|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-373 |
4.99e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 19 QSLQTRVLELQQQLAVAvaADRKKDTMIEQLDKTLArvvegwnrheaERTEVLRGLQEEHQAAELTRSKQQETVTRLEQS 98
Cdd:COG1196 216 RELKEELKELEAELLLL--KLRELEAELEELEAELE-----------ELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 99 LSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQ 178
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 179 QEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 258
Cdd:COG1196 363 AEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 259 IQLESELAVQLEQrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELR 338
Cdd:COG1196 442 EALEEAAEEEAEL---EEEEEALLELLAELLEEAALLEAALAEL----LEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350
....*....|....*....|....*....|....*.
gi 1213953301 339 LAREQARVC-ELQSGNQQLEEQRVELVERLQAMLQA 373
Cdd:COG1196 515 LLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-385 |
1.95e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 12 QHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEV---LRGLQEEHQAAELTRSKQ 88
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeeLAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 89 QETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAA 168
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 169 LEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMS 248
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 249 LVQARYESQRIQLESELAVQLEQRVTERLA--QAQESSLRQAASLREHHRKQLQDLSGQHQQELASQL----AQFKVEMA 322
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagrATFLPLDK 581
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213953301 323 EREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERlqAMLQAHWDEANQLLSTT 385
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR--TLVAARLEAALRRAVTL 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-381 |
4.22e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 40 RKKDTMiEQLDKT---LARVvegwnrhEAERTEV---LRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESA 113
Cdd:COG1196 173 RKEEAE-RKLEATeenLERL-------EDILGELerqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 114 RLQQRERETLEEerqaltlRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLkEHYQALQEE 193
Cdd:COG1196 245 EAELEELEAELE-------ELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 194 SQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRV 273
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 274 TERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVcELQSGN 353
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEA 472
|
330 340
....*....|....*....|....*...
gi 1213953301 354 QQLEEQRVELVERLQAMLQAHWDEANQL 381
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
128-413 |
1.62e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 128 QALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR 207
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 208 EAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQ 287
Cdd:COG1196 294 LAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 288 AASLREHHRKQLQDLSGQHQQELASQLAQfkvemaerEERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERL 367
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQ--------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1213953301 368 QAMLQAHWDEANQLLSTTLPPPNPPAPPAGPSSPGPQEPEKEERRV 413
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-302 |
3.57e-13 |
|
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: 73.17 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 13 HCERHIQSLQTRVLELQQQLAVAvaadRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETV 92
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAEL----RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 93 TRLEQSLSEAMEALNREQESARLQQRERETLEEERQ-------ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETL 165
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeelkALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 166 RAALEEERQTWAQQEHQLK------EHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRE 239
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953301 240 RDALQLEMSLVQARY---ESQRIQLESELAV--QLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 302
Cdd:TIGR02168 917 LEELREKLAQLELRLeglEVRIDNLQERLSEeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-372 |
2.78e-12 |
|
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: 70.47 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 98 SLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE--HRELETLRAALEEERQT 175
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 176 WAQQEHQLkehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYE 255
Cdd:TIGR02168 745 LEERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 256 SQRIQLESEL--AVQLEQRVTERLAQAQESSLRQAASlrEHHRKQLQDLSGQHQQELAS---QLAQFKVEMAEREERQQQ 330
Cdd:TIGR02168 821 NLRERLESLErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEAllnERASLEEALALLRSELEE 898
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1213953301 331 VAEdyELRLAREQARvcELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:TIGR02168 899 LSE--ELRELESKRS--ELRRELEELREKLAQLELRLEGLEV 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-373 |
3.78e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 142 CVLQEERDAARAGQLSEH-RELETLRAALEEERQtwaQQEH--QLKEHYQALQEesqAQLEREKEKSQREAQAAWETQHQ 218
Cdd:COG4913 216 YMLEEPDTFEAADALVEHfDDLERAHEALEDARE---QIELlePIRELAERYAA---ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 219 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQrvTERLAQAQESSLRQAASLREHHRKQ 298
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 299 LQDLSGQHQ------QELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:COG4913 368 LAALGLPLPasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
.
gi 1213953301 373 A 373
Cdd:COG4913 448 A 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-357 |
1.53e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 64 EAERTEVLRGLQEEHQAAELT------------RSKQQETVTRLEQSLSEAMEALNREQES---ARLQQRERETLEEERQ 128
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllvlrleelreeLEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 129 ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqRE 208
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL--EA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 209 AQAAWETQhqlalvqseVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVtERLAQAQESslrQA 288
Cdd:TIGR02168 366 ELEELESR---------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-----RLEDRR-ERLQQEIEE---LL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213953301 289 ASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE------DYELRLAREQARVCELQSGNQQLE 357
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaldAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
46-366 |
2.50e-09 |
|
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: 60.85 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 46 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEEH----------QAAELTRSKQQETVTRLE---QSLSEAMEALNREQES 112
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeiEQLEQEEEKLKERLEELEedlSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 113 --ARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlsEHRELETLRAALE---EERQTWAQQEHQLKEHY 187
Cdd:TIGR02169 763 leARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE----EVSRIEARLREIEqklNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 188 QALQEESQAQL-EREKEKSQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEsela 266
Cdd:TIGR02169 839 QEQRIDLKEQIkSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE---- 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 267 vQLEQRVTERLAQAQEsslrQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQV----AEDYElrlaRE 342
Cdd:TIGR02169 914 -KKRKRLSELKAKLEA----LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnmlaIQEYE----EV 984
|
330 340
....*....|....*....|....
gi 1213953301 343 QARVCELQSGNQQLEEQRVELVER 366
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILER 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-365 |
4.14e-09 |
|
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: 60.08 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 65 AERTEVLRgLQEEHQAAELTRSKQQETVTRLEQSLSEA---MEALNREQESARLQQRERETLEEERQALTLRLEAEQQRC 141
Cdd:TIGR02169 671 SEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 142 cvlQEERDAARAgqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqreaqaawetqhqlal 221
Cdd:TIGR02169 750 ---EQEIENVKS-------ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK----------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 222 VQSEVRRLEGELDTARRERDALQLEMSlvqarYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLRE--HHRKQL 299
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKE-----YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleELEAAL 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953301 300 QDLSGQHqQELASQLAQFKVEMAEREERQQQVAEDYEL---RLAREQARVCELQSGNQQLEEQRVELVE 365
Cdd:TIGR02169 878 RDLESRL-GDLKKERDELEAQLRELERKIEELEAQIEKkrkRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-373 |
1.01e-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: 58.91 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 148 RDAARAGQLSEHRELETLRAALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVR 227
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 228 RLEGELDTARRERDALQLEMSLVQAR---YESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLREHH---RKQLQD 301
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALdelRAELTL 814
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213953301 302 LSG-QHQQELASQLAQFKVEMAERE-ERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQA 373
Cdd:TIGR02168 815 LNEeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-367 |
1.44e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 127 RQALTLRLEAEQQRCCVLQEERDAARAgQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQ--AQLEREKEK 204
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDdlAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 205 SQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQRVTERLAQAQES 283
Cdd:COG4913 697 LEAELEEL---EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 284 SLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREE----RQQQVAED--------YELRLAREQARVCELQS 351
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylalLDRLEEDGlpeyeerfKELLNENSIEFVADLLS 853
|
250
....*....|....*.
gi 1213953301 352 gnqQLEEQRVELVERL 367
Cdd:COG4913 854 ---KLRRAIREIKERI 866
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
49-381 |
2.20e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 49 LDKTLARVVEGWNRHEAERTEVLRG---LQEEHQAAELTRSKQQETVTR--------------LEQSLSEAMEALNREQE 111
Cdd:PRK04863 263 ITESTNYVAADYMRHANERRVHLEEaleLRRELYTSRRQLAAEQYRLVEmarelaelneaesdLEQDYQAASDHLNLVQT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 112 sARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALE------EERQTWAQQEHQLKe 185
Cdd:PRK04863 343 -ALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqalDVQQTRAIQYQQAV- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 186 hyQALQEESQ-------------AQLEREKEKSQREAQAAWETQHQLALVQ----------SEVRRLEGELDTARRERDA 242
Cdd:PRK04863 421 --QALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayQLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 243 LQLEmslvqARYESQRIQleselAVQLEQRvterlaQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQlAQFKVEMA 322
Cdd:PRK04863 499 RELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQE 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953301 323 EREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHwDEANQL 381
Cdd:PRK04863 562 ELEARL----ESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ-DALARL 615
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
15-369 |
3.61e-08 |
|
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: 57.16 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 95 LEqslSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE-HRELETLRAALEEER 173
Cdd:pfam12128 327 LE---DQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 174 QTWAQQEHQLKEHYQALQEESQAQLEREK-----EKSQREAQAAW------------ETQHQLALVQSEVRRLEGELDTA 236
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELREQLEAGKlefneEEYRLKSRLGElklrlnqatatpELLLQLENFDERIERAREEQEAA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 237 RRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLREHHRKQLQDLSgQHQQELAS--QL 314
Cdd:pfam12128 484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRKEAPDWE-QSIGKVISpeLL 560
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1213953301 315 AQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 369
Cdd:pfam12128 561 HRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
47-267 |
5.37e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 47 EQLDkTLARVVEGWNRHEAERTEVlrglqeEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQesARLQQRERETLEEE 126
Cdd:COG4913 249 EQIE-LLEPIRELAERYAAARERL------AELEYLRAALRLWFAQRRLEL-LEAELEELRAEL--ARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 127 RQALTLRLEAEQQRccvlqEERDAARAGQLSehRELETLRAALEEERQTWAQQEHQLK----------EHYQALQEESQA 196
Cdd:COG4913 319 DALREELDELEAQI-----RGNGGDRLEQLE--REIERLERELEERERRRARLEALLAalglplpasaEEFAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213953301 197 QLEREKEKSQREAQAAWETqhqlalvQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAV 267
Cdd:COG4913 392 LLEALEEELEALEEALAEA-------EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGL 455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-381 |
8.12e-08 |
|
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: 55.84 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 131 TLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQ 210
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 211 aawETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAAS 290
Cdd:TIGR02169 748 ---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--IEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 291 LREHHRKQLQDLSgqhqQELASQLAQFKVEMAEREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVEL---VERL 367
Cdd:TIGR02169 823 RLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDEL 894
|
250
....*....|....
gi 1213953301 368 QAMLQAHWDEANQL 381
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
65-381 |
8.39e-08 |
|
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: 56.11 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 65 AERTEVLRGLQEEHQAAE------LTRSKQQETVTRLEQSLSEAMEALnREQESARLQQRERETleeerqaltlRLEAEQ 138
Cdd:COG3096 316 EELSARESDLEQDYQAASdhlnlvQTALRQQEKIERYQEDLEELTERL-EEQEEVVEEAAEQLA----------EAEARL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 139 QRCcvlQEERDAARAGQLSEHRELETL--RA--------ALEEERQTWAQQE---HQLKEHYQALQEESQAQLEREKEKS 205
Cdd:COG3096 385 EAA---EEEVDSLKSQLADYQQALDVQqtRAiqyqqavqALEKARALCGLPDltpENAEDYLAAFRAKEQQATEEVLELE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 206 QR--EAQAAwETQHQLALvqSEVRRLEGELDTARRERDALQLemslvQARYESQRIQLESELAVQLEQRVTERLAQAQES 283
Cdd:COG3096 462 QKlsVADAA-RRQFEKAY--ELVCKIAGEVERSQAWQTAREL-----LRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 284 SLRQAASLREHHRKQLQDlsgqhQQELASQLAQFKvemAEREERQQQVAEDYELRLAREQARvcelqsgnQQLEEQRVEL 363
Cdd:COG3096 534 AERLLEEFCQRIGQQLDA-----AEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQL--------EQLRARIKEL 597
|
330
....*....|....*...
gi 1213953301 364 VERLQAMLQAHwDEANQL 381
Cdd:COG3096 598 AARAPAWLAAQ-DALERL 614
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-369 |
1.05e-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: 54.77 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 150 AARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQREAQaawETQHQLALVQSEVRRL 229
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 230 EGELDTARRERDALQLEMS-LVQARYESQRIQ-----LESELAVQLEQRVT--ERLAQAQESSLRQAASLREHHRKQLQD 301
Cdd:COG4942 89 EKEIAELRAELEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 302 LSGQHQQ--ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 369
Cdd:COG4942 169 LEAERAEleALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-216 |
2.26e-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: 54.30 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 14 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLAR-------VVEGWNRHEAERTEVLRGLQEEHQAAELTRS 86
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 87 KQQETVTRLEQsLSEAMEALNREQEsaRLQQRERETLEEERQaLTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR 166
Cdd:TIGR02169 386 ELKDYREKLEK-LKREINELKRELD--RLQEELQRLSEELAD-LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1213953301 167 AALEEERqtwaQQEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQ 216
Cdd:TIGR02169 462 ADLSKYE----QELYDLKEEYDRVEKE-LSKLQRELAEAEAQARASEERV 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
77-370 |
3.53e-07 |
|
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: 53.59 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 77 EHQAAeLTRSKQQETVTRLEQS-LSEAMEALNREQESAR-LQQRERETLEEERQALTLRleAEQQRCcVLQEERDAARAG 154
Cdd:pfam17380 279 QHQKA-VSERQQQEKFEKMEQErLRQEKEEKAREVERRRkLEEAEKARQAEMDRQAAIY--AEQERM-AMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 155 QLSEHRELETLRA---ALEEERQ---TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRR 228
Cdd:pfam17380 355 QEERKRELERIRQeeiAMEISRMrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 229 LEGELDTARRERdalqlEMSLVQARyESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASlrEHHRKQLQDLSGQHQQ 308
Cdd:pfam17380 435 REVRRLEEERAR-----EMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE--EQRRKILEKELEERKQ 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213953301 309 ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVE---RLQAM 370
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEersRLEAM 571
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
65-383 |
4.64e-07 |
|
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: 53.42 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 65 AERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQreretleeerQALTlRLEaEQQRCCVL 144
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQ----------QAVQ-ALE-KARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 145 qEERDAARAGQlsehrELETLRAALEEERQTWAQQEHQL-------KEHYQALQ---------EESQA-QLEREKEKSQR 207
Cdd:COG3096 432 -PDLTPENAED-----YLAAFRAKEQQATEEVLELEQKLsvadaarRQFEKAYElvckiagevERSQAwQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 208 EAQAAWETQHQLALVQSEVRRLEGELDTARRerdaLQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQ 287
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQL--EELEEQAAEAVEQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 288 AASLReHHRKQLQDLSGQHQQ------ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRV 361
Cdd:COG3096 580 RSELR-QQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQ 654
|
330 340
....*....|....*....|..
gi 1213953301 362 ELVERLQAMLQAHWDEANQLLS 383
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLA 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-369 |
5.43e-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: 53.15 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 160 RELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQR--------EAQAAWETQHQLALVQSEVRRLEG 231
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLE-----RLRREREKAERyqallkekREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 232 ELDTARRERDALQLEMSLVQARYESQRIQLEsELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlQDLSGQHQQELA 311
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953301 312 SQLAQFKVEMaereERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 369
Cdd:TIGR02169 322 ERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
26-348 |
1.15e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 26 LELQQQLAVAVAADRKK-DTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAME 104
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSlHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 105 ALNREQEsARLQQRERETLEEERQALTLRLEAEQQRCCVLQ--------EERDAARAGQLSEHRELETLRAALEEERQTW 176
Cdd:TIGR00618 255 QLKKQQL-LKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 177 AQQEHQLKEHYQALQ----EESQAQLEREKEKSQRE--AQAAWETQHQLALvQSEVRRLEGELDTARRERDALQLEMSLV 250
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIREisCQQHTLTQHIHTL-QQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 251 QARYESQRIqLESELAV-----QLEQRVTERLAQAQESSLrQAASLREHHRKQLQdlsgQHQQELASQLAQFKVeMAERE 325
Cdd:TIGR00618 413 DTRTSAFRD-LQGQLAHakkqqELQQRYAELCAAAITCTA-QCEKLEKIHLQESA----QSLKEREQQLQTKEQ-IHLQE 485
|
330 340
....*....|....*....|...
gi 1213953301 326 ERQQQVAEDYELRLAREQARVCE 348
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCG 508
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
19-229 |
1.51e-06 |
|
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: 51.88 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 19 QSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKtLARVVEGWNRHEAERTEVLRGLQEEHQAaeltrskqqETVTRLEQS 98
Cdd:COG3096 451 QQATEEVLELEQKLSVADAARRQFEKAYELVCK-IAGEVERSQAWQTARELLRRYRSQQALA---------QRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 99 LSEAMEALNREQESARLQQRERETLEEERQA---LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQT 175
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEFCQRIGQQLDAaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953301 176 ---W----------AQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHqlalVQSEVRRL 229
Cdd:COG3096 601 apaWlaaqdalerlREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQA----LESQIERL 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-370 |
1.63e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV---VEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQET 91
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 92 VTRLEQSLSEAMEALNREQESARLQQRERETLEEERQ------------------------------ALTLRLEAEQQRC 141
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaalllaglrglagavavligveaayeaALEAALAAALQNI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 142 CVLQEERDAARAGQLSEHRE--LETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWE-TQHQ 218
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlVAAR 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 219 LALVQSEVRRLEGELDTARRERDALQL----------EMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEsslRQA 288
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEE---ERE 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 289 ASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREqarvcelqsgnQQLEEQRVELVERLQ 368
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL-----------EELERELERLEREIE 777
|
..
gi 1213953301 369 AM 370
Cdd:COG1196 778 AL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-281 |
1.75e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 101 EAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagQLSEHRELETLRAALEEERQTWAQQE 180
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 181 HQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQ 260
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|.
gi 1213953301 261 LESELAVQLEQRVTERLAQAQ 281
Cdd:COG4717 229 LEQLENELEAAALEERLKEAR 249
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
144-367 |
2.25e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 144 LQEERDAARAGQLSEHRELETLRAALEEERQTW--AQQEHQLKEHYQALQEESQAQL--EREKEKSQREAQAAWETQHQL 219
Cdd:PRK10929 32 LEQAKAAKTPAQAEIVEALQSALNWLEERKGSLerAKQYQQVIDNFPKLSAELRQQLnnERDEPRSVPPNMSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 220 ALVQSEV----RRLEGELDTARRERDALQLemsLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHH 295
Cdd:PRK10929 112 LQVSSQLleksRQAQQEQDRAREISDSLSQ---LPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213953301 296 RKQLQ--DLSGQHQQElasqLAQFKVEMAEReeRQQQVaeDYELRLAREQarvceLQSGNQQLEEQRVELVERL 367
Cdd:PRK10929 189 VDELElaQLSANNRQE----LARLRSELAKK--RSQQL--DAYLQALRNQ-----LNSQRQREAERALESTELL 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
40-360 |
2.43e-06 |
|
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: 50.99 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 40 RKKDTMIEQLDKTLARVVEGWN-RHEAERTEVLRGLQEEHQAAEltrskqqetvtRLEQSLSEAMEALNREQESARLQQR 118
Cdd:pfam12128 375 AKYNRRRSKIKEQNNRDIAGIKdKLAKIREARDRQLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 119 ERETLEEERQA-------LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR--------------AALEEERQTWA 177
Cdd:pfam12128 444 SRLGELKLRLNqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARkrrdqasealrqasRRLEERQSALD 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 178 QQEHQL------------------------------------------------------KEHYQALQEESQAQLEREKE 203
Cdd:pfam12128 524 ELELQLfpqagtllhflrkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 204 KSQREAQAAWETQHQLAlvqsevRRLEGELDTARRERDALQLEMSLVQARYESQRIQL------ESELAVQLEQRVTERL 277
Cdd:pfam12128 604 ERLDKAEEALQSAREKQ------AAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdeKQSEKDKKNKALAERK 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 278 AQAQEsSLRQAAslrehhrKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGN---- 353
Cdd:pfam12128 678 DSANE-RLNSLE-------AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAkael 749
|
....*..
gi 1213953301 354 QQLEEQR 360
Cdd:pfam12128 750 KALETWY 756
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-380 |
2.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 64 EAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQR----ERETLEEERQALTLRLEAEQQ 139
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 140 RCcvlQEERDAARAGQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQL 219
Cdd:PTZ00121 1547 KA---DELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 220 ALVQ--SEVRRLEGELDTARRE--RDALQL----EMSLVQARYESQRIQLESELAVQL-----EQRVTERLAQAQESSLR 286
Cdd:PTZ00121 1623 EELKkaEEEKKKVEQLKKKEAEekKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAkkaeeDEKKAAEALKKEAEEAK 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 287 QAASLRehhRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDyELRLAREQARvcELQSGNQQLEEQRVELVER 366
Cdd:PTZ00121 1703 KAEELK---KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKK--KIAHLKKEEEKKAEEIRKE 1776
|
330
....*....|....
gi 1213953301 367 LQAMLQAHWDEANQ 380
Cdd:PTZ00121 1777 KEAVIEEELDEEDE 1790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
88-327 |
3.70e-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: 49.76 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 88 QQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRA 167
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 168 ALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwetqHQLALVQSEVRRLEGELDTARRERDALQlem 247
Cdd:COG4942 98 ELEA-------QKEELAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 248 sLVQARYESQRIQLESELAVQLEQRVT-ERLAQAQESSLRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREE 326
Cdd:COG4942 164 -ALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
.
gi 1213953301 327 R 327
Cdd:COG4942 242 R 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
7-373 |
8.39e-06 |
|
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: 49.35 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 7 PHPFPQHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQldkTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRS 86
Cdd:pfam15921 69 AYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQ---SVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 87 KQQETVTRLE--QSLSEAMEAlNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELET 164
Cdd:pfam15921 146 QLQNTVHELEaaKCLKEDMLE-DSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 165 LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWeTQHQLalvqsEVRRLEGELDTARRERDALQ 244
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLI-SEHEV-----EITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 245 LEMSLVQARYESQRIQLESELAvQLEQRVTErlaqaQESSLRQAASLREHHRKQLQD---LSGQHQQELASQLAQFKVEM 321
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLS-DLESTVSQ-----LRSELREAKRMYEDKIEELEKqlvLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1213953301 322 AEREERQQQVAEDY-----ELRLAREQ-ARVCELQSGN--------QQLEEQRVElVERLQAMLQA 373
Cdd:pfam15921 373 GNLDDQLQKLLADLhkrekELSLEKEQnKRLWDRDTGNsitidhlrRELDDRNME-VQRLEALLKA 437
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-367 |
9.23e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 39 DRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLsEAMEALnrEQESARLQQR 118
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR-EELETL--EAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 119 ERETLEEErQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQaQL 198
Cdd:PRK02224 267 IAETERER-EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE-EA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 199 EREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLE-----SELAVQLEQRV 273
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 274 TERLAQAqESSLRQAASLREHHRKQL---------QDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQA 344
Cdd:PRK02224 425 REREAEL-EATLRTARERVEEAEALLeagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
330 340
....*....|....*....|...
gi 1213953301 345 RVcELQSGNQQLEEQRVELVERL 367
Cdd:PRK02224 504 LV-EAEDRIERLEERREDLEELI 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-381 |
9.52e-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: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 189 ALQEESQAQLEREKEKSQREAQAA----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR---YESQRIQL 261
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELekelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 262 ESELAvQLEQRVTERLAQAQESS--------LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE 333
Cdd:COG4942 96 RAELE-AQKEELAELLRALYRLGrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1213953301 334 DYELRLAREQARVCELqsgnQQLEEQRVELVERLQAMLQAHWDEANQL 381
Cdd:COG4942 175 ELEALLAELEEERAAL----EALKAERQKLLARLEKELAELAAELAEL 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
74-287 |
2.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 74 LQEEHQAAEltrsKQQETVTRLEQsLSEAMEALNREQESARLQQReretleeerQALTLRLEAEQQRCCVLQEERDAARA 153
Cdd:COG4913 237 LERAHEALE----DAREQIELLEP-IRELAERYAAARERLAELEY---------LRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 154 gqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLER-EKEKSQREAQAAwETQHQLALVQSEVRRLEGE 232
Cdd:COG4913 303 -------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELE-ERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1213953301 233 LDTARRERDALQLEMSLVQARYESQRIQLESELAvqlEQRVTERLAQAQESSLRQ 287
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEA 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-383 |
2.51e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 196 AQLEREKEKSQREAQAAWETQHQLALVQSEVR----RLEGELDTARRERDAL----QLEMSLVQARYES---QRIQLESE 264
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRqqleRLRREREKAERYQALLkekrEYEGYELLKEKEAlerQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 265 LAvQLEQRVTERLAQAQESSLR--QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMA-------EREERQQQVAE-- 333
Cdd:TIGR02169 246 LA-SLEEELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiaEKERELEDAEErl 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1213953301 334 -DYELRLAREQARVCELQsgnQQLEEQRVElVERLQAMLQAHWDEANQLLS 383
Cdd:TIGR02169 325 aKLEAEIDKLLAEIEELE---REIEEERKR-RDKLTEEYAELKEELEDLRA 371
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
195-380 |
2.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 195 QAQLEREKEKSqREAQAAWE---TQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAV---- 267
Cdd:COG3206 181 EEQLPELRKEL-EEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 268 ---QLEQRVTERLAQAQESSLRQAASLREHH------RKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEdyelR 338
Cdd:COG3206 260 lqsPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA----Q 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1213953301 339 LAREQARVCELQSGNQQLE--EQRVELVERLQAMLQAHWDEANQ 380
Cdd:COG3206 336 LAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEARL 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
75-366 |
2.70e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 75 QEEHQAAELTRSKQQETVTRLEQS---------------------------LSEAMEALNREQESARLQQRERETLEEER 127
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAeekaeaaekkkeeakkkadaakkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 128 QALTLRLEAEQQRCC-----VLQEERDAARAGQLSEH-RELETLRAALEEERQTwaqQEHQLKEHYQALQEESQAQLERE 201
Cdd:PTZ00121 1419 KADEAKKKAEEKKKAdeakkKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEA 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 202 KEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSlvQARYESQRIQLESELAVQLEQRVTERLAQAQ 281
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 282 E---SSLRQAASLREHHRKQLQDLSGQHQQElasqlAQFKVEMAEREERQQQVAEdyELRLAREQARVCELQSGNQQLEE 358
Cdd:PTZ00121 1574 EdknMALRKAEEAKKAEEARIEEVMKLYEEE-----KKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEK 1646
|
....*...
gi 1213953301 359 QRVELVER 366
Cdd:PTZ00121 1647 KKAEELKK 1654
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-379 |
3.16e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEgwnrHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 95 LEQSLSEAMEALNreqesarlqqreretleeerqALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQ 174
Cdd:PRK02224 389 LEEEIEELRERFG---------------------DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 175 TWAQ-------QEHQLKEHYQALQE--ESQAQLEREKEKSqREAQAAWETQHQLAlvqSEVRRLEGELDTARRERDALQL 245
Cdd:PRK02224 448 LLEAgkcpecgQPVEGSPHVETIEEdrERVEELEAELEDL-EEEVEEVEERLERA---EDLVEAEDRIERLEERREDLEE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 246 EMSLVQARYESQRIQLES--ELAVQLEQRVTERLAQAQEssLRQAAslrEHHRKQLQDLSGQhQQELASQLaqfkvEMAE 323
Cdd:PRK02224 524 LIAERRETIEEKRERAEElrERAAELEAEAEEKREAAAE--AEEEA---EEAREEVAELNSK-LAELKERI-----ESLE 592
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1213953301 324 REERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAmLQAHWDEAN 379
Cdd:PRK02224 593 RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE-LEAEFDEAR 647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
27-302 |
3.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 27 ELQQQLAVAVAADRKKdtmIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 106
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 107 NREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagqlsEHRELETLRAALEEERqtwaQQEHQLKEh 186
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEK----KAAEALKK- 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 187 yqalQEESQAQLEREKEKSQREAQAAWETQHqlalvQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELA 266
Cdd:PTZ00121 1697 ----EAEEAKKAEELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270
....*....|....*....|....*....|....*.
gi 1213953301 267 VQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 302
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
51-373 |
4.41e-05 |
|
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: 46.89 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 51 KTLARVVEGWNRHEAERTEVLRGLQ-EEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQA 129
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 130 LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREA 209
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 210 QAAwETQHQLALVQ-SEVRRLEGELDTARRERDALQLEMSLV--QARYESQRIQLESELAVQLEQRVTErlaqaqessLR 286
Cdd:pfam02463 336 EIE-ELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLakKKLESERLSSAAKLKEEELELKSEE---------EK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 287 QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVER 366
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
....*..
gi 1213953301 367 LQAMLQA 373
Cdd:pfam02463 486 LELLLSR 492
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
69-344 |
4.50e-05 |
|
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: 46.87 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 69 EVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALnreQESARLQqreretleeeRQALTLRLEAEQQRCCVLQEER 148
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL---QLLNKLL----------PQANLLADETLADRLEELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 149 DAARAGQ--LSEH----RELETLRAALeeerQTWAQQEHQLKEHYQAL---QEESQAQLEREKEKSQREAQAAWE-TQHQ 218
Cdd:COG3096 903 DAAQEAQafIQQHgkalAQLEPLVAVL----QSDPEQFEQLQADYLQAkeqQRRLKQQIFALSEVVQRRPHFSYEdAVGL 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 219 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES---QRIQLES------ELAVQLEQRVTERLAQAQESSLRQAA 289
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqVLASLKSsrdakqQTLQELEQELEELGVQADAEAEERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953301 290 SlrehHRKQLQDLSGQHQQ---ELASQLAQFKVEMAEREERQQQVAEDYelRLAREQA 344
Cdd:COG3096 1059 I----RRDELHEELSQNRSrrsQLEKQLTRCEAEMDSLQKRLRKAERDY--KQEREQV 1110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
213-381 |
4.79e-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: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 213 WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQ------RVTERLAQAQESS- 284
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASaereiaELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 285 -LRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREERQQQV---AEDYELRLAREQARVCELQSGNQQLEEQR 360
Cdd:COG4913 686 dLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELqdrLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|.
gi 1213953301 361 VELVERLQAMLQAHWDEANQL 381
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-254 |
5.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 45 MIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARlQQRERETLE 124
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELR-EELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 125 EERQALTLRLEAEQQRCCVLQEERDAARAgqlsEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEK 204
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1213953301 205 SQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARY 254
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
191-385 |
6.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 191 QEESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLE 270
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 271 QRVT----ERLAQAQESS--LRQAASLR---EHHRKQLQDlsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRLAR 341
Cdd:COG3883 98 SGGSvsylDVLLGSESFSdfLDRLSALSkiaDADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1213953301 342 EQARVCELQSGNQQLEEQRVELVERLQAMLQAHWDEANQLLSTT 385
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
19-229 |
8.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 19 QSLQTRVLELQQQLAVAVAADRKkdtmIEQLDKTLARVVEGWNRHEAERT--EVLRGLQEE-HQAAELTRSKQQetVTRL 95
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQ----FEQAYQLVRKIAGEVSRSEAWDVarELLRRLREQrHLAEQLQQLRMR--LSEL 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 96 EQSLSEAMEAlNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQT 175
Cdd:PRK04863 526 EQRLRQQQRA-ERLLAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953301 176 wAQQEHQLKEHYQALQEES--------------QAQLEREKEKSQREAQAAWETQHqlalVQSEVRRL 229
Cdd:PRK04863 602 -APAWLAAQDALARLREQSgeefedsqdvteymQQLLERERELTVERDELAARKQA----LDEEIERL 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-277 |
8.72e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARvvegwnrHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 95 LEQsLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDaaragqlsEHRELEtlrAALEEERQ 174
Cdd:PRK02224 581 LAE-LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE--------RKRELE---AEFDEARI 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 175 TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAawetqhqlalVQSEVRRLEgeldTARRERDALQLEMSLVQARY 254
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA----------VENELEELE----ELRERREALENRVEALEALY 714
|
250 260
....*....|....*....|....*.
gi 1213953301 255 ESQRiQLES---ELAVQLEQRVTERL 277
Cdd:PRK02224 715 DEAE-ELESmygDLRAELRQRNVETL 739
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
29-269 |
8.76e-05 |
|
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: 45.88 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 29 QQQLAVAVAADRKKDTMIEQLDKTLARVvegwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVtRLEQSLSEAMEALNR 108
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERV-----RQELEAARKVKILEEERQRKIQQQKVEMEQI-RAEQEEARQREVRRL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 109 EQESARLQQRERETLEEERQALT-LRLEAEQQRCCVLQ---EERDAARAGQLSE---HRELETLRAALEEERQTWAQQEH 181
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVErLRQQEEERKRKKLElekEKRDRKRAEEQRRkilEKELEERKQAMIEEERKRKLLEK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 182 QLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEgeldtarrerdALQLEMSLVQARYESQRIQL 261
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-----------AMEREREMMRQIVESEKARA 589
|
....*...
gi 1213953301 262 ESELAVQL 269
Cdd:pfam17380 590 EYEATTPI 597
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
16-371 |
9.25e-05 |
|
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: 46.12 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 16 RHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVV--------EGWNRHEAERTEVLRGLQEEHQAAELTRSK 87
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEiqelqekaESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 88 QQETVTRLEQSLSEAMEALNREQEsaRLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAA----RAGQLSEHRELE 163
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELK--LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAeereKTEKLKVEEEKE 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 164 TLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELdtarrerdaL 243
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI---------T 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 244 QLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlqdlSGQHQQELASQLAQFKVEmaE 323
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE-----IEERIKEEAEILLKYEEE--P 937
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1213953301 324 REERQQQVAEDYELRLAREQARVcelqsgNQQLEEQRVELVERLQAML 371
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEE------RNKRLLLAKEELGKVNLMA 979
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
19-369 |
1.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 19 QSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEvlrgLQEEHQAAELTRSKQQETVTRLEQS 98
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN----AEDFLEELREERDELREREAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 99 LSEAMEALNREQEsarlqqreretleeerqaltLRLEAEQQRCCvlQEERDAARAGQLSEHRE-LETLRAALEEERQTWA 177
Cdd:PRK02224 435 LRTARERVEEAEA--------------------LLEAGKCPECG--QPVEGSPHVETIEEDRErVEELEAELEDLEEEVE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 178 QQEHQLKEHYQALQEESQAQLEREKEK------SQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQ 251
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERREdleeliAERRETIE-EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 252 ---ARYESQRIQLESELAvQLEqRVTERLAQAQEssLRQAASLREHHRKQLQDLSGQHQQELAsqlaqfkvemaEREERQ 328
Cdd:PRK02224 572 eevAELNSKLAELKERIE-SLE-RIRTLLAAIAD--AEDEIERLREKREALAELNDERRERLA-----------EKRERK 636
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1213953301 329 QQVAEDYElrlareQARVCELQSGNQQLEEQRVELVERLQA 369
Cdd:PRK02224 637 RELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-258 |
1.43e-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: 44.75 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 27 ELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAErtevLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 106
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 107 NREQESARlQQRERETLEEERQALTLRLEAEQqrccVLQEERDAARAGQLSEHR--ELETLRAALEEERQTWAQQEHQLK 184
Cdd:COG4942 100 EAQKEELA-ELLRALYRLGRQPPLALLLSPED----FLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213953301 185 EHYQALQEESQAQLEREKEKSQREAqaawetqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 258
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
74-355 |
1.66e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 74 LQEEHQAAELTRSKQQE---------TVTRLEQSLSEAMEALNreqESARLQQRERETLEEERQALTLRLEAEQQRCCVL 144
Cdd:PRK10929 112 LQVSSQLLEKSRQAQQEqdrareisdSLSQLPQQQTEARRQLN---EIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 145 QEERDAAragQLSEH--RELETLRAALEEERQtwaqqeHQLKEHYQALQEESQAQlerekekSQREAQAAWETQHQLAlv 222
Cdd:PRK10929 189 VDELELA---QLSANnrQELARLRSELAKKRS------QQLDAYLQALRNQLNSQ-------RQREAERALESTELLA-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 223 qsevrrlEGELDTARRERDALQLEMSLVQA-RYESQRIQLeseLAVQleqrvtERLAQAQESSLRQAAS-LREHH----- 295
Cdd:PRK10929 251 -------EQSGDLPKSIVAQFKINRELSQAlNQQAQRMDL---IASQ------QRQAASQTLQVRQALNtLREQSqwlgv 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213953301 296 --------RKQLQDLSGQHQ-QELASQLAQFKV------EMAEREERQQQVAEDYELRLAREQARVCELQSGNQQ 355
Cdd:PRK10929 315 snalgealRAQVARLPEMPKpQQLDTEMAQLRVqrlryeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQR 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-333 |
1.72e-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: 45.06 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAvavaadrKKDTMIEQLDKTLARVVEgwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 95 LEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlsehrELETLRAALEEERq 174
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVD- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 175 twaqqehqlKEHYQALQEESQAQLEREKEKSQREaqaawETQHQLALVQSEVRRLEGELdtarrerdaLQLEMSLvqARY 254
Cdd:TIGR02169 378 ---------KEFAETRDELKDYREKLEKLKREIN-----ELKRELDRLQEELQRLSEEL---------ADLNAAI--AGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 255 ESQRIQLESEL-AVQLEQRvterlaqAQESSLRQAASLREHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAE 333
Cdd:TIGR02169 433 EAKINELEEEKeDKALEIK-------KQEWKLEQLAADLSKYEQELYDLK-EEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
15-371 |
1.89e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV--VEGWNRHEAERTEVLRGLQEEHQAAEltrSKQQETV 92
Cdd:PRK04863 382 EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEEL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 93 TRLEQSLSEAMEALNREQESARLQQreretleeerqaltlRLEAEQQRccvlQEERDAARagqlsehrelETLRAAleEE 172
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVR---------------KIAGEVSR----SEAWDVAR----------ELLRRL--RE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 173 RQTWAQQEHQLKEHYQALQEESQAQleREKEKSQREAQAAWETQHQLAlvqSEVRRLEGELDTarrERDALQLEMSLVQA 252
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDE---DELEQLQEELEA---RLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 253 RYESQRIQLEselavQLEQRVTERLAQAQESSLRQAASlrehhrKQLQDLSGQHqQELASQLAQFKVEMAEREERQQQVA 332
Cdd:PRK04863 580 RRMALRQQLE-----QLQARIQRLAARAPAWLAAQDAL------ARLREQSGEE-FEDSQDVTEYMQQLLERERELTVER 647
|
330 340 350
....*....|....*....|....*....|....*....
gi 1213953301 333 EDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAML 371
Cdd:PRK04863 648 DELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
158-382 |
1.93e-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: 44.94 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 158 EHRELETLRAALEEERQTWAQQEHQLKEHYQALQ----------EESQAQLEREKEksqREAQAAWETQHQLALVQSEVR 227
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanllaDETLADRLEELR---EELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 228 RLEGELDTARR---ERDALQLEMSLVQARYESQRIQLESelAVQLEQRVT--------ERLAQAQESS------LRQAAS 290
Cdd:COG3096 921 QLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFA--LSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 291 LREHHRKQLQDLSGQHQ---QELAS----------QLAQFKVEMAEREERQQQVAEdyelrlAREQARVCELQSGNQQLE 357
Cdd:COG3096 999 ARREAREQLRQAQAQYSqynQVLASlkssrdakqqTLQELEQELEELGVQADAEAE------ERARIRRDELHEELSQNR 1072
|
250 260
....*....|....*....|....*
gi 1213953301 358 EQRVELvERLQAMLQAHWDEANQLL 382
Cdd:COG3096 1073 SRRSQL-EKQLTRCEAEMDSLQKRL 1096
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-386 |
2.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 12 QHCERHIQSLQTRVLELQQQLAVA------VAADRKKDTMIEQLDKTLARVVEgWNRHEAERTEVLRGLQEEHQ----AA 81
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEeleeLL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 82 ELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRE 161
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 162 LETLRAALEEERQ---------TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQS-----EVR 227
Cdd:COG4717 264 LGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 228 RLEGELDTARRERDALQLEMSLvqARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAASLREHHRKQLQDLSGQHQ 307
Cdd:COG4717 344 DRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVEDEEELRAALEQAEE--YQELKEELEELEEQLEELLGELE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 308 Q--------ELASQLAQFKVEMAEREERQQQVAEdyelRLAREQARVCELQSGN--QQLEEQRVELVERLQAMLQAHwdE 377
Cdd:COG4717 420 EllealdeeELEEELEELEEELEELEEELEELRE----ELAELEAELEQLEEDGelAELLQELEELKAELRELAEEW--A 493
|
....*....
gi 1213953301 378 ANQLLSTTL 386
Cdd:COG4717 494 ALKLALELL 502
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
216-377 |
2.65e-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: 42.99 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 216 QHQLALVQSEVRRLEGELDTARRERDALQLEmsLVQARYESQRIQLESELAVQLEQRVTERLAQAqeSSLRQAASLR--- 292
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQkei 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 293 EHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:COG1579 99 ESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
....*
gi 1213953301 373 AHWDE 377
Cdd:COG1579 178 ALYER 182
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-253 |
2.67e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 21 LQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEhqaaeltrSKQQETVTRLEQSLS 100
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE--------RKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 101 EAMEALNREQESarlqqreretLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQE 180
Cdd:TIGR02169 364 EELEDLRAELEE----------VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213953301 181 HQLKEhYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR 253
Cdd:TIGR02169 434 AKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-298 |
3.78e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARvvegwnrhEAERTEVLRGLQEEH--QAAELTRS-----K 87
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--------EKKKAEELKKAEEENkiKAAEEAKKaeedkK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 88 QQETVTRLEQSLSEAMEALNREQESAR-LQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagqlsEHRELETLR 166
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAK 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 167 AAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVrRLEGELDTARRERDALQLE 246
Cdd:PTZ00121 1751 KD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN-IIEGGKEGNLVINDSKEME 1828
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1213953301 247 MSLVQARYESQRIQLESELAVQleQRVTERLAQAQESSLRQAASLREHHRKQ 298
Cdd:PTZ00121 1829 DSAIKEVADSKNMQLEEADAFE--KHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
15-370 |
3.81e-04 |
|
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: 44.01 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDtmiEQLDKTLARVVEgwnrHEAERTEVLRGLQE-EHQAAELTRSKQQETVT 93
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARLEE----ETAQKNNALKKIRElEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 94 R-----LEQSLSEAMEALNREQESarlqqreretleeerqalTLRLEAEQQRccvLQEERDaaragqlsehRELETLRAA 168
Cdd:pfam01576 287 RnkaekQRRDLGEELEALKTELED------------------TLDTTAAQQE---LRSKRE----------QEVTELKKA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 169 LEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMS 248
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 249 LVQARY---ESQRIQLESELA-VQLE-QRVTERLAQAQESSLRQAASLREHHrKQLQDLSGQHQQELASQLA---QFKVE 320
Cdd:pfam01576 416 ELQARLsesERQRAELAEKLSkLQSElESVSSLLNEAEGKNIKLSKDVSSLE-SQLQDTQELLQEETRQKLNlstRLRQL 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1213953301 321 MAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRVELVERLQAM 370
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVER----QLSTLQAQLSDMKKKLEEDAGTL 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-360 |
4.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 64 EAERTEVLRGLQEEHQAAELTR---SKQQETVTRLEQSLSEAMEALNREQ----------ESARL----QQRERETLEEE 126
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAEEernneeirkfEEARMahfaRRQAAIKAEEA 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 127 RQALTLRlEAEqqrccvlqEERDAARAGQLSEHRELETLRAALEEERQTwaqqehqlkehyqalqEESQAQLEREKEKSQ 206
Cdd:PTZ00121 1278 RKADELK-KAE--------EKKKADEAKKAEEKKKADEAKKKAEEAKKA----------------DEAKKKAEEAKKKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 207 REAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavqlEQRVTERLAQAQESSLR 286
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-------EKKKADEAKKKAEEDKK 1405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 287 QAASLR--EHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDY----ELRLAREQARVCElqSGNQQLEEQR 360
Cdd:PTZ00121 1406 KADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeEAKKKAEEAKKAD--EAKKKAEEAK 1483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-381 |
4.81e-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: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 192 EESQAQLEREKEKSQREAQaawetqhqLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLeSELAVQLEQ 271
Cdd:TIGR02168 667 KTNSSILERRREIEELEEK--------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 272 rvterlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVaEDYELRLAREQARVCELQS 351
Cdd:TIGR02168 738 ------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRA 810
|
170 180 190
....*....|....*....|....*....|
gi 1213953301 352 GNQQLEEQRVELVERLQAMLQAHWDEANQL 381
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRL 840
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
218-346 |
6.02e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 218 QLALVQSEVRRLEGELDTARRERDALQ-------------LEMSLVqARYESQRIQLESELAvQLEQRVTE---RLAQAQ 281
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFRnrngildpeataeALLQLI-ATLEGQLAELEAELA-ALRSYLSPnspQVRQLR 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953301 282 esslRQAASLREHHRKQLQDLSGQHQQE-LASQLAQFKVEMAEREERQQQvaedYELRLAR-EQARV 346
Cdd:COG3524 256 ----RRIAALEKQIAAERARLTGASGGDsLASLLAEYERLELEREFAEKA----YTSALAAlEQARI 314
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-372 |
6.67e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 22 QTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSE 101
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 102 AMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE---HRELETLraALEEERQTWAQ 178
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalHALQLTL--TQERVREHALS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 179 QEHQlkehyqalQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 258
Cdd:TIGR00618 667 IRVL--------PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 259 IQLESELAVQLEQRVTERLAQAQESSLR-QAASLREHHRKQLQDLSG--QHQQELASQLAQfkvEMAEREERQQQVAEDY 335
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEAHFNNnEEVTAALQTGAELSHLAAeiQFFNRLREEDTH---LLKTLEAEIGQEIPSD 815
|
330 340 350
....*....|....*....|....*....|....*...
gi 1213953301 336 EL-RLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:TIGR00618 816 EDiLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
15-212 |
6.74e-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: 42.44 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLArvvegwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------AQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 95 LEQSLsEAMEALNREQESarlQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQ 174
Cdd:COG4942 134 AVRRL-QYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 1213953301 175 TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAA 212
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
15-275 |
1.11e-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: 42.63 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQ-------LDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSK 87
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQlkeqlqlLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 88 QQETVTRLEQSLSeameALNREQES-ARLQQreretleeERQALTLRLEAEQQRCCVLQE--ERDAA-----RAGQLSEH 159
Cdd:COG3096 915 HGKALAQLEPLVA----VLQSDPEQfEQLQA--------DYLQAKEQQRRLKQQIFALSEvvQRRPHfsyedAVGLLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 160 REL-ETLRAALEEERQTWAQQEHQLKehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 238
Cdd:COG3096 983 SDLnEKLRARLEQAEEARREAREQLR---QAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1213953301 239 ERDALQLEMSLVQAR---YESQRIQLESELAvQLEQRVTE 275
Cdd:COG3096 1060 RRDELHEELSQNRSRrsqLEKQLTRCEAEMD-SLQKRLRK 1098
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
64-363 |
1.25e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 64 EAERTEVLRGLQ----EEHQAAELTRSKQQET--VTRLEqslsEAMEALNREQESARLQQRERETLEEERQALTLRLEAE 137
Cdd:PRK10246 215 PEQVQSLTASLQvltdEEKQLLTAQQQQQQSLnwLTRLD----ELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 138 QQRCCVL-QEERDAARAGQLSEHRELET-LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWET 215
Cdd:PRK10246 291 QLRPHWErIQEQSAALAHTRQQIEEVNTrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 216 Q-HQLALVQSEVRRLEGELDTARRERDAL-QLEMSLVqaryesqriqlESELAVQLEQRVTERLAQAQESSLRQAASLRE 293
Cdd:PRK10246 371 QfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLT-----------ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 294 HHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAedyelrlarEQARVCELQSGNQQLEEQRVEL 363
Cdd:PRK10246 440 KRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLA---------DVKTICEQEARIKDLEAQRAQL 500
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
206-373 |
1.30e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 41.89 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 206 QREAQAAWetQHQLALVQSEVR-RLEGELDTARRER---DALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAq 281
Cdd:pfam04632 158 RARLRARL--RDALRLAAAALAgAPGAEAFEAARLRlaaDILALEALRSHAAFESPRGRARARALRRLLARMLALLPRL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 282 eSSLRQaaslrehHRKQLQDLSGQHQQELASQLAqfkvEMAEREERQQqvAEDYELRLAREQARVCELQSGNQQLEEQRV 361
Cdd:pfam04632 235 -RSLAR-------LLARLRTEGAGTVPELAALLD----ELAAWEAALA--AEALQAALAALRARLRALRPALPLDFDTAA 300
|
170
....*....|..
gi 1213953301 362 ELVERLQAMLQA 373
Cdd:pfam04632 301 ELLARLADLLAE 312
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
90-380 |
1.32e-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: 42.25 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 90 ETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHR--ELETLRA 167
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH---LNLVQTALRQQEKIERYqeDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 168 ALEEERQTWAQQEHQLKEHYQALQeesQAQLEREKEKSQ-REAQAAWETQHQLAL-VQSEVRRLEgeldTARRERDALQL 245
Cdd:COG3096 362 RLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSLKSQlADYQQALDVQQTRAIqYQQAVQALE----KARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 246 EMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASL---------REHHRKQLQDLSGQH--QQELASQL 314
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELvckiageveRSQAWQTARELLRRYrsQQALAQRL 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953301 315 AQFKVEMAE---REERQQQV---AEDYELRLAREQARVCELQSGNQQLEEQRVELVERL------QAMLQAHWDEANQ 380
Cdd:COG3096 515 QQLRAQLAEleqRLRQQQNAerlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqRSELRQQLEQLRA 592
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-513 |
1.36e-03 |
|
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: 42.03 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 21 LQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVvegwnrheAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLS 100
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL--------ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 101 EAMEALnrEQESARLQQRERETLEEERQALTLRLEAEQQRCcvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQE 180
Cdd:pfam15921 507 EKERAI--EATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 181 HQLKehyqALQEEsQAQLEREKEKSQREAQaawetqhqlalvqsEVRRLEGELDTARRERDA----LQLE-MSLVQAryE 255
Cdd:pfam15921 583 RTAG----AMQVE-KAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEArvsdLELEkVKLVNA--G 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 256 SQRIQLESELAVQLEQRVTErlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQ------ 329
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNE--VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlksme 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 330 -------QVAEDYELRLAREQARVCELQSGNQQLEEQRVElVERLQAMLQAHWDEANQLLSTTlpPPNPPAPPAGPSSPG 402
Cdd:pfam15921 720 gsdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN-ANKEKHFLKEEKNKLSQELSTV--ATEKNKMAGELEVLR 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 403 PQEPEKEERrvwtMPPMAVALKPVLQQSREARD----ELPGAPPVLCSSSSDLSLLLGPSFQSQHSFQPLEPKP---DLT 475
Cdd:pfam15921 797 SQERRLKEK----VANMEVALDKASLQFAECQDiiqrQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPasfTRT 872
|
490 500 510
....*....|....*....|....*....|....*...
gi 1213953301 476 SSTAGAFSALGAFHPDHRAERPFPEEDPGPDGEGLLKQ 513
Cdd:pfam15921 873 HSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQE 910
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
15-328 |
1.62e-03 |
|
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: 42.13 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 15 ERHIQSLQTRVLELQQQLAVAVAADRKKD-------TMIEQLDKTLARVVegwNRHEAERTEVLRGLQEEHQAAELTRSK 87
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASreetfarTALKNARLDLRRLF---DEKQSEKDKKNKALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 88 QQETVTRLEQSLSEAMEALNREQESARLQQRERETL---------EEERQALTLRLEAEQQRCCVLQEERDAARAGQ--- 155
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVvegaldaqlALLKAAIAARRSGAKAELKALETWYKRDLASLgvd 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 156 ----LSEHRELETLRAALEEErqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEG 231
Cdd:pfam12128 767 pdviAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRA 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 232 ELDTARRERDALQLEMS--LVQARYESQRIQL--ESELAVQLEQRVTERLAQAQEsSLRQAASLREHHRKQLQDLSGQHQ 307
Cdd:pfam12128 843 KLEMERKASEKQQVRLSenLRGLRCEMSKLATlkEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHFKNVIA 921
|
330 340
....*....|....*....|.
gi 1213953301 308 QELASQLAQFKVEMAEREERQ 328
Cdd:pfam12128 922 DHSGSGLAETWESLREEDHYQ 942
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
144-281 |
1.78e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 144 LQEERDAARAGQLSEHRELETLRAALEEerqtwaqqehqLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 223
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953301 224 SEVRRLEGELdtaRRERDALQLEMSLVQARYESQRIQL---------ESELAVQLEQrVTERLAQAQ 281
Cdd:pfam09787 121 EELRYLEEEL---RRSKATLQSRIKDREAEIEKLRNQLtsksqssssQSELENRLHQ-LTETLIQKQ 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
56-212 |
1.91e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 56 VVEGWNRHE-----AERTEVLRGLQEEHQAAELtRSKQQETVTRLEQslseamealnREQESARLQQRERETLEEERQAL 130
Cdd:PRK09510 60 VVEQYNRQQqqqksAKRAEEQRKKKEQQQAEEL-QQKQAAEQERLKQ----------LEKERLAAQEQKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 131 TLRLEAEQQRccvlQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQA---LQEESQAQLERE-KEKSQ 206
Cdd:PRK09510 129 LKQKQAEEAA----AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAkkkAEAEAAAKAAAEaKKKAE 204
|
....*.
gi 1213953301 207 REAQAA 212
Cdd:PRK09510 205 AEAKKK 210
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
160-384 |
3.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 160 RELETLRAALEEERQT--WAQQEHQLKEHYQALQEESQAQLEREKEKSQREA-------------QAAWETQHQLALVQS 224
Cdd:TIGR00618 226 KELKHLREALQQTQQShaYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqerinrarKAAPLAAHIKAVTQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 225 EVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLR-----QAASLREHHRKQL 299
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreiscQQHTLTQHIHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 300 QDLSGQHQQE--LASQLAQFKVEMA--------EREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQrveLVERLQA 369
Cdd:TIGR00618 386 QQKTTLTQKLqsLCKELDILQREQAtidtrtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQ 462
|
250
....*....|....*
gi 1213953301 370 MLQAHWDEANQLLST 384
Cdd:TIGR00618 463 ESAQSLKEREQQLQT 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-220 |
3.93e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 14 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVT 93
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 94 RLEQ------SLSEAMEALNREQESARLQ----QRERETLEEERQALTLRL-EAEQQRCCVLQEERDAARAGQLSEHREL 162
Cdd:TIGR02168 380 QLETlrskvaQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 163 ETLRAALEEERQTWAQQEHQLKEHYQALQE--ESQAQLEREKEKSQREAQAAWETQHQLA 220
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-302 |
4.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 18 IQSLQTRVLELQQQLAVA----VAADRKKDTMIEQLD--KTLARVVEGWNRHEAERTEvLRGLQEEHQAAELTRS---KQ 88
Cdd:COG4913 612 LAALEAELAELEEELAEAeerlEALEAELDALQERREalQRLAEYSWDEIDVASAERE-IAELEAELERLDASSDdlaAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 89 QETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAA 168
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 169 LEEERQTWAQQEHQL-----------KEHYQALQEESQAQLER-----------------EKEKSQREAQAAWETQHQLA 220
Cdd:COG4913 771 LEERIDALRARLNRAeeeleramrafNREWPAETADLDADLESlpeylalldrleedglpEYEERFKELLNENSIEFVAD 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 221 LVQsevrRLEGELDTARRERDalQLEMSLVQARYESQR-IQLE-SELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQ 298
Cdd:COG4913 851 LLS----KLRRAIREIKERID--PLNDSLKRIPFGPGRyLRLEaRPRPDPEVREFRQELRAVTSGASLFDEELSEARFAA 924
|
....
gi 1213953301 299 LQDL 302
Cdd:COG4913 925 LKRL 928
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
10-384 |
4.96e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.12 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 10 FPQHCERHIQSLQTRVLELQQQLAvavAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSkqq 89
Cdd:pfam07111 300 FPKKCRSLLNRWREKVFALMVQLK---AQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERM--- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 90 eTVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCcvlqeERDAARAGQLSEH-----RELET 164
Cdd:pfam07111 374 -SAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV-----EQAVARIPSLSNRlsyavRKVHT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 165 LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVRRL--EGELDTARRERDA 242
Cdd:pfam07111 448 IKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA-ELQLSAHLIQQEVGRAreQGEAERQQLSEVA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 243 LQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQaaslREHHRKQLQDLSGQHQQELASQLAQFKVEMA 322
Cdd:pfam07111 527 QQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQ----QEIYGQALQEKVAEVETRLREQLSDTKRRLN 602
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1213953301 323 EREERQQQVAedyeLRLAREQARVCELQSGNQQL----EEQRVELVERLQAMLQAHWDEANQLLST 384
Cdd:pfam07111 603 EARREQAKAV----VSLRQIQHRATQEKERNQELrrlqDEARKEEGQRLARRVQELERDKNLMLAT 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
144-316 |
5.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 144 LQEERDAARAgQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQA--------QLEREKEKSQREAQAAWET 215
Cdd:COG4717 76 LEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqeleALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953301 216 QHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvTERLAQAQESslrqaaslREHH 295
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL-EEELEEAQEE--------LEEL 225
|
170 180
....*....|....*....|..
gi 1213953301 296 RKQLQDLSGQHQ-QELASQLAQ 316
Cdd:COG4717 226 EEELEQLENELEaAALEERLKE 247
|
|
| |
