLELRALLEERFAAALGDAV----ERELRENLEERIDALRARLNRA 785
|
170 180
....*....|....*....|
gi 578828127 209 RQELAVQQKQEKPRTPMPSS 228
Cdd:COG4913 786 EEELERAMRAFNREWPAETA 805
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
56-228 |
3.15e-06 |
|
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: 48.61 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFevqhSEGYRQISALEDDLAQT 135
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 136 KAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLES-VQRLKDEARDLRQE 211
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERaelEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEAL 228
|
170
....*....|....*..
gi 578828127 212 LAVQQKQEKPRTPMPSS 228
Cdd:COG4942 229 IARLEAEAAAAAERTPA 245
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
80-196 |
1.06e-05 |
|
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: 45.67 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 80 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV--QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDLE 157
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578828127 158 RAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 196
Cdd:pfam13851 113 QRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-220 |
1.29e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 69 REFQEGSREYEAEL--------ETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR----------QISALED 130
Cdd:COG1196 216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqaEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 210
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170
....*....|
gi 578828127 211 ELAVQQKQEK 220
Cdd:COG1196 376 EAEEELEELA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-218 |
1.37e-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: 46.68 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 127 ALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 206
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93
|
90
....*....|..
gi 578828127 207 DLRQELAVQQKQ 218
Cdd:COG4942 94 ELRAELEAQKEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-208 |
1.61e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 44 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYEAELET---QLQQIETRNRDLLSENNRLRMELETIKEKFEVQhse 120
Cdd:TIGR02168 361 EELEAELEEL----ESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEA--- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 121 gyrQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 200
Cdd:TIGR02168 434 ---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
....*...
gi 578828127 201 LKDEARDL 208
Cdd:TIGR02168 511 LLKNQSGL 518
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
52-222 |
2.23e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 52 DLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE------GYRQ- 124
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 125 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 185
Cdd:pfam12128 723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802
|
170 180 190
....*....|....*....|....*....|....*...
gi 578828127 186 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 222
Cdd:pfam12128 803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
36-219 |
2.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 36 SGKTFSSEEEEANYWKDLAMTyKQRAENTQEELREFQEGSREYEAELE---TQLQQIETRNRDLLSENNRLRMELETIKE 112
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 113 K----------FEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNA 182
Cdd:TIGR02168 748 RiaqlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190
....*....|....*....|....*....|....*..
gi 578828127 183 FLESELDEKENLLESVQRLKDEARDLRQELAVQQKQE 219
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-235 |
2.65e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 44 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYE---AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE 120
Cdd:TIGR04523 303 QKEQDWNKEL----KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 121 --GYR--------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAIERnafLESELDE 190
Cdd:TIGR04523 379 nqSYKqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----EIERLKETIIKNNSEIKD---LTNQDSV 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828127 191 KENLLESVQRLKD-----------EARDLRQELAVQQKQEKPRTPMPSSVEAERTD 235
Cdd:TIGR04523 452 KELIIKNLDNTREsletqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
58-206 |
3.44e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEgsrEYEAeLETQLQQIETRNRDLLSENNRLRMELETIK---EKFEVQHSEG--YRQISALEDDL 132
Cdd:COG1579 23 EHRLKELPAELAELED---ELAA-LEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828127 133 AQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 206
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
37-205 |
5.77e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 37 GKTFSSEEEEANYWKDLAMTYKQRAENTQ----EELREFQEGSREYEAELETQLQQIETRNRDLLSennrlrmELETIKE 112
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKATESLEEQlaaaEAEQELEESKRETETGIQNLTAEIEQGQESLTE-------NLEAIKE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 113 KFEvqHSEGYRQISALEDDLaqtKAIKDQLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEKE 192
Cdd:COG5185 362 EIE--NIVGEVELSKSSEEL---DSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQAT 433
|
170
....*....|...
gi 578828127 193 NLLESVQRLKDEA 205
Cdd:COG5185 434 SSNEEVSKLLNEL 446
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
58-203 |
6.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSE--NNR----LRMELETIKekfevqhsegyRQISALEDD 131
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNvrNNKeyeaLQKEIESLK-----------RRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828127 132 LAQTKAIKDQLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 203
Cdd:COG1579 112 ILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
123-195 |
6.30e-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: 44.75 E-value: 6.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828127 123 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 195
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
33-220 |
7.20e-05 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 43.59 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREF--QEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI 110
Cdd:PRK14160 1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIekEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 111 KEKFE--VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 183
Cdd:PRK14160 81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578828127 184 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 220
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
51-220 |
7.43e-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: 45.11 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 51 KDLAMTYKQRAENTQEEL-REFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALE 129
Cdd:pfam15921 244 EDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 130 DDLAQtkaIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLR 209
Cdd:pfam15921 324 STVSQ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKRE 390
|
170
....*....|.
gi 578828127 210 QELAVQQKQEK 220
Cdd:pfam15921 391 KELSLEKEQNK 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
56-222 |
7.61e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRD-----LLSENNRLRMELETIKEKFEVQHSegyrQISALED 130
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELSARYTPNHP----DVIALRA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQTKA-IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIErnafLESELDEKENLLESVQRLKDEARDLR 209
Cdd:COG3206 299 QIAALRAqLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRL 374
|
170
....*....|...
gi 578828127 210 QELAVQQKQEKPR 222
Cdd:COG3206 375 EEARLAEALTVGN 387
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-208 |
8.37e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAI 138
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828127 139 KDQLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 208
Cdd:COG1196 762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-212 |
1.15e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 44 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELEtQLQQIetrnRDLLSENNRLRMELETIKEKFEVQH----- 118
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERI----RTLLAAIADAEDEIERLREKREALAelnde 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 119 -----SEGYRQISALEDD-----LAQTKAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLE 185
Cdd:PRK02224 625 rrerlAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALE 704
|
170 180
....*....|....*....|....*..
gi 578828127 186 SELDEKENLLESVQRLKDEARDLRQEL 212
Cdd:PRK02224 705 NRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
60-219 |
1.22e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 60 RAENTQEELrefqEGSREYEAELetqLQQIETRNRDLLSEnnrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIK 139
Cdd:pfam07888 28 RAELLQNRL----EECLQERAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 140 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEARdlrqELAVQQKQE 219
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK----KAGAQRKEE 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-216 |
1.22e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 65 QEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKEKFEvqhsEGYRQISALEDDLAQTKAIKDQLQK 144
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 145 YIRELEQANDDLERAkratimsLEDFEQRLNQAI------------ERNAFLESELDEKENLLESVQRLKDEARDLRQEL 212
Cdd:TIGR02169 766 RIEELEEDLHKLEEA-------LNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
....
gi 578828127 213 AVQQ 216
Cdd:TIGR02169 839 QEQR 842
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
72-222 |
1.33e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 72 QEGSREYEAELETQLQQIETRNRDL-----LSENNRLRME-----LETIKEkfEVQHSEGY-------RQISALEDDLAQ 134
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELeqklsVADAARRQFEkayelVCKIAG--EVERSQAWqtarellRRYRSQQALAQR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 135 TKAIKDQLqkyiRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAV 214
Cdd:COG3096 514 LQQLRAQL----AELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
....*...
gi 578828127 215 QQKQEKPR 222
Cdd:COG3096 586 QLEQLRAR 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
81-221 |
1.45e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 81 ELETQLQQIETR--NRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLER 158
Cdd:TIGR02168 217 ELKAELRELELAllVLRLEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828127 159 AkratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 221
Cdd:TIGR02168 296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-218 |
1.55e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 44 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLR-------ME 106
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerfgdapvDLGNAEDFLEELREERDELRereaeleAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 107 LETIKEKFEV--------------QHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKratimSLEDFEQ 172
Cdd:PRK02224 435 LRTARERVEEaealleagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-----DLVEAED 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578828127 173 RLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQQKQ 218
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREA 559
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
53-222 |
1.90e-04 |
|
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: 43.57 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 53 LAMTYKQRAENTQEELREFQ-EGSREYEAELE-TQLQQIETRNRDLLSENNRLRMELETIKeKFEVQHSEGYRQISALED 130
Cdd:pfam17380 342 MAMERERELERIRQEERKRElERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQTKAIKDQL-QKYIRELEQanddlERAKRATIMSLEDFEQRlnQAIERNAFLESELDEKENLLESVQRLKDEARDLR 209
Cdd:pfam17380 421 EMEQIRAEQEEArQREVRRLEE-----ERAREMERVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
|
170
....*....|...
gi 578828127 210 QELAVQQKQEKPR 222
Cdd:pfam17380 494 RKILEKELEERKQ 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-224 |
2.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 66 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEkFEVQHSEGYRQISALEDDLAQTKAIKDQLQKY 145
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 146 IReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------ELDEKENLLESVQRLKDEARDLRQEL 212
Cdd:PRK03918 296 IK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkELEKRLEELEERHELYEEAKAKKEEL 374
|
170
....*....|..
gi 578828127 213 AVQQKQEKPRTP 224
Cdd:PRK03918 375 ERLKKRLTGLTP 386
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
57-220 |
2.60e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 57 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRN---RDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDdla 133
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKELIIKNLDNTRESLE----TQLKVLSR--- 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 134 QTKAIKDQLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQ 210
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDF 552
|
170
....*....|....*..
gi 578828127 211 EL-------AVQQKQEK 220
Cdd:TIGR04523 553 ELkkenlekEIDEKNKE 569
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
53-222 |
2.75e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 53 LAMTYKQRAENTQEELREFQEGSREYEAELE---TQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsEGYRQISALE 129
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQ----AAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 130 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR--LKDEARD 207
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAE 180
|
170
....*....|....*
gi 578828127 208 LRQELAVQQKQEKPR 222
Cdd:COG4372 181 AEQALDELLKEANRN 195
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
58-223 |
2.91e-04 |
|
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: 43.04 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEdDLAQTKA 137
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL-ELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRATIMSLedfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESS---KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
....*.
gi 578828127 218 QEKPRT 223
Cdd:pfam02463 304 KLERRK 309
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
51-212 |
3.29e-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: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 51 KDLAMTYKQRAEnTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALED 130
Cdd:TIGR02169 237 RQKEAIERQLAS-LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 DLAQTKAikdQLQKYIRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESV----QRLKDEAR 206
Cdd:TIGR02169 316 ELEDAEE---RLAKLEAEIDKLLAEIEELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELK 388
|
....*.
gi 578828127 207 DLRQEL 212
Cdd:TIGR02169 389 DYREKL 394
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
28-221 |
3.40e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 28 SPVFTMEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSEN---NRLR 104
Cdd:COG5185 230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFE-NTKEKIAEYtksIDIK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 105 MELETIKE---------KFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIR-----------------ELEQANDDLER 158
Cdd:COG5185 309 KATESLEEqlaaaeaeqELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienivgevelsksseELDSFKDTIES 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828127 159 AKRatimslEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 221
Cdd:COG5185 389 TKE------SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-230 |
3.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 48 NYWKDLA---MTYKQRAENTQEELR---EFQEGSREYEAELETQLQQI---ETRNRDLLSENNRLRMELETIKEKFEvQH 118
Cdd:PRK03918 162 NAYKNLGeviKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREIneiSSELPELREELEKLEKEVKELEELKE-EI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 119 SEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLE-RAKRatimsLEDFEQRLNQAIERNAFLESELDEKenlles 197
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEeKVKE-----LKELKEKAEEYIKLSEFYEEYLDEL------ 309
|
170 180 190
....*....|....*....|....*....|...
gi 578828127 198 vQRLKDEARDLRQELAVQQKQEKPRTPMPSSVE 230
Cdd:PRK03918 310 -REIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
170-225 |
4.50e-04 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 40.72 E-value: 4.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828127 170 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 225
Cdd:COG3166 43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
51-234 |
5.78e-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: 42.02 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 51 KDLAMTYKQRAENTQEELR----EFQEGSREYE----------AELEtQLQQIETRNRDLLSENNRLRMELETIKEK--- 113
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKiitmELQKKSSELEemtkfknnkeVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKeqe 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 114 --FEVQHSEgyRQISALEddlAQTKAIKDQLQKYIRELEQANDDLERAKRATI--------MSLED-----------FEQ 172
Cdd:pfam05483 441 liFLLQARE--KEIHDLE---IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltahcdkLLLENkeltqeasdmtLEL 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828127 173 RLNQAIERNAFLESE--LDEKENLLESVQRLKDEARDLRQELavQQKQEKPRTPMPSSVEAERT 234
Cdd:pfam05483 516 KKHQEDIINCKKQEErmLKQIENLEEKEMNLRDELESVREEF--IQKGDEVKCKLDKSEENARS 577
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
86-284 |
7.95e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 86 LQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIM 165
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 166 SLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVP 245
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
|
170 180 190
....*....|....*....|....*....|....*....
gi 578828127 246 STPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARIS 284
Cdd:COG3883 284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-219 |
8.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 66 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfeVQHSEgyrQISALEDDLAQTKAIKDQLQKY 145
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELK---ELKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 146 IRELEQANDDLE---RAKRATIMSLEDFEQRLNQAIERNAFLE---SELDEKENLLESVQRLKDEARDLRQELAVQQKQE 219
Cdd:PRK03918 309 LREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
51-213 |
8.59e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 51 KDLAMTYKQRAEnTQEELREFQEGSREYEAE---LETQLQQIETRNrdlLSENnrlrmELETIKEKFEV-QHSEGYRQ-- 124
Cdd:COG0497 158 EEYREAYRAWRA-LKKELEELRADEAERAREldlLRFQLEELEAAA---LQPG-----EEEELEEERRRlSNAEKLREal 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 125 ---ISALEDD----LAQTKAIKDQLQKYIRELEQANDDLERAKRATImSLEDFEQRLNQAIERNAFLESELDEKENLLES 197
Cdd:COG0497 229 qeaLEALSGGeggaLDLLGQALRALERLAEYDPSLAELAERLESALI-ELEEAASELRRYLDSLEFDPERLEEVEERLAL 307
|
170 180
....*....|....*....|...
gi 578828127 198 VQRLK-------DEARDLRQELA 213
Cdd:COG0497 308 LRRLArkygvtvEELLAYAEELR 330
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
10-220 |
9.18e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 10 WASRKEILRHHATRRVISSPVFTMEDSGKTFSSEEEEANYWKDLAMTykqrAENTQEELREFQEGSREYEAELETQL--- 86
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT----ALRQQEKIERYQADLEELEERLEEQNevv 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 87 -----QQIETRNRDLLSEN--NRLRMELETIKEKFEVQHSEG--YRQ-ISALE--------DDLAQTKAIK--DQLQKYI 146
Cdd:PRK04863 372 eeadeQQEENEARAEAAEEevDELKSQLADYQQALDVQQTRAiqYQQaVQALErakqlcglPDLTADNAEDwlEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 147 RELEQANDDLERAKRATIMSLEDFEQ------RLNQAIERNAF------LESELDEKENLLESVQRLKDEARDLRQELAV 214
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQFEQayqlvrKIAGEVSRSEAwdvareLLRRLREQRHLAEQLQQLRMRLSELEQRLRQ 531
|
....*.
gi 578828127 215 QQKQEK 220
Cdd:PRK04863 532 QQRAER 537
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
80-266 |
1.27e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 80 AELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 159
Cdd:pfam00529 61 DSAEAQLAKAQAQ-----------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 160 K-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprtpmPSSVEAERTD 235
Cdd:pfam00529 130 RvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ-------IAEAEAELKL 202
|
170 180 190
....*....|....*....|....*....|.
gi 578828127 236 TAVQATGSVPSTPIAHRGPSSSLNTPGSFRR 266
Cdd:pfam00529 203 AKLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
58-218 |
1.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEkfevqhsegyrQISALEDDLAQTka 137
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE-----------ELEQLEEELEQA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 iKDQLQKYIRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELD----EKENLLESVQRLKDEARDLRQELA 213
Cdd:COG4372 72 -RSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLEAQIAELQSEIA 146
|
....*
gi 578828127 214 VQQKQ 218
Cdd:COG4372 147 EREEE 151
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
42-220 |
1.42e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 42 SEEEEANYWKDLAMTYKQRaENTQEELREFQEGSRE------YEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFE 115
Cdd:COG5185 210 SETGNLGSESTLLEKAKEI-INIEEALKGFQDPESEledlaqTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 116 VQHSEGYRQISALEDDLAQTKAIkDQLQKYIRELEqANDDLERAKRATIMSLEDFEQRLNQaiernafleseldEKENLL 195
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKAT-ESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQ-------------GQESLT 353
|
170 180
....*....|....*....|....*
gi 578828127 196 ESVQRLKDEARDLRQELAVQQKQEK 220
Cdd:COG5185 354 ENLEAIKEEIENIVGEVELSKSSEE 378
|
|
| PRKG1_interact |
pfam15898 |
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ... |
129-208 |
1.66e-03 |
|
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.
Pssm-ID: 464927 [Multi-domain] Cd Length: 102 Bit Score: 37.67 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 129 EDDLAQTKAIKDQLQKYIRELEQANDDLERA---------KRATIMSLEDFEQRlnqAIERNAF-LESELDEKENLLESV 198
Cdd:pfam15898 7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83
|
90
....*....|
gi 578828127 199 QRLKDEARDL 208
Cdd:pfam15898 84 QRLKDENGAL 93
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
76-111 |
1.74e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 40.20 E-value: 1.74e-03
10 20 30
....*....|....*....|....*....|....*.
gi 578828127 76 REYEAELETQLQQIETRNRDLLSENNRLRMELETIK 111
Cdd:PRK03992 7 EERNSELEEQIRQLELKLRDLEAENEKLERELERLK 42
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
40-206 |
1.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 40 FSSEEEEANYWKDLAMTYKQ--RAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKEKF-EV 116
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL----EELRKELEELEKKYsEE 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 117 QHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRAtimsledfeqrLNQAIERNAFLESELDEKENLLE 196
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE-----------REKAKKELEKLEKALERVEELRE 728
|
170
....*....|
gi 578828127 197 SVQRLKDEAR 206
Cdd:PRK03918 729 KVKKYKALLK 738
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
52-240 |
1.91e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 39.42 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 52 DLAMTYKQRAENTQEELREFQegsREYEAELETQLQqiETRNRDLLSENNRLRMELETIKEK--------FEVQHSEGYR 123
Cdd:pfam17045 74 ELVAKYEQQLQKLQEELSKLK---RSYEKLQRKQLK--EAREEAKSREEDRSELSRLNGKLEefrqksleWEQQRLQYQQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 124 QISALEddlAQTKAIKDQL-----QKYIRELEQANDDLErAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL-ES 197
Cdd:pfam17045 149 QVASLE---AQRKALAEQSsliqsAAYQVQLEGRKQCLE-ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELgDS 224
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578828127 198 VQRLKDEARDLRQELAVQQKQEKPRtpmpsSVEAERTDTAVQA 240
Cdd:pfam17045 225 NRKLLEEQQRLLEELRMSQRQLQVL-----QNELMELKATLQS 262
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-217 |
1.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 42 SEEEEanywKDLAMTYKQRAENTQEELREFQEGSREYEAE---LETQLQQIET--RNRDLLSENNRLRMELETI-KEKFE 115
Cdd:PRK03918 446 TEEHR----KELLEEYTAELKRIEKELKEIEEKERKLRKElreLEKVLKKESEliKLKELAEQLKELEEKLKKYnLEELE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 116 vQHSEGYR-----------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLE----RAKRATIMSLEDFE---QRLNQA 177
Cdd:PRK03918 522 -KKAEEYEklkekliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAellkELEELGFESVEELEerlKELEPF 600
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578828127 178 IERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
123-218 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 123 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAfLESELDEKENLLES----- 197
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREA----LQRLAEYSWDEIDVAS-AEREIAELEAELERldass 684
|
90 100
....*....|....*....|...
gi 578828127 198 --VQRLKDEARDLRQELAVQQKQ 218
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEE 707
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
174-236 |
2.03e-03 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 39.58 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828127 174 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVEAERTDT 236
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-220 |
2.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 59 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKF-EVQHSEgyrqiSALEDDLAQTKA 137
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlELKDAE-----KELEREEKELKK 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKR-----ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 212
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKeleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
....*...
gi 578828127 213 AVQQKQEK 220
Cdd:PRK03918 704 EEREKAKK 711
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
65-206 |
2.49e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 65 QEELREFQEGSREYEAELETQLQQIETrnrdLLSENNRLRMELETIKEKFEVQH-------SEGYRQIsaleddLAQTKA 137
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEdklleeaEKEAQQA------IKEAKK 584
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578828127 138 IKDQLQKYIRELEQANDDLERAKRatimsLEDFEQRLNQAIERnafLESELDEKENLLESVQrLKDEAR 206
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVKAHE-----LIEARKRLNKANEK---KEKKKKKQKEKQEELK-VGDEVK 644
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
62-217 |
2.62e-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: 40.09 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 62 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIkeKFEVQHSEGYRQisALEDDLAQTKAIKDQ 141
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI--KMSLQRSMSTQK--ALEEDLQIATKTICQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 142 LQKyirELEQANDDLERAK----------RATIMSLEDF----EQRLNQAIERNAFLESELDEKENLLESVQRLKD---- 203
Cdd:pfam05483 329 LTE---EKEAQMEELNKAKaahsfvvtefEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnkev 405
|
170
....*....|....
gi 578828127 204 EARDLRQELAVQQK 217
Cdd:pfam05483 406 ELEELKKILAEDEK 419
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
54-204 |
2.64e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 54 AMTYKQRAENTQEElrEFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI-KEKFEVQHSEgyRQISALEDDL 132
Cdd:PRK12704 51 AEAIKKEALLEAKE--EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKE--KELEQKQQEL 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578828127 133 AQTKA-IKDQLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESVQRLKDE 204
Cdd:PRK12704 127 EKKEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAIQRCAAD 204
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
76-218 |
2.82e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 76 REYEA--ELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEgyrqisaleddLAQTKAIKDQLQKYIRELEQAN 153
Cdd:PRK04778 300 REVKArkYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESE-----------LESVRQLEKQLESLEKQYDEIT 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828127 154 DDLERAKRATIMSLEDFEQRLNQ--AIErnafleselDEKENLLESVQRLKDEARDLRQELAVQQKQ 218
Cdd:PRK04778 369 ERIAEQEIAYSELQEELEEILKQleEIE---------KEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
81-228 |
2.90e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 38.79 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 81 ELETQLQQIETRNRDLlSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAK 160
Cdd:pfam15934 76 HQIKQLQSMITGYSDI-SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEEQCQELKRAN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 161 RatimSLEDFEQRLNQaIERnafLESELDEKENLL-ESVQRLKD-EARDLRQELAVQQKQEKPRTPMPSS 228
Cdd:pfam15934 155 R----RVQSLQTRLSQ-VEK---LQEELRTERKILrEEVIALKEkDAKSNGRERALQDQLKCCQTEIEKS 216
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-212 |
3.16e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRL---RMELETIKEKFEVQ-------HSEGYRQISA 127
Cdd:pfam01576 351 RQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEGQlqelqarLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 128 LEDdlaqtkaikdQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARD 207
Cdd:pfam01576 431 LAE----------KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
....*
gi 578828127 208 LRQEL 212
Cdd:pfam01576 501 LQEQL 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-217 |
3.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREyeaELETQLQQIETRNRDLLSENNrLRMELETIKEKFEVQHSEgyrqISALEDDLAQTKA 137
Cdd:PRK03918 569 EEELAELLKELEELGFESVE---ELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEE----LDKAFEELAETEK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 138 IKDQLQKYIRELEQANDDLE-RAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQ 216
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEE---LEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
.
gi 578828127 217 K 217
Cdd:PRK03918 718 K 718
|
|
| GrpE |
pfam01025 |
GrpE; |
79-159 |
3.49e-03 |
|
GrpE;
Pssm-ID: 425996 [Multi-domain] Cd Length: 165 Bit Score: 37.97 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 79 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyRQISaleddlaqtKAIKDQLQKYIRELEQANDDLER 158
Cdd:pfam01025 13 IESLEEEIEELEKKIEELKEKLLRALAEFENLRKRTE-------KEKE---------EAKKFAIEKFAKDLLPVIDNLER 76
|
.
gi 578828127 159 A 159
Cdd:pfam01025 77 A 77
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
99-212 |
3.50e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 38.84 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 99 ENNRLRMELETIKEKFEVQHSEGYRQIS--ALEDDLAQTKAIKDQLqkyIRELEQANDDLERAKRATIMSLE----DFEQ 172
Cdd:PRK06669 34 EKERLREEEEEQVEQLREEANDEAKEIIeeAEEDAFEIVEAAEEEA---KEELLKKTDEASSIIEKLQMQIEreqeEWEE 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578828127 173 RLNQAIER---NAFLESELDEKENLLESVQRLKDEARDLRQEL 212
Cdd:PRK06669 111 ELERLIEEakaEGYEEGYEKGREEGLEEVRELIEQLNKIIEKL 153
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
123-225 |
3.89e-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: 38.98 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 123 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllesvQRLK 202
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------AELE 100
|
90 100
....*....|....*....|...
gi 578828127 203 DEARDLRQELAVQQKQEKPRTPM 225
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLA 123
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
43-217 |
4.15e-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: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETR-------NRDLLSENNRLRMELETIKE--- 112
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKleeeiqeNKDLIKENNATRHLCNLLKEtca 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 113 -------KFEVQHSEGY-----------RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLErakratimslEDFEQRL 174
Cdd:pfam05483 166 rsaektkKYEYEREETRqvymdlnnnieKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLE----------EEYKKEI 235
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578828127 175 NQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 217
Cdd:pfam05483 236 NDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
58-213 |
4.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGY--RQI 125
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEEleeeldelkgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeeRFA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 126 SALEDDLAQT--KAIKDQLQKYIRELEQANDDLERAKR--------------ATIMSLEDFEQRLNQAIE---------- 179
Cdd:COG4913 757 AALGDAVERElrENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglpeyeerf 836
|
170 180 190
....*....|....*....|....*....|....
gi 578828127 180 RNAFLESELDEKENLLesvQRLKDEARDLRQELA 213
Cdd:COG4913 837 KELLNENSIEFVADLL---SKLRRAIREIKERID 867
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
56-218 |
4.43e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRN-RDLLSENNRLRMELETIKEKFEVQHSEGYRQISALED---- 130
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDEEIERYEEQREQARETRDEADEvlee 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 131 ------DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDE 204
Cdd:PRK02224 246 heerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170
....*....|....
gi 578828127 205 ARDLRQELAVQQKQ 218
Cdd:PRK02224 326 LRDRLEECRVAAQA 339
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
58-203 |
4.51e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAELE----------TQLQQ---IETRNRDLLSENNRLRMELETIKEKFEvQHSEGYRQ 124
Cdd:COG3096 305 QYRLVEMARELEELSARESDLEQDYQaasdhlnlvqTALRQqekIERYQEDLEELTERLEEQEEVVEEAAE-QLAEAEAR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 125 ISALEDDLaqtKAIKDQLQKYIRELE----------QANDDLERAKR---ATIMSLEDFEQRLNQAIERnaflESELDEK 191
Cdd:COG3096 384 LEAAEEEV---DSLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYLAAFRAK----EQQATEE 456
|
170
....*....|..
gi 578828127 192 enLLESVQRLKD 203
Cdd:COG3096 457 --VLELEQKLSV 466
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
58-213 |
5.54e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 38.86 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEG-SREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTK 136
Cdd:pfam05701 97 KQDSELAKLRVEEMEQGiADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 137 AIKDQLQKYIRELEQANDDLERAKRAtimSLEDFEQRLNQAIERNA---FLESELDEKEnllESVQRLKDE---ARDLRQ 210
Cdd:pfam05701 177 EIEKTVEELTIELIATKESLESAHAA---HLEAEEHRIGAALAREQdklNWEKELKQAE---EELQRLNQQllsAKDLKS 250
|
...
gi 578828127 211 ELA 213
Cdd:pfam05701 251 KLE 253
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
124-219 |
5.96e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.22 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 124 QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ---- 199
Cdd:pfam08614 58 LLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQdelv 137
|
90 100 110
....*....|....*....|....*....|....
gi 578828127 200 --------------RLKDEARDLRQELaVQQKQE 219
Cdd:pfam08614 138 alqlqlnmaeeklrKLEKENRELVERW-MKRKGQ 170
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
66-190 |
6.10e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 36.46 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 66 EELREFQEGSREYEAELETQLQQietrnrdLLSENNRLRMELETIKEKFE---VQHSEGYRQISALEDDLAQTKA----I 138
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQK-------LQEDLEKQAEIAREAQQNYErelVLHAEDIKALQALREELNELKAeiaeL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578828127 139 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDE 190
Cdd:pfam07926 77 KAEAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
11-261 |
6.27e-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: 38.57 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 11 ASRKEILRHHATRRVISSPVFTMEDsgktFSSEEEEAnywkdlamtyKQRAENTQEELREfQEGSREYEAELETQlQQIE 90
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQ----IRAEQEEA----------RQREVRRLEEERA-REMERVRLEEQERQ-QQVE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 91 TRNRDllsENNRLRMELETIKEKFEVQHSEGYRqisaleddlaqtkaiKDQLQKYIRELEQANDDLERAKRATIMSLEDF 170
Cdd:pfam17380 464 RLRQQ---EEERKRKKLELEKEKRDRKRAEEQR---------------RKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 171 EQRLNQAIERNAFLESELDEKEnlLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTPIA 250
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPI 603
|
250
....*....|.
gi 578828127 251 HRGPSSSLNTP 261
Cdd:pfam17380 604 YRPRISEYQPP 614
|
|
| BAR |
cd07307 |
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ... |
57-197 |
6.29e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.
Pssm-ID: 153271 [Multi-domain] Cd Length: 194 Bit Score: 37.42 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 57 YKQRAENTQEELREFQEGSREYEAeleTQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYrqisaLEDDLAQTK 136
Cdd:cd07307 26 LPAAAEKLSEALQELGKELPDLSN---TDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEY-----LKKDLKEIK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828127 137 AIKDQLQKYIRELEQANDDLERAKRATIMS--LEDFEQRLNQAIERNAFLESELDEKENLLES 197
Cdd:cd07307 98 KRRKKLDKARLDYDAAREKLKKLRKKKKDSskLAEAEEELQEAKEKYEELREELIEDLNKLEE 160
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
58-180 |
7.07e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 36.51 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 58 KQRAENTQEELREFQEGSREYEAEL---ETQLQQIETRNRDLLSENNRLRMELETIKEKFE-----VQHSEGY-RQISAL 128
Cdd:pfam12718 6 KLEAENAQERAEELEEKVKELEQENlekEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEeseklKTNNENLtRKIQLL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578828127 129 EDDLAQT-KAIKDQLQKyIRELEQANDDLERAKRATIMSLEDFEQRLNQAIER 180
Cdd:pfam12718 86 EEELEESdKRLKETTEK-LRETDVKAEHLERKVQALEQERDEWEKKYEELEEK 137
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
87-218 |
7.27e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 38.57 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 87 QQIETRNRDLLSENNRLRMELETIKEKFEVQhsegyRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIms 166
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELE-----KKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578828127 167 leDFEQRLNQAIERNAFLESELDEKENLLESVQR-LKDEARDLRQELAVQQKQ 218
Cdd:pfam05557 76 --ELNRLKKKYLEALNKKLNEKESQLADAREVIScLKNELSELRRQIQRAELE 126
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
56-203 |
7.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 56 TYKQRAENTQEELREFQEGSR------EYEAELETQL-------QQIETRNRDLL---SENNRLRMELETIKEKFEVQHS 119
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRfvqqhgNALAQLEPIVsvlqsdpEQFEQLKQDYQqaqQTQRDAKQQAFALTEVVQRRAH 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 120 EGYRQIsalEDDLAQTKAIKDQLQKYIRELEQandDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEK-ENLLESV 198
Cdd:PRK04863 971 FSYEDA---AEMLAKNSDLNEKLRQRLEQAEQ---ERTRAREQ----LRQAQAQLAQYNQVLASLKSSYDAKrQMLQELK 1040
|
....*
gi 578828127 199 QRLKD 203
Cdd:PRK04863 1041 QELQD 1045
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
80-218 |
8.17e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 37.69 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 80 AELETQ-------LQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEgyrqisaleddLAQTKAIKDQLQKYIRELEQA 152
Cdd:smart00787 126 ARLEAKkmwyewrMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSI-----------KPKLRDRKDALEEELRQLKQL 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828127 153 NDDLERAKRATIMSL-EDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 218
Cdd:smart00787 195 EDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
60-213 |
8.93e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 38.23 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 60 RAENTQEELREFQEGSREYEAELETQLQQietrnrdllsennrlRMELETIKEKFEVQHSEGYRQISAL----EDDLAQT 135
Cdd:pfam01576 736 RDEQGEEKRRQLVKQVRELEAELEDERKQ---------------RAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQL 800
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578828127 136 KAIKDQLQKYIRELEQAnddleRAKRATIMSL-EDFEQRLNQaiernafLESELDEKENLLESVQRLKDEARDLRQELA 213
Cdd:pfam01576 801 KKLQAQMKDLQRELEEA-----RASRDEILAQsKESEKKLKN-------LEAELLQLQEDLAASERARRQAQQERDELA 867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-218 |
9.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 83 ETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA--- 159
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAall 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828127 160 KRATIMSLEDFEQRLNQAIERN------AFLESELDE-------------KENLLESVQRLKDEARDLRQELAVQQKQ 218
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQelkeelEELEEQLEEllgeleellealdEEELEEELEELEEELEELEEELEELREE 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-213 |
9.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.82 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 42 SEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRME--LETIKEKFEVQHS 119
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAGV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828127 120 EGyrqisalEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDF-EQRLNQAIERnafLESELDEKENLLEsv 198
Cdd:COG4717 382 ED-------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdEEELEEELEE---LEEELEELEEELE-- 449
|
170
....*....|....*
gi 578828127 199 qRLKDEARDLRQELA 213
Cdd:COG4717 450 -ELREELAELEAELE 463
|
|
| |
