|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
134-309 |
1.54e-54 |
|
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: 176.13 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880 81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
|
170 180
....*....|....*....|....*.
gi 221316642 284 NRtggpasgRSSKNRDGGERRPSSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-187 |
2.83e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
....
gi 221316642 184 QKQE 187
Cdd:COG1196 430 LAEL 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-188 |
3.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELEtQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ----RLKDEARDLRQELA 181
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerleRLEEELEELEEALA 431
|
....*..
gi 221316642 182 VQQKQEK 188
Cdd:COG1196 432 ELEEEEE 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-186 |
3.75e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168 818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
....*...
gi 221316642 179 ELAVQQKQ 186
Cdd:TIGR02168 898 ELSEELRE 905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-188 |
4.25e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 11 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGY 90
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170
....*....|....*...
gi 221316642 171 DEARDLRQELAVQQKQEK 188
Cdd:COG1196 460 ALLELLAELLEEAALLEA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-187 |
4.99e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
..
gi 221316642 186 QE 187
Cdd:COG1196 478 AL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-188 |
1.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRM------ELETIKEKFEVQHSEGYRQISALE 97
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 98 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELA 399
|
170
....*....|.
gi 221316642 178 QELAVQQKQEK 188
Cdd:COG1196 400 AQLEELEEAEE 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-187 |
1.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDDLAQTKA 105
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
..
gi 221316642 186 QE 187
Cdd:COG1196 485 EL 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-201 |
3.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 27 QRAENTQEELREFQEGSREYEAE-----LETQLQQIETRNRDLLSENNRLRMELETIKEK---FEVQHSE-GYRQISALE 97
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGnGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 98 DDLAQTKAIKDQLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN----LLESVQRLKDEA 173
Cdd:COG4913 345 REIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRREL 421
|
170 180
....*....|....*....|....*...
gi 221316642 174 RDLRQELAVQQKQekpRTPMPSSVEAER 201
Cdd:COG4913 422 RELEAEIASLERR---KSNIPARLLALR 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-186 |
3.85e-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: 51.98 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKAIKDQL 110
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221316642 111 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-200 |
4.08e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVqhSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221316642 128 KR---ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAE 200
Cdd:COG4913 691 EEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-188 |
7.23e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyrqisALEDDLAQTKA 105
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----------EAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
...
gi 221316642 186 QEK 188
Cdd:COG1196 443 ALE 445
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-211 |
8.79e-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: 50.15 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQ---------- 92
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 93 ----ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLesvQR 168
Cdd:COG4942 127 spedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---AR 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 221316642 169 LKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGS 211
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-186 |
1.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 27 QRAENTQEELREFQEGSREYeAELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 107 KDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERnaFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQ--LSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
24-186 |
1.67e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 24 TYKQRAENTQEELREFQEGSREYE------------AELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYR 91
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPD--ALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 92 QISALEDDLAQTKA-IKDQLQKY------IRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG3206 264 VIQQLRAQLAELEAeLAELSARYtpnhpdVIALRAQIAALRAQLQQEAqRILASLEAELEALQAREASLQAQLAQLEARL 343
|
170 180
....*....|....*....|...
gi 221316642 164 ESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG3206 344 AELPELEAELRRLEREVEVAREL 366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-181 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 173
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974
|
....*...
gi 221316642 174 RDLRQELA 181
Cdd:TIGR02168 975 KRLENKIK 982
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-188 |
2.01e-06 |
|
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: 49.25 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 30 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRL---RMELETIK-EKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
....
gi 221316642 185 KQEK 188
Cdd:TIGR04523 405 KLNQ 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-181 |
2.43e-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: 49.28 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 19 KDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSegyrQISALED 98
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN----EIERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQTKAIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
...
gi 221316642 179 ELA 181
Cdd:TIGR02168 486 QLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-187 |
2.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
..
gi 221316642 186 QE 187
Cdd:COG1196 502 DY 503
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
41-186 |
2.86e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 41 EGSREYEAELETQLQQIETRnrdLLSENNRLRMElETIKEKFE------------VQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863 514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
.
gi 221316642 186 Q 186
Cdd:PRK04863 590 Q 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-180 |
3.64e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 27 QRAENTQEELREFQEGS-----REYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfEVQHSEGYRQISALEDDLA 101
Cdd:TIGR02168 213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221316642 102 QTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-173 |
4.42e-06 |
|
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: 48.53 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 11 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA-----------------ELETQLQQIETRNRDLLSENNRLRM 73
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 74 ELETIKEKFEVQHSEgyrqISALEDDLAQTKAIK------DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIE 147
Cdd:TIGR02169 918 RLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
170 180
....*....|....*....|....*.
gi 221316642 148 RNAFLESELDEKENLLESVQRLKDEA 173
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
48-188 |
4.67e-06 |
|
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: 47.23 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 48 AELETQLQQIETRNRDLLSENNRLRMELETIK---EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYI------RELE 118
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221316642 119 QANDDLERAKRAtIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQ-RLKDEARDLRQELAVQQKQEK 188
Cdd:COG1579 93 ALQKEIESLKRR-ISDLEDEILELMERIEE---LEEELAELEAELAELEaELEEKKAELDEELAELEAELE 159
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
26-253 |
5.09e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlSENNRLRMELETIKEkfevqhSEGyrqISALEDDLAQTKA 105
Cdd:COG3883 57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-YRSGGSVSYLDVLLG------SES---FSDFLDRLSALSK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221316642 186 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-188 |
7.48e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIK- 79
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 80 --------------EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQK-------YIRELE-------QANDDLERAKRAT 131
Cdd:TIGR02169 787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqeQRIDLKeqiksieKEIENLNGKKEEL 866
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221316642 132 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-191 |
7.83e-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: 47.74 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELET 77
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 78 IKEKFEVQHSegyrqiSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEqrlnQAIERNAFLESELD 157
Cdd:TIGR02168 941 LQERLSEEYS------LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE----ELKERYDFLTAQKE 1010
|
170 180 190
....*....|....*....|....*....|....*...
gi 221316642 158 E----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-187 |
1.07e-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: 47.36 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 24 TYKQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLRMELETIKEKF----------E 83
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEElrlevseleeEIEELQKELYALANEISRLEQQKQILRERLanlerqleelE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 84 VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQAND-------DLERAKRATIMSLEDFEQRLNQAIERNAFLESEL 156
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190
....*....|....*....|....*....|....*
gi 221316642 157 ----DEKENLLESVQRLKDEARDLRQELAVQQKQE 187
Cdd:TIGR02168 403 erleARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-188 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 25 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSEN---NRLRMELETIKEKFEVQHS---EGYRQISALED 98
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealDELRAELTLLNEEAANLRErleSLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
170
....*....|
gi 221316642 179 ELAVQQKQEK 188
Cdd:TIGR02168 919 ELREKLAQLE 928
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
24-196 |
1.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFevqhSEGYRQISALEDDLAQT 103
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 104 KAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLES-VQRLKDEARDLRQE 179
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERaelEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEAL 228
|
170
....*....|....*..
gi 221316642 180 LAVQQKQEKPRTPMPSS 196
Cdd:COG4942 229 IARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-196 |
1.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 48 AELETQLQQIETRNRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQkyiRELEQANDDLERA 127
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---EELDELQDRLEAA 739
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 128 -KRATIMSLEDFEQRLNQAIERNAflesELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSS 196
Cdd:COG4913 740 eDLARLELRALLEERFAAALGDAV----ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-181 |
1.48e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 27 QRAENTQEELREFQEGSREYEA--------ELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALED 98
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGyellkekeALERQKEAIERQ-----------LASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQ-TKAIKD-------QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EK 159
Cdd:TIGR02169 273 LLEElNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRR 352
|
170 180
....*....|....*....|..
gi 221316642 160 ENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELE 374
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-191 |
1.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 47 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLER 126
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221316642 127 AKRA--TIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:COG4717 124 LLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
19-188 |
1.97e-05 |
|
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: 45.82 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 19 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKEkfevqhsegyrQISAL 96
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLL 163
Cdd:cd22656 192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLL 269
|
170 180
....*....|....*....|....*
gi 221316642 164 ESVQRlkDEARDLRQELAVQQKQEK 188
Cdd:cd22656 270 EDDIS--KIPAAILAKLELEKAIEK 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-186 |
4.05e-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: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 95 ALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 174
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93
|
90
....*....|..
gi 221316642 175 DLRQELAVQQKQ 186
Cdd:COG4942 94 ELRAELEAQKEE 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-187 |
7.01e-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: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 37 REFQEGSREYEAEL--------ETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKA 105
Cdd:COG1196 216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElelELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
..
gi 221316642 186 QE 187
Cdd:COG1196 376 EA 377
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-176 |
9.95e-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: 44.28 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 10 SEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELET---QLQQIETRNRDLLSENNRLRMELETIKEKFEVQh 86
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 87 segyrQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESV 166
Cdd:TIGR02168 434 -----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
170
....*....|
gi 221316642 167 QRLKDEARDL 176
Cdd:TIGR02168 509 KALLKNQSGL 518
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
20-190 |
1.30e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 20 DLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE------GYRQ- 92
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 93 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128 723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802
|
170 180 190
....*....|....*....|....*....|....*...
gi 221316642 154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128 803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
48-164 |
1.41e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV--QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDLE 125
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 221316642 126 RAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 164
Cdd:pfam13851 113 QRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-187 |
1.55e-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: 43.51 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 29 AENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEK----------FEVQHSEGYRQISALED 98
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelteLEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
....*....
gi 221316642 179 ELAVQQKQE 187
Cdd:TIGR02168 856 SLAAEIEEL 864
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
91-163 |
1.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221316642 91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
24-190 |
2.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRD-----LLSENNRLRMELETIKEKFEVQHSegyrQISALED 98
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELSARYTPNHP----DVIALRA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQTKA-IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIErnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG3206 299 QIAALRAqLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRL 374
|
170
....*....|...
gi 221316642 178 QELAVQQKQEKPR 190
Cdd:COG3206 375 EEARLAEALTVGN 387
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
19-188 |
3.20e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 19 KDLAMTYKQRAENTQEEL-REFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALE 97
Cdd:pfam15921 244 EDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 98 DDLAQtkaIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLR 177
Cdd:pfam15921 324 STVSQ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKRE 390
|
170
....*....|.
gi 221316642 178 QELAVQQKQEK 188
Cdd:pfam15921 391 KELSLEKEQNK 401
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
21-190 |
5.18e-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: 41.65 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 21 LAMTYKQRAENTQEELREFQ-EGSREYEAELE-TQLQQIETRNRDLLSENNRLRMELETIKeKFEVQHSEGYRQISALED 98
Cdd:pfam17380 342 MAMERERELERIRQEERKRElERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQTKAIKDQL-QKYIRELEQanddlERAKRATIMSLEDFEQRlnQAIERNAFLESELDEKENLLESVQRLKDEARDLR 177
Cdd:pfam17380 421 EMEQIRAEQEEArQREVRRLEE-----ERAREMERVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
|
170
....*....|...
gi 221316642 178 QELAVQQKQEKPR 190
Cdd:pfam17380 494 RKILEKELEERKQ 506
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
40-190 |
5.48e-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: 41.86 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 40 QEGSREYEAELETQLQQIETRNRDL-----LSENNRLRME-----LETIKEkfEVQHSEGYRQISALEDDLAQTKAIKDQ 109
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELeqklsVADAARRQFEkayelVCKIAG--EVERSQAWQTARELLRRYRSQQALAQR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 110 LQKYIRELEQANDDLERAKRATIMsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
.
gi 221316642 190 R 190
Cdd:COG3096 593 R 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-176 |
6.09e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221316642 107 KDQLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 176
Cdd:COG1196 762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1-188 |
7.00e-04 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 40.12 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREF--QEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI 78
Cdd:PRK14160 1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIekEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 79 KEKFE--VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 151
Cdd:PRK14160 81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221316642 152 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-189 |
8.03e-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: 41.20 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 49 ELETQLQQIETR--NRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLER 126
Cdd:TIGR02168 217 ELKAELRELELAllVLRLEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221316642 127 AkratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:TIGR02168 296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
26-174 |
9.07e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtrnrDLLSENNRLRMELETIK---EKFEVQHSEG--YRQISALEDDL 100
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEariKKYEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221316642 101 AQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 174
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
138-193 |
1.02e-03 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 39.56 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 221316642 138 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 193
Cdd:COG3166 43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-184 |
1.02e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 33 QEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKEKFEvqhsEGYRQISALEDDLAQTKAIKDQLQK 112
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 113 YIRELEQANDDLERAkratimsLEDFEQRLNQAI------------ERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02169 766 RIEELEEDLHKLEEA-------LNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
....
gi 221316642 181 AVQQ 184
Cdd:TIGR02169 839 QEQR 842
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
5-173 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 5 GKTFSSEEEEANYWKDLAMTYKQRAENTQ----EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKE 80
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKATESLEEQlaaaEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 81 kfevqhsegyrqISALEDDLAQTKAIKDQLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEKE 160
Cdd:COG5185 369 ------------EVELSKSSEELDSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQAT 433
|
170
....*....|...
gi 221316642 161 NLLESVQRLKDEA 173
Cdd:COG5185 434 SSNEEVSKLLNEL 446
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
12-180 |
1.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 12 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELEtQLQQIetrnRDLLSENNRLRMELETIKEKFEVQH----- 86
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERI----RTLLAAIADAEDEIERLREKREALAelnde 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 87 -----SEGYRQISALEDD-----LAQTKAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:PRK02224 625 rrerlAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALE 704
|
170 180
....*....|....*....|....*..
gi 221316642 154 SELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK02224 705 NRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-187 |
1.62e-03 |
|
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: 40.26 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 28 RAENTQEELrefqEGSREYEAELetqLQQIETRNRDLLSEnnrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIK 107
Cdd:pfam07888 28 RAELLQNRL----EECLQERAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 108 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEARdlrqELAVQQKQE 187
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK----KAGAQRKEE 169
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
142-204 |
1.68e-03 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 39.58 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221316642 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVEAERTDT 204
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
12-203 |
1.79e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 12 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYE---AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE 88
Cdd:TIGR04523 303 QKEQDWNKEL----KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 89 --GYR--------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAIERnafLESELDE 158
Cdd:TIGR04523 379 nqSYKqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----EIERLKETIIKNNSEIKD---LTNQDSV 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221316642 159 KENLLESVQRLKD-----------EARDLRQELAVQQKQEKPRTPMPSSVEAERTD 203
Cdd:TIGR04523 452 KELIIKNLDNTREsletqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
44-79 |
1.86e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 39.82 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|....*.
gi 221316642 44 REYEAELETQLQQIETRNRDLLSENNRLRMELETIK 79
Cdd:PRK03992 7 EERNSELEEQIRQLELKLRDLEAENEKLERELERLK 42
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-192 |
1.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEkFEVQHSEGYRQISALEDDLAQTKAIKDQLQKY 113
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 114 IReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------ELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK03918 296 IK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkELEKRLEELEERHELYEEAKAKKEEL 374
|
170
....*....|..
gi 221316642 181 AVQQKQEKPRTP 192
Cdd:PRK03918 375 ERLKKRLTGLTP 386
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-180 |
2.04e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 19 KDLAMTYKQRAEnTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALED 98
Cdd:TIGR02169 237 RQKEAIERQLAS-LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 99 DLAQTKAIKDQLQKYIRELEQANDDLERakratimSLEDFEQRLNQAIERNAFLESELDEKENLLESV----QRLKDEAR 174
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELK 388
|
....*.
gi 221316642 175 DLRQEL 180
Cdd:TIGR02169 389 DYREKL 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
54-252 |
2.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 54 LQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIM 133
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 134 SLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVP 213
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
|
170 180 190
....*....|....*....|....*....|....*....
gi 221316642 214 STPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARIS 252
Cdd:COG3883 284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-186 |
2.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 28 RAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLrmeLETIKEKFEVQHSEGYRQISALEDDLAQTKAIK 107
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARER----VEEAEAL---LEAGKCPECGQPVEGSPHVETIEEDRERVEELE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 108 DQLQKYIRELEQANDDLERAKratimSLEDFEQRLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQ 183
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEK 556
|
...
gi 221316642 184 QKQ 186
Cdd:PRK02224 557 REA 559
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
26-171 |
2.61e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSE--NNR----LRMELETIKekfevqhsegyRQISALEDD 99
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNvrNNKeyeaLQKEIESLK-----------RRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221316642 100 LAQTKAIKDQLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 171
Cdd:COG1579 112 ILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
48-234 |
2.87e-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: 38.94 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 48 AELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:pfam00529 61 DSAEAQLAKAQAQ-----------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 128 K-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprtpmPSSVEAERTD 203
Cdd:pfam00529 130 RvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ-------IAEAEAELKL 202
|
170 180 190
....*....|....*....|....*....|.
gi 221316642 204 TAVQATGSVPSTPIAHRGPSSSLNTPGSFRR 234
Cdd:pfam00529 203 AKLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
19-181 |
3.08e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.29 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 19 KDLAMTYKQRAEnTQEELREFQEGSREYEAE---LETQLQQIETRNrdlLSENnrlrmELETIKEKFEV-QHSEGYRQ-- 92
Cdd:COG0497 158 EEYREAYRAWRA-LKKELEELRADEAERAREldlLRFQLEELEAAA---LQPG-----EEEELEEERRRlSNAEKLREal 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 93 ---ISALEDD----LAQTKAIKDQLQKYIRELEQANDDLERAKRATImSLEDFEQRLNQAIERNAFLESELDEKENLLES 165
Cdd:COG0497 229 qeaLEALSGGeggaLDLLGQALRALERLAEYDPSLAELAERLESALI-ELEEAASELRRYLDSLEFDPERLEEVEERLAL 307
|
170 180
....*....|....*....|...
gi 221316642 166 VQRLK-------DEARDLRQELA 181
Cdd:COG0497 308 LRRLArkygvtvEELLAYAEELR 330
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
26-191 |
3.56e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.18 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEdDLAQTKA 105
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL-ELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 106 IKDQLQKYIRELEQANDDLERAKRATIMSLedfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESS---KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
....*.
gi 221316642 186 QEKPRT 191
Cdd:pfam02463 304 KLERRK 309
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
33-174 |
3.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 33 QEELREFQEGSREYEAELETQLQQIETrnrdLLSENNRLRMELETIKEKF-EVQHSEGYRQISALEDDLAQTKAIKDQLQ 111
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLqEEEDKLLEEAEKEAQQAIKEAKKEADEII 590
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221316642 112 KYIRELEQANDDLERAKRatimsLEDFEQRLNQAIERnafLESELDEKENLLESVQrLKDEAR 174
Cdd:PRK00409 591 KELRQLQKGGYASVKAHE-----LIEARKRLNKANEK---KEKKKKKQKEKQEELK-VGDEVK 644
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-186 |
4.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLN--QAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLAA 689
|
90
....*....|....*...
gi 221316642 169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4913 690 LEEQLEELEAELEELEEE 707
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
22-172 |
5.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 22 AMTYKQRAENTQEElrEFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI-KEKFEVQHSEgyRQISALEDDL 100
Cdd:PRK12704 51 AEAIKKEALLEAKE--EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKE--KELEQKQQEL 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221316642 101 AQTKA-IKDQLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESVQRLKDE 172
Cdd:PRK12704 127 EKKEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAIQRCAAD 204
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-198 |
5.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQEELR---EFQEGSREYEAELETQLQQI---ETRNRDLLSENNRLRMELETIKEKFEvQHSEGYRQISALEDD 99
Cdd:PRK03918 175 KRRIERLEKFIKrteNIEELIKEKEKELEEVLREIneiSSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 100 LAQTKAIKDQLQKYIRELEQANDDLE-RAKRatimsLEDFEQRLNQAIERNAFLESELDEKenllesvQRLKDEARDLRQ 178
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEeKVKE-----LKELKEKAEEYIKLSEFYEEYLDEL-------REIEKRLSRLEE 321
|
170 180
....*....|....*....|
gi 221316642 179 ELAVQQKQEKPRTPMPSSVE 198
Cdd:PRK03918 322 EINGIEERIKELEEKEERLE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-187 |
7.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfeVQHSEgyrQISALEDDLAQTKAIKDQLQKY 113
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELK---ELKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 114 IRELEQANDDLE---RAKRATIMSLEDFEQRLNQAIERNAFLE---SELDEKENLLESVQRLKDEARDLRQELAVQQKQE 187
Cdd:PRK03918 309 LREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
22-188 |
7.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 22 AMTYKQRAENTQEELREFQEgsREYEAEL---ETQLQQIETRNRDLLSEN--NRLRMELETIKEKFEVQHSEG--YRQ-I 93
Cdd:PRK04863 343 ALRQQEKIERYQADLEELEE--RLEEQNEvveEADEQQEENEARAEAAEEevDELKSQLADYQQALDVQQTRAiqYQQaV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 94 SALE--------DDLAQTKAIK--DQLQKYIRELEQANDDLERAKRATIMSLEDFEQ------RLNQAIERNAF------ 151
Cdd:PRK04863 421 QALErakqlcglPDLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrKIAGEVSRSEAwdvare 500
|
170 180 190
....*....|....*....|....*....|....*..
gi 221316642 152 LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK04863 501 LLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAER 537
|
|
| GrpE |
pfam01025 |
GrpE; |
47-127 |
7.52e-03 |
|
GrpE;
Pssm-ID: 425996 [Multi-domain] Cd Length: 165 Bit Score: 36.82 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 47 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyRQISaleddlaqtKAIKDQLQKYIRELEQANDDLER 126
Cdd:pfam01025 13 IESLEEEIEELEKKIEELKEKLLRALAEFENLRKRTE-------KEKE---------EAKKFAIEKFAKDLLPVIDNLER 76
|
.
gi 221316642 127 A 127
Cdd:pfam01025 77 A 77
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
26-174 |
7.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 26 KQRAENTQE-----ELREFQEGSREYEAELET------QLQQIETRNRDLLSENNRLRMELEtikEKFEVQHSEGYRQis 94
Cdd:PRK02224 579 SKLAELKERiesleRIRTLLAAIADAEDEIERlrekreALAELNDERRERLAEKRERKRELE---AEFDEARIEEARE-- 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 95 aledDLAQTKAIKDQLQKYIRELEQANDDLER---AKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKD 171
Cdd:PRK02224 654 ----DKERAEEYLEQVEEKLDELREERDDLQAeigAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRA 729
|
...
gi 221316642 172 EAR 174
Cdd:PRK02224 730 ELR 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
25-188 |
8.92e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.08 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 25 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRN---RDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDdla 101
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKELIIKNLDNTRESLE----TQLKVLSR--- 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316642 102 QTKAIKDQLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQ 178
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDF 552
|
170
....*....|....*..
gi 221316642 179 EL-------AVQQKQEK 188
Cdd:TIGR04523 553 ELkkenlekEIDEKNKE 569
|
|
| |
