|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-373 |
1.80e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 19 QSLQTRVLELQQQLAVAvaADRKKDTMIEQLDKTLArvvegwnrheaERTEVLRGLQEEHQAAELTRSKQQETVTRLEQS 98
Cdd:COG1196 216 RELKEELKELEAELLLL--KLRELEAELEELEAELE-----------ELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 99 LSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQ 178
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 179 QEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 258
Cdd:COG1196 363 AEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 259 IQLESELAVQLEQrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELR 338
Cdd:COG1196 442 EALEEAAEEEAEL---EEEEEALLELLAELLEEAALLEAALAEL----LEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034598051 339 LAREQARVC-ELQSGNQQLEEQRVELVERLQAMLQA 373
Cdd:COG1196 515 LLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-385 |
1.01e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 12 QHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEV---LRGLQEEHQAAELTRSKQ 88
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeeLAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 89 QETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAA 168
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 169 LEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMS 248
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 249 LVQARYESQRIQLESELAVQLEQRVTERLA--QAQESSLRQAASLREHHRKQLQDLSGQHQQELASQL----AQFKVEMA 322
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagrATFLPLDK 581
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034598051 323 EREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERlqAMLQAHWDEANQLLSTT 385
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR--TLVAARLEAALRRAVTL 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-381 |
1.94e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 40 RKKDTMiEQLDKT---LARVvegwnrhEAERTEV---LRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESA 113
Cdd:COG1196 173 RKEEAE-RKLEATeenLERL-------EDILGELerqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 114 RLQQRERETLEEerqaltlRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLkEHYQALQEE 193
Cdd:COG1196 245 EAELEELEAELE-------ELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 194 SQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRV 273
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 274 TERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVcELQSGN 353
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEA 472
|
330 340
....*....|....*....|....*...
gi 1034598051 354 QQLEEQRVELVERLQAMLQAHWDEANQL 381
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
128-413 |
9.76e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 128 QALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR 207
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 208 EAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQ 287
Cdd:COG1196 294 LAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 288 AASLREHHRKQLQDLSGQHQQELASQLAQfkvemaerEERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERL 367
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQ--------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034598051 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 |
1.87e-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: 74.32 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 13 HCERHIQSLQTRVLELQQQLAVAvaadRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETV 92
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAEL----RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 93 TRLEQSLSEAMEALNREQESARLQQRERETLEEE-------RQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETL 165
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeeLKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 166 RAALEEERQTWAQQEHQLK------EHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRE 239
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598051 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 |
1.43e-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: 71.63 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 98 SLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE--HRELETLRAALEEERQT 175
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 176 WAQQEHQLkehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYE 255
Cdd:TIGR02168 745 LEERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 256 SQRIQLESEL--AVQLEQRVTERLAQAQESSLRQAASlrEHHRKQLQDLSGQHQQELAS---QLAQFKVEMAEREERQQQ 330
Cdd:TIGR02168 821 NLRERLESLErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEAllnERASLEEALALLRSELEE 898
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034598051 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 |
1.99e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 142 CVLQEERDAARAGQLSEH-RELETLRAALEEERQtwaQQEH--QLKEHYQALQEesqAQLEREKEKSQREAQAAWETQHQ 218
Cdd:COG4913 216 YMLEEPDTFEAADALVEHfDDLERAHEALEDARE---QIELlePIRELAERYAA---ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 219 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQrvTERLAQAQESSLRQAASLREHHRKQ 298
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 299 LQDLSGQHQ------QELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:COG4913 368 LAALGLPLPasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
.
gi 1034598051 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 |
7.49e-11 |
|
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: 65.85 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 64 EAERTEVLRGLQEEHQAAELT------------RSKQQETVTRLEQSLSEAMEALNREQES---ARLQQRERETLEEERQ 128
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllvlrleelreeLEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 129 ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqRE 208
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL--EA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 209 AQAAWETQhqlalvqseVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVtERLAQAQESslrQA 288
Cdd:TIGR02168 366 ELEELESR---------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-----RLEDRR-ERLQQEIEE---LL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034598051 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 |
1.37e-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: 61.62 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 46 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEEH----------QAAELTRSKQQETVTRLE---QSLSEAMEALNREQES 112
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeiEQLEQEEEKLKERLEELEedlSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 113 --ARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlsEHRELETLRAALE---EERQTWAQQEHQLKEHY 187
Cdd:TIGR02169 763 leARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE----EVSRIEARLREIEqklNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 188 QALQEESQAQL-EREKEKSQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEsela 266
Cdd:TIGR02169 839 QEQRIDLKEQIkSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE---- 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 267 vQLEQRVTERLAQAQEsslrQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQV----AEDYElrlaRE 342
Cdd:TIGR02169 914 -KKRKRLSELKAKLEA----LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnmlaIQEYE----EV 984
|
330 340
....*....|....*....|....
gi 1034598051 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 |
2.76e-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: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 65 AERTEVLRgLQEEHQAAELTRSKQQETVTRLEQSLSEA---MEALNREQESARLQQRERETLEEERQALTLRLEAEQQRC 141
Cdd:TIGR02169 671 SEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 142 cvlQEERDAARAgqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqreaqaawetqhqlal 221
Cdd:TIGR02169 750 ---EQEIENVKS-------ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK----------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 222 VQSEVRRLEGELDTARRERDALQLEMSlvqarYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLRE--HHRKQL 299
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKE-----YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleELEAAL 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034598051 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 |
4.85e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 148 RDAARAGQLSEHRELETLRAALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVR 227
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 228 RLEGELDTARRERDALQLEMSLVQAR---YESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLREHH---RKQLQD 301
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALdelRAELTL 814
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034598051 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 |
7.56e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 127 RQALTLRLEAEQQRCCVLQEERDAARAgQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQ--AQLEREKEK 204
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDdlAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 205 SQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQRVTERLAQAQES 283
Cdd:COG4913 697 LEAELEEL---EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 284 SLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREE----RQQQVAED--------YELRLAREQARVCELQS 351
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylalLDRLEEDGlpeyeerfKELLNENSIEFVADLLS 853
|
250
....*....|....*.
gi 1034598051 352 gnqQLEEQRVELVERL 367
Cdd:COG4913 854 ---KLRRAIREIKERI 866
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
49-381 |
7.82e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 49 LDKTLARVVEGWNRHEAERTEVLRG---LQEEHQAAELTRSKQQETVTR--------------LEQSLSEAMEALNREQE 111
Cdd:PRK04863 263 ITESTNYVAADYMRHANERRVHLEEaleLRRELYTSRRQLAAEQYRLVEmarelaelneaesdLEQDYQAASDHLNLVQT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 112 sARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALE------EERQTWAQQEHQLKe 185
Cdd:PRK04863 343 -ALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqalDVQQTRAIQYQQAV- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 186 hyQALQEESQ-------------AQLEREKEKSQREAQAAWETQHQLALVQ----------SEVRRLEGELDTARRERDA 242
Cdd:PRK04863 421 --QALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayQLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 243 LQLEmslvqARYESQRIQleselAVQLEQRvterlaQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQlAQFKVEMA 322
Cdd:PRK04863 499 RELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQE 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034598051 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 |
2.04e-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: 57.93 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 95 LEqslSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEH-RELETLRAALEEER 173
Cdd:pfam12128 327 LE---DQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 174 QTWAQQEHQLKEHYQALQEESQAQLEREK-----EKSQREAQAAW------------ETQHQLALVQSEVRRLEGELDTA 236
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELREQLEAGKlefneEEYRLKSRLGElklrlnqatatpELLLQLENFDERIERAREEQEAA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 237 RRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLREHHRKQLQDLSgQHQQELAS--QL 314
Cdd:pfam12128 484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRKEAPDWE-QSIGKVISpeLL 560
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034598051 315 AQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 369
Cdd:pfam12128 561 HRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
65-381 |
3.21e-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: 57.27 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 65 AERTEVLRGLQEEHQAAE------LTRSKQQETVTRLEQSLSEAMEALnREQESARLQQRERETleeerqaltlRLEAEQ 138
Cdd:COG3096 316 EELSARESDLEQDYQAASdhlnlvQTALRQQEKIERYQEDLEELTERL-EEQEEVVEEAAEQLA----------EAEARL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 139 QRCcvlQEERDAARAGQLSEHRELETL--RA--------ALEEERQTWAQQE---HQLKEHYQALQEESQAQLEREKEKS 205
Cdd:COG3096 385 EAA---EEEVDSLKSQLADYQQALDVQqtRAiqyqqavqALEKARALCGLPDltpENAEDYLAAFRAKEQQATEEVLELE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 206 QR--EAQAAwETQHQLALvqSEVRRLEGELDTARRERDALQLemslvQARYESQRIQLESELAVQLEQRVTERLAQAQES 283
Cdd:COG3096 462 QKlsVADAA-RRQFEKAY--ELVCKIAGEVERSQAWQTAREL-----LRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 284 SLRQAASLREHHRKQLQDlsgqhQQELASQLAQFKvemAEREERQQQVAEDYELRLAREQARvcelqsgnQQLEEQRVEL 363
Cdd:COG3096 534 AERLLEEFCQRIGQQLDA-----AEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQL--------EQLRARIKEL 597
|
330
....*....|....*...
gi 1034598051 364 VERLQAMLQAHwDEANQL 381
Cdd:COG3096 598 AARAPAWLAAQ-DALERL 614
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
47-267 |
3.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 47 EQLDkTLARVVEGWNRHEAERTEVlrglqeEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQesARLQQRERETLEEE 126
Cdd:COG4913 249 EQIE-LLEPIRELAERYAAARERL------AELEYLRAALRLWFAQRRLEL-LEAELEELRAEL--ARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 127 RQALTLRLEAEQQRccvlqEERDAARAGQLSehRELETLRAALEEERQTWAQQEHQLK----------EHYQALQEESQA 196
Cdd:COG4913 319 DALREELDELEAQI-----RGNGGDRLEQLE--REIERLERELEERERRRARLEALLAalglplpasaEEFAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034598051 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 |
4.83e-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: 56.61 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 131 TLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQ 210
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 211 aawETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAAS 290
Cdd:TIGR02169 748 ---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--IEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 291 LREHHRKQLQDLSgqhqQELASQLAQFKVEMAEREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVEL---VERL 367
Cdd:TIGR02169 823 RLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDEL 894
|
250
....*....|....
gi 1034598051 368 QAMLQAHWDEANQL 381
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-369 |
5.12e-08 |
|
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: 55.54 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 150 AARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQREAQaawETQHQLALVQSEVRRL 229
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 230 EGELDTARRERDALQLEMS-LVQARYESQRIQ-----LESELAVQLEQRVT--ERLAQAQESSLRQAASLREHHRKQLQD 301
Cdd:COG4942 89 EKEIAELRAELEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 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 |
1.54e-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: 55.07 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 14 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLAR-------VVEGWNRHEAERTEVLRGLQEEHQAAELTRS 86
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 87 KQQETVTRLEQsLSEAMEALNREQEsaRLQQRERETLEEERQaLTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR 166
Cdd:TIGR02169 386 ELKDYREKLEK-LKREINELKRELD--RLQEELQRLSEELAD-LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034598051 167 AALEEERqtwaQQEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQ 216
Cdd:TIGR02169 462 ADLSKYE----QELYDLKEEYDRVEKE-LSKLQRELAEAEAQARASEERV 506
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
65-383 |
1.63e-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: 54.96 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 65 AERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQreretleeerQALTlRLEaEQQRCCVL 144
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQ----------QAVQ-ALE-KARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 145 qEERDAARAGQlsehrELETLRAALEEERQTWAQQEHQL-------KEHYQALQ---------EESQA-QLEREKEKSQR 207
Cdd:COG3096 432 -PDLTPENAED-----YLAAFRAKEQQATEEVLELEQKLsvadaarRQFEKAYElvckiagevERSQAwQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 208 EAQAAWETQHQLALVQSEVRRLEGELDTARRerdaLQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQ 287
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQL--EELEEQAAEAVEQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 288 AASLReHHRKQLQDLSGQHQQ------ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRV 361
Cdd:COG3096 580 RSELR-QQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQ 654
|
330 340
....*....|....*....|..
gi 1034598051 362 ELVERLQAMLQAHWDEANQLLS 383
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLA 676
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
77-370 |
1.69e-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: 54.74 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 77 EHQAAeLTRSKQQETVTRLEQS-LSEAMEALNREQESAR-LQQRERETLEEERQALTLRleAEQQRCcVLQEERDAARAG 154
Cdd:pfam17380 279 QHQKA-VSERQQQEKFEKMEQErLRQEKEEKAREVERRRkLEEAEKARQAEMDRQAAIY--AEQERM-AMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 155 QLSEHRELETLRA---ALEEERQ---TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRR 228
Cdd:pfam17380 355 QEERKRELERIRQeeiAMEISRMrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 229 LEGELDTARRERdalqlEMSLVQARyESQRIQLESELAVQLEQRVTERLAQAQESSLRQAAslREHHRKQLQDLSGQHQQ 308
Cdd:pfam17380 435 REVRRLEEERAR-----EMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA--EEQRRKILEKELEERKQ 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034598051 309 ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVE---RLQAM 370
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEersRLEAM 571
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
26-348 |
3.01e-07 |
|
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: 54.20 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 26 LELQQQLAVAVAADRKK-DTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAME 104
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSlHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 105 ALNREQEsARLQQRERETLEEERQALTLRLEAEQQRCCVLQ--------EERDAARAGQLSEHRELETLRAALEEERQTW 176
Cdd:TIGR00618 255 QLKKQQL-LKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 177 AQQEHQLKEHYQALQ----EESQAQLEREKEKSQRE--AQAAWETQHQLALvQSEVRRLEGELDTARRERDALQLEMSLV 250
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIREisCQQHTLTQHIHTL-QQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 251 QARYESQRIqLESELAV-----QLEQRVTERLAQAQESSLrQAASLREHHRKQLQdlsgQHQQELASQLAQFKVeMAERE 325
Cdd:TIGR00618 413 DTRTSAFRD-LQGQLAHakkqqELQQRYAELCAAAITCTA-QCEKLEKIHLQESA----QSLKEREQQLQTKEQ-IHLQE 485
|
330 340
....*....|....*....|...
gi 1034598051 326 ERQQQVAEDYELRLAREQARVCE 348
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCG 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-369 |
3.73e-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: 53.92 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 160 RELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQR--------EAQAAWETQHQLALVQSEVRRLEG 231
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLE-----RLRREREKAERyqallkekREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 232 ELDTARRERDALQLEMSLVQARYESQRIQLEsELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlQDLSGQHQQELA 311
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598051 312 SQLAQFKVEMaereERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 369
Cdd:TIGR02169 322 ERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-370 |
7.43e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV---VEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQET 91
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 92 VTRLEQSLSEAMEALNREQESARLQQRERETLEEERQ------------------------------ALTLRLEAEQQRC 141
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaalllaglrglagavavligveaayeaALEAALAAALQNI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 142 CVLQEERDAARAGQLSEHRE--LETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWE-TQHQ 218
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlVAAR 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 219 LALVQSEVRRLEGELDTARRERDALQL----------EMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEsslRQA 288
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEE---ERE 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 289 ASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREqarvcelqsgnQQLEEQRVELVERLQ 368
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL-----------EELERELERLEREIE 777
|
..
gi 1034598051 369 AM 370
Cdd:COG1196 778 AL 779
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
19-229 |
8.07e-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: 52.65 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 19 QSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKtLARVVEGWNRHEAERTEVLRGLQEEHQAaeltrskqqETVTRLEQS 98
Cdd:COG3096 451 QQATEEVLELEQKLSVADAARRQFEKAYELVCK-IAGEVERSQAWQTARELLRRYRSQQALA---------QRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 99 LSEAMEALNREQESARLQQRERETLEEERQA---LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQT 175
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEFCQRIGQQLDAaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034598051 176 ---W----------AQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHqlalVQSEVRRL 229
Cdd:COG3096 601 apaWlaaqdalerlREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQA----LESQIERL 663
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
40-360 |
9.76e-07 |
|
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: 52.53 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 40 RKKDTMIEQLDKTLARVVEGWN-RHEAERTEVLRGLQEEHQAAEltrskqqetvtRLEQSLSEAMEALNREQESARLQQR 118
Cdd:pfam12128 375 AKYNRRRSKIKEQNNRDIAGIKdKLAKIREARDRQLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 119 ERETLEEERQA-------LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR--------------AALEEERQTWA 177
Cdd:pfam12128 444 SRLGELKLRLNqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARkrrdqasealrqasRRLEERQSALD 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 178 QQEHQL------------------------------------------------------KEHYQALQEESQAQLEREKE 203
Cdd:pfam12128 524 ELELQLfpqagtllhflrkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 204 KSQREAQAAWETQHQLAlvqsevRRLEGELDTARRERDALQLEMSLVQARYESQRIQL------ESELAVQLEQRVTERL 277
Cdd:pfam12128 604 ERLDKAEEALQSAREKQ------AAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdeKQSEKDKKNKALAERK 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 278 AQAQEsSLRQAAslrehhrKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGN---- 353
Cdd:pfam12128 678 DSANE-RLNSLE-------AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAkael 749
|
....*..
gi 1034598051 354 QQLEEQR 360
Cdd:pfam12128 750 KALETWY 756
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-281 |
1.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 101 EAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagQLSEHRELETLRAALEEERQTWAQQE 180
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 181 HQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQ 260
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|.
gi 1034598051 261 LESELAVQLEQRVTERLAQAQ 281
Cdd:COG4717 229 LEQLENELEAAALEERLKEAR 249
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
144-367 |
1.47e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.98 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 144 LQEERDAARAGQLSEHRELETLRAALEEERQTW--AQQEHQLKEHYQALQEESQAQL--EREKEKSQREAQAAWETQHQL 219
Cdd:PRK10929 32 LEQAKAAKTPAQAEIVEALQSALNWLEERKGSLerAKQYQQVIDNFPKLSAELRQQLnnERDEPRSVPPNMSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 220 ALVQSEV----RRLEGELDTARRERDALQLemsLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHH 295
Cdd:PRK10929 112 LQVSSQLleksRQAQQEQDRAREISDSLSQ---LPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034598051 296 RKQLQ--DLSGQHQQElasqLAQFKVEMAEReeRQQQVaeDYELRLAREQarvceLQSGNQQLEEQRVELVERL 367
Cdd:PRK10929 189 VDELElaQLSANNRQE----LARLRSELAKK--RSQQL--DAYLQALRNQ-----LNSQRQREAERALESTELL 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
88-327 |
2.05e-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: 50.53 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 88 QQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRA 167
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 168 ALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwetqHQLALVQSEVRRLEGELDTARRERDALQlem 247
Cdd:COG4942 98 ELEA-------QKEELAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 248 sLVQARYESQRIQLESELAVQLEQRVT-ERLAQAQESSLRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREE 326
Cdd:COG4942 164 -ALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
.
gi 1034598051 327 R 327
Cdd:COG4942 242 R 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-380 |
2.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 64 EAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQRERETL----EEERQALTLRLEAEQQ 139
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEakkaEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 140 RCcvlQEERDAARAGQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQL 219
Cdd:PTZ00121 1547 KA---DELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 220 ALVQ--SEVRRLEGELDTARRE--RDALQL----EMSLVQARYESQRIQLESELAVQL-----EQRVTERLAQAQESSLR 286
Cdd:PTZ00121 1623 EELKkaEEEKKKVEQLKKKEAEekKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAkkaeeDEKKAAEALKKEAEEAK 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 287 QAASLRehhRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDyELRLAREQARvcELQSGNQQLEEQRVELVER 366
Cdd:PTZ00121 1703 KAEELK---KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKK--KIAHLKKEEEKKAEEIRKE 1776
|
330
....*....|....
gi 1034598051 367 LQAMLQAHWDEANQ 380
Cdd:PTZ00121 1777 KEAVIEEELDEEDE 1790
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
7-373 |
3.28e-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: 50.89 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 7 PHPFPQHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQldkTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRS 86
Cdd:pfam15921 69 AYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQ---SVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 87 KQQETVTRLE--QSLSEAMEAlNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELET 164
Cdd:pfam15921 146 QLQNTVHELEaaKCLKEDMLE-DSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 165 LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWeTQHQLalvqsEVRRLEGELDTARRERDALQ 244
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLI-SEHEV-----EITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 245 LEMSLVQARYESQRIQLESELAvQLEQRVTErlaqaQESSLRQAASLREHHRKQLQD---LSGQHQQELASQLAQFKVEM 321
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLS-DLESTVSQ-----LRSELREAKRMYEDKIEELEKqlvLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598051 322 AEREERQQQVAEDY-----ELRLAREQ-ARVCELQSGN--------QQLEEQRVElVERLQAMLQA 373
Cdd:pfam15921 373 GNLDDQLQKLLADLhkrekELSLEKEQnKRLWDRDTGNsitidhlrRELDDRNME-VQRLEALLKA 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-381 |
4.96e-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: 49.38 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 189 ALQEESQAQLEREKEKSQREAQAA----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR---YESQRIQL 261
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELekelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 262 ESELAvQLEQRVTERLAQAQESS--------LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE 333
Cdd:COG4942 96 RAELE-AQKEELAELLRALYRLGrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034598051 334 DYELRLAREQARVCELqsgnQQLEEQRVELVERLQAMLQAHWDEANQL 381
Cdd:COG4942 175 ELEALLAELEEERAAL----EALKAERQKLLARLEKELAELAAELAEL 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-367 |
5.16e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 39 DRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLsEAMEALnrEQESARLQQR 118
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR-EELETL--EAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 119 ERETLEEErQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQaQL 198
Cdd:PRK02224 267 IAETERER-EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE-EA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 199 EREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLE-----SELAVQLEQRV 273
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 274 TERLAQAqESSLRQAASLREHHRKQL---------QDLSG-----------QHQQELASQLAQFKVEMAEREERQQQVAE 333
Cdd:PRK02224 425 REREAEL-EATLRTARERVEEAEALLeagkcpecgQPVEGsphvetieedrERVEELEAELEDLEEEVEEVEERLERAED 503
|
330 340 350
....*....|....*....|....*....|....
gi 1034598051 334 dyelrlareqarVCELQSGNQQLEEQRVELVERL 367
Cdd:PRK02224 504 ------------LVEAEDRIERLEERREDLEELI 525
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
195-380 |
8.20e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 195 QAQLEREKEKSqREAQAAWE---TQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAV---- 267
Cdd:COG3206 181 EEQLPELRKEL-EEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 268 ---QLEQRVTERLAQAQESSLRQAASLREHH------RKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEdyelR 338
Cdd:COG3206 260 lqsPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA----Q 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034598051 339 LAREQARVCELQSGNQQLE--EQRVELVERLQAMLQAHWDEANQ 380
Cdd:COG3206 336 LAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEARL 379
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-379 |
1.42e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEgwnrHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 95 LEQSLSEAMEALNreqesarlqqreretleeerqALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQ 174
Cdd:PRK02224 389 LEEEIEELRERFG---------------------DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 175 TWAQ-------QEHQLKEHYQALQE--ESQAQLEREKEKSqREAQAAWETQHQLAlvqSEVRRLEGELDTARRERDALQL 245
Cdd:PRK02224 448 LLEAgkcpecgQPVEGSPHVETIEEdrERVEELEAELEDL-EEEVEEVEERLERA---EDLVEAEDRIERLEERREDLEE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 246 EMSLVQARYESQRIQLES--ELAVQLEQRVTERLAQAQEssLRQAAslrEHHRKQLQDLSGQhQQELASQLaqfkvEMAE 323
Cdd:PRK02224 524 LIAERRETIEEKRERAEElrERAAELEAEAEEKREAAAE--AEEEA---EEAREEVAELNSK-LAELKERI-----ESLE 592
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598051 324 REERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAmLQAHWDEAN 379
Cdd:PRK02224 593 RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE-LEAEFDEAR 647
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
74-287 |
1.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 74 LQEEHQAAEltrsKQQETVTRLEQsLSEAMEALNREQESARLQQReretleeerQALTLRLEAEQQRCCVLQEERDAARA 153
Cdd:COG4913 237 LERAHEALE----DAREQIELLEP-IRELAERYAAARERLAELEY---------LRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 154 gqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLER-EKEKSQREAQAAwETQHQLALVQSEVRRLEGE 232
Cdd:COG4913 303 -------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELE-ERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034598051 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 |
1.55e-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: 48.53 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 196 AQLEREKEKSQREAQAAWETQHQLALVQSEVR----RLEGELDTARRERDAL----QLEMSLVQARYES---QRIQLESE 264
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRqqleRLRREREKAERYQALLkekrEYEGYELLKEKEAlerQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 265 LAvQLEQRVTERLAQAQESSLR--QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMA-------EREERQQQVAE-- 333
Cdd:TIGR02169 246 LA-SLEEELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiaEKERELEDAEErl 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034598051 334 -DYELRLAREQARVCELQsgnQQLEEQRVElVERLQAMLQAHWDEANQLLS 383
Cdd:TIGR02169 325 aKLEAEIDKLLAEIEELE---REIEEERKR-RDKLTEEYAELKEELEDLRA 371
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
69-344 |
1.94e-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: 48.41 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 69 EVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALnreQESARLQqreretleeeRQALTLRLEAEQQRCCVLQEER 148
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL---QLLNKLL----------PQANLLADETLADRLEELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 149 DAARAGQ--LSEH----RELETLRAALeeerQTWAQQEHQLKEHYQAL---QEESQAQLEREKEKSQREAQAAWE-TQHQ 218
Cdd:COG3096 903 DAAQEAQafIQQHgkalAQLEPLVAVL----QSDPEQFEQLQADYLQAkeqQRRLKQQIFALSEVVQRRPHFSYEdAVGL 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 219 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES---QRIQLES------ELAVQLEQRVTERLAQAQESSLRQAA 289
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqVLASLKSsrdakqQTLQELEQELEELGVQADAEAEERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598051 290 SlrehHRKQLQDLSGQHQQ---ELASQLAQFKVEMAEREERQQQVAEDYelRLAREQA 344
Cdd:COG3096 1059 I----RRDELHEELSQNRSrrsQLEKQLTRCEAEMDSLQKRLRKAERDY--KQEREQV 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-369 |
2.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 45 MIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQRERETLE 124
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 125 EERQALTLRLEAEQQRccvlqeERDAARAGQLSEH-RELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE 203
Cdd:COG4717 126 QLLPLYQELEALEAEL------AELPERLEELEERlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 204 KSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARY----ESQRIQLESELAVQLEQRVT----- 274
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 275 ---ERLAQAQESSLRQAASLREHHRKQLQDLSGQ---HQQELASQLAQFKVEMAEREERQQQVAEDY-ELRLAREQARVC 347
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIeELQELLREAEEL 359
|
330 340
....*....|....*....|..
gi 1034598051 348 ELQSGNQQLEEQRVELVERLQA 369
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGV 381
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
75-366 |
2.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 75 QEEHQAAELTRSKQQETVTRLEQS---------------------------LSEAMEALNREQESARLQQRERETLEEER 127
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAeekaeaaekkkeeakkkadaakkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 128 QALTLRLEAEQQRCC-----VLQEERDAARAGQLSEH-RELETLRAALEEERQTwaqQEHQLKEHYQALQEESQAQLERE 201
Cdd:PTZ00121 1419 KADEAKKKAEEKKKAdeakkKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEA 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 202 KEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSlvQARYESQRIQLESELAVQLEQRVTERLAQAQ 281
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 282 E---SSLRQAASLREHHRKQLQDLSGQHQQElasqlAQFKVEMAEREERQQQVAEdyELRLAREQARVCELQSGNQQLEE 358
Cdd:PTZ00121 1574 EdknMALRKAEEAKKAEEARIEEVMKLYEEE-----KKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEK 1646
|
....*...
gi 1034598051 359 QRVELVER 366
Cdd:PTZ00121 1647 KKAEELKK 1654
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
191-373 |
2.87e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 191 QEESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLE 270
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 271 QRVT----ERLAQAQESS--LRQAASLR---EHHRKQLQDlsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRLAR 341
Cdd:COG3883 98 SGGSvsylDVLLGSESFSdfLDRLSALSkiaDADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|..
gi 1034598051 342 EQARVCELQSGNQQLEEQRVELVERLQAMLQA 373
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
213-381 |
2.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 213 WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQ------RVTERLAQAQESS- 284
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASaereiaELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 285 -LRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREERQQQV---AEDYELRLAREQARVCELQSGNQQLEEQR 360
Cdd:COG4913 686 dLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELqdrLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|.
gi 1034598051 361 VELVERLQAMLQAHWDEANQL 381
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
51-373 |
2.95e-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: 47.66 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 51 KTLARVVEGWNRHEAERTEVLRGLQ-EEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQA 129
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 130 LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREA 209
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 210 QAAwETQHQLALVQ-SEVRRLEGELDTARRERDALQLEMSLV--QARYESQRIQLESELAVQLEQRVTE--------RLA 278
Cdd:pfam02463 336 EIE-ELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLakKKLESERLSSAAKLKEEELELKSEEekeaqlllELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 279 QAQESSLR----QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRL-AREQARVCELQSGN 353
Cdd:pfam02463 415 RQLEDLLKeekkEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvKLQEQLELLLSRQK 494
|
330 340
....*....|....*....|
gi 1034598051 354 QQLEEQRVELVERLQAMLQA 373
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLA 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
27-302 |
3.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 27 ELQQQLAVAVAADRKKdtmIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 106
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 107 NREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagqlsEHRELETLRAALEEERqtwaQQEHQLKEh 186
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEK----KAAEALKK- 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 187 yqalQEESQAQLEREKEKSQREAQAAWETQHqlalvQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELA 266
Cdd:PTZ00121 1697 ----EAEEAKKAEELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034598051 267 VQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 302
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
19-229 |
4.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 19 QSLQTRVLELQQQLAVAVAADRKkdtmIEQLDKTLARVVEGWNRHEAERT--EVLRGLQEE-HQAAELTRSKQQetVTRL 95
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQ----FEQAYQLVRKIAGEVSRSEAWDVarELLRRLREQrHLAEQLQQLRMR--LSEL 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 96 EQSLSEAMEAlNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQT 175
Cdd:PRK04863 526 EQRLRQQQRA-ERLLAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598051 176 wAQQEHQLKEHYQALQEES--------------QAQLEREKEKSQREAQAAWETQHqlalVQSEVRRL 229
Cdd:PRK04863 602 -APAWLAAQDALARLREQSgeefedsqdvteymQQLLERERELTVERDELAARKQA----LDEEIERL 664
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
16-371 |
4.92e-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: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 16 RHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVV--------EGWNRHEAERTEVLRGLQEEHQAAELTRSK 87
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEiqelqekaESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 88 QQETVTRLEQSLSEAMEALNREQEsaRLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAA----RAGQLSEHRELE 163
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELK--LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAeereKTEKLKVEEEKE 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 164 TLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELdtarrerdaL 243
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI---------T 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 244 QLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlqdlSGQHQQELASQLAQFKVEmaE 323
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE-----IEERIKEEAEILLKYEEE--P 937
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034598051 324 REERQQQVAEDYELRLAREQARVcelqsgNQQLEEQRVELVERLQAML 371
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEE------RNKRLLLAKEELGKVNLMA 979
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-277 |
5.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARvvegwnrHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 95 LEQsLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDaaragqlsEHRELEtlrAALEEERQ 174
Cdd:PRK02224 581 LAE-LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE--------RKRELE---AEFDEARI 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 175 TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAawetqhqlalVQSEVRRLEgeldTARRERDALQLEMSLVQARY 254
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA----------VENELEELE----ELRERREALENRVEALEALY 714
|
250 260
....*....|....*....|....*.
gi 1034598051 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 |
5.36e-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: 46.66 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 29 QQQLAVAVAADRKKDTMIEQLDKTLARVvegwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVtRLEQSLSEAMEALNR 108
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERV-----RQELEAARKVKILEEERQRKIQQQKVEMEQI-RAEQEEARQREVRRL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 109 EQESARLQQRERETLEEERQALT-LRLEAEQQRCCVLQ---EERDAARAGQLSE---HRELETLRAALEEERQTWAQQEH 181
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVErLRQQEEERKRKKLElekEKRDRKRAEEQRRkilEKELEERKQAMIEEERKRKLLEK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 182 QLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEgeldtarrerdALQLEMSLVQARYESQRIQL 261
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-----------AMEREREMMRQIVESEKARA 589
|
....*...
gi 1034598051 262 ESELAVQL 269
Cdd:pfam17380 590 EYEATTPI 597
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-386 |
6.09e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 12 QHCERHIQSLQTRVLELQQQLAVA------VAADRKKDTMIEQLDKTLARVVEgWNRHEAERTEVLRGLQEEHQ----AA 81
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEeleeLL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 82 ELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSehrE 161
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALL---A 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 162 LETLRAALEEERQTWA------------QQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQS----- 224
Cdd:COG4717 261 LLGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeell 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 225 EVRRLEGELDTARRERDALQLEMSLvqARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAASLREHHRKQLQDLSG 304
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVEDEEELRAALEQAEE--YQELKEELEELEEQLEELLG 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 305 QHQQ--------ELASQLAQFKVEMAEREERQQQVAEdyelRLAREQARVCELQSGN--QQLEEQRVELVERLQAMLQAH 374
Cdd:COG4717 417 ELEEllealdeeELEEELEELEEELEELEEELEELRE----ELAELEAELEQLEEDGelAELLQELEELKAELRELAEEW 492
|
410
....*....|..
gi 1034598051 375 wdEANQLLSTTL 386
Cdd:COG4717 493 --AALKLALELL 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-258 |
7.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 27 ELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAErtevLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 106
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 107 NREQESARlQQRERETLEEERQALTLRLEAEQqrccVLQEERDAARAGQLSEHR--ELETLRAALEEERQTWAQQEHQLK 184
Cdd:COG4942 100 EAQKEELA-ELLRALYRLGRQPPLALLLSPED----FLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034598051 185 EHYQALQEESQAQLEREKEKSQREAqaawetqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 258
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
15-371 |
8.06e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV--VEGWNRHEAERTEVLRGLQEEHQAAEltrSKQQETV 92
Cdd:PRK04863 382 EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEEL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 93 TRLEQSLSEAMEALNREQESARLQQreretleeerqaltlRLEAEQQRccvlQEERDAARagqlsehrelETLRAAleEE 172
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVR---------------KIAGEVSR----SEAWDVAR----------ELLRRL--RE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 173 RQTWAQQEHQLKEHYQALQEESQAQleREKEKSQREAQAAWETQHQLAlvqSEVRRLEGELDTarrERDALQLEMSLVQA 252
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDE---DELEQLQEELEA---RLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 253 RYESQRIQLEselavQLEQRVTERLAQAQESSLRQAASlrehhrKQLQDLSGQHqQELASQLAQFKVEMAEREERQQQVA 332
Cdd:PRK04863 580 RRMALRQQLE-----QLQARIQRLAARAPAWLAAQDAL------ARLREQSGEE-FEDSQDVTEYMQQLLERERELTVER 647
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034598051 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 |
8.14e-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: 46.10 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 158 EHRELETLRAALEEERQTWAQQEHQLKEHYQALQ----------EESQAQLEREKEksqREAQAAWETQHQLALVQSEVR 227
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanllaDETLADRLEELR---EELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 228 RLEGELDTARR---ERDALQLEMSLVQARYESQRIQLESelAVQLEQRVT--------ERLAQAQESS------LRQAAS 290
Cdd:COG3096 921 QLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFA--LSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 291 LREHHRKQLQDLSGQHQ---QELAS----------QLAQFKVEMAEREERQQQVAEdyelrlAREQARVCELQSGNQQLE 357
Cdd:COG3096 999 ARREAREQLRQAQAQYSqynQVLASlkssrdakqqTLQELEQELEELGVQADAEAE------ERARIRRDELHEELSQNR 1072
|
250 260
....*....|....*....|....*
gi 1034598051 358 EQRVELvERLQAMLQAHWDEANQLL 382
Cdd:COG3096 1073 SRRSQL-EKQLTRCEAEMDSLQKRL 1096
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
74-355 |
8.82e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 74 LQEEHQAAELTRSKQQE---------TVTRLEQSLSEAMEALNreqESARLQQRERETLEEERQALTLRLEAEQQRCCVL 144
Cdd:PRK10929 112 LQVSSQLLEKSRQAQQEqdrareisdSLSQLPQQQTEARRQLN---EIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 145 QEERDAAragQLSEH--RELETLRAALEEERQtwaqqeHQLKEHYQALQEESQAQlerekekSQREAQAAWETQHQLAlv 222
Cdd:PRK10929 189 VDELELA---QLSANnrQELARLRSELAKKRS------QQLDAYLQALRNQLNSQ-------RQREAERALESTELLA-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 223 qsevrrlEGELDTARRERDALQLEMSLVQA-RYESQRIQLeseLAVQleqrvtERLAQAQESSLRQAAS-LREHH----- 295
Cdd:PRK10929 251 -------EQSGDLPKSIVAQFKINRELSQAlNQQAQRMDL---IASQ------QRQAASQTLQVRQALNtLREQSqwlgv 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034598051 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 |
1.06e-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: 45.83 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAvavaadrKKDTMIEQLDKTLARVVEgwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 95 LEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlsehrELETLRAALEEERq 174
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVD- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 175 twaqqehqlKEHYQALQEESQAQLEREKEKSQREaqaawETQHQLALVQSEVRRLEGELdtarrerdaLQLEMSLvqARY 254
Cdd:TIGR02169 378 ---------KEFAETRDELKDYREKLEKLKREIN-----ELKRELDRLQEELQRLSEEL---------ADLNAAI--AGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 255 ESQRIQLESEL-AVQLEQRvterlaqAQESSLRQAASLREHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAE 333
Cdd:TIGR02169 433 EAKINELEEEKeDKALEIK-------KQEWKLEQLAADLSKYEQELYDLK-EEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
15-370 |
1.30e-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: 45.55 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDtmiEQLDKTLARVVEgwnrHEAERTEVLRGLQE-EHQAAELTRSKQQETVT 93
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARLEE----ETAQKNNALKKIRElEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 94 R-----LEQSLSEAMEALNREQESarlqqreretleeerqalTLRLEAEQQRccvLQEERDaaragqlsehRELETLRAA 168
Cdd:pfam01576 287 RnkaekQRRDLGEELEALKTELED------------------TLDTTAAQQE---LRSKRE----------QEVTELKKA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 169 LEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMS 248
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 249 LVQARY---ESQRIQLESELA-VQLE-QRVTERLAQAQESSLRQAASLREHHrKQLQDLSGQHQQE------LASQLAQF 317
Cdd:pfam01576 416 ELQARLsesERQRAELAEKLSkLQSElESVSSLLNEAEGKNIKLSKDVSSLE-SQLQDTQELLQEEtrqklnLSTRLRQL 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034598051 318 KvemAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRVELVERLQAM 370
Cdd:pfam01576 495 E---DERNSLQEQLEEEEEAKRNVER----QLSTLQAQLSDMKKKLEEDAGTL 540
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
216-377 |
1.43e-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: 44.15 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 216 QHQLALVQSEVRRLEGELDTARRERDALQLEmsLVQARYESQRIQLESELAVQLEQRVTERLAQAqeSSLRQAASLR--- 292
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQkei 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 293 EHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:COG1579 99 ESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
....*
gi 1034598051 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 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 21 LQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEhqaaeltrSKQQETVTRLEQSLS 100
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE--------RKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 101 EAMEALNREQESarlqqreretLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQE 180
Cdd:TIGR02169 364 EELEDLRAELEE----------VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034598051 181 HQLKEhYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR 253
Cdd:TIGR02169 434 AKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-372 |
2.63e-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: 44.57 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 22 QTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSE 101
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 102 AMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE---HRELETLraALEEERQTWAQ 178
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalHALQLTL--TQERVREHALS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 179 QEHQlkehyqalQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 258
Cdd:TIGR00618 667 IRVL--------PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 259 IQLESELAVQLEQRVTERLAQAQESSLR-QAASLREHHRKQLQDLSG--QHQQELASQLAQfkvEMAEREERQQQVAEDY 335
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEAHFNNnEEVTAALQTGAELSHLAAeiQFFNRLREEDTH---LLKTLEAEIGQEIPSD 815
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034598051 336 EL-RLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 372
Cdd:TIGR00618 816 EDiLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
218-346 |
2.98e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.69 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 218 QLALVQSEVRRLEGELDTARRERDALQ-------------LEMSLVqARYESQRIQLESELAvQLEQRVTE---RLAQAQ 281
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFRnrngildpeataeALLQLI-ATLEGQLAELEAELA-ALRSYLSPnspQVRQLR 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034598051 282 esslRQAASLREHHRKQLQDLSGQHQQE-LASQLAQFKVEMAEREERQQQvaedYELRLAR-EQARV 346
Cdd:COG3524 256 ----RRIAALEKQIAAERARLTGASGGDsLASLLAEYERLELEREFAEKA----YTSALAAlEQARI 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-381 |
3.11e-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: 44.28 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 192 EESQAQLEREKEKSQREAQaawetqhqLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLeSELAVQLEQ 271
Cdd:TIGR02168 667 KTNSSILERRREIEELEEK--------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 272 rvterlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVaEDYELRLAREQARVCELQS 351
Cdd:TIGR02168 738 ------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRA 810
|
170 180 190
....*....|....*....|....*....|
gi 1034598051 352 GNQQLEEQRVELVERLQAMLQAHWDEANQL 381
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRL 840
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-298 |
4.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARvvegwnrhEAERTEVLRGLQEEH--QAAELTRS-----K 87
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--------EKKKAEELKKAEEENkiKAAEEAKKaeedkK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 88 QQETVTRLEQSLSEAMEALNREQESAR-LQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagqlsEHRELETLR 166
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAK 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 167 AAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVrRLEGELDTARRERDALQLE 246
Cdd:PTZ00121 1751 KD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN-IIEGGKEGNLVINDSKEME 1828
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034598051 247 MSLVQARYESQRIQLESELAVQleQRVTERLAQAQESSLRQAASLREHHRKQ 298
Cdd:PTZ00121 1829 DSAIKEVADSKNMQLEEADAFE--KHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-513 |
4.31e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 21 LQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVvegwnrheAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLS 100
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL--------ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 101 EAMEALnrEQESARLQQRERETLEEERQALTLRLEAEQQRCcvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQE 180
Cdd:pfam15921 507 EKERAI--EATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 181 HQLKehyqALQEEsQAQLEREKEKSQREAQaawetqhqlalvqsEVRRLEGELDTARRERDA----LQLE-MSLVQAryE 255
Cdd:pfam15921 583 RTAG----AMQVE-KAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEArvsdLELEkVKLVNA--G 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 256 SQRIQLESELAVQLEQRVTErlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQ------ 329
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNE--VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlksme 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 330 -------QVAEDYELRLAREQARVCELQSGNQQLEEQRVElVERLQAMLQAHWDEANQLLSTTlpPPNPPAPPAGPSSPG 402
Cdd:pfam15921 720 gsdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN-ANKEKHFLKEEKNKLSQELSTV--ATEKNKMAGELEVLR 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 403 PQEPEKEERrvwtMPPMAVALKPVLQQSREARD----ELPGAPPVLCSSSSDLSLLLGPSFQSQHSFQPLEPKP---DLT 475
Cdd:pfam15921 797 SQERRLKEK----VANMEVALDKASLQFAECQDiiqrQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPasfTRT 872
|
490 500 510
....*....|....*....|....*....|....*...
gi 1034598051 476 SSTAGAFSALGAFHPDHRAERPFPEEDPGPDGEGLLKQ 513
Cdd:pfam15921 873 HSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQE 910
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
15-212 |
4.45e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLArvvegwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 94
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------AQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 95 LEQSLsEAMEALNREQESarlQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQ 174
Cdd:COG4942 134 AVRRL-QYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034598051 175 TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAA 212
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-360 |
4.66e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 64 EAERTEVLRGLQEEHQAAELTR---SKQQETVTRLEQSLSEAMEALNREQ----------ESARLQQRERETLEEERQ-- 128
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAEEernneeirkfEEARMAHFARRQAAIKAEea 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 129 --ALTLRlEAEqqrccvlqEERDAARAGQLSEHRELETLRAALEEERQTwaqqehqlkehyqalqEESQAQLEREKEKSQ 206
Cdd:PTZ00121 1278 rkADELK-KAE--------EKKKADEAKKAEEKKKADEAKKKAEEAKKA----------------DEAKKKAEEAKKKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 207 REAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavqlEQRVTERLAQAQESSLR 286
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-------EKKKADEAKKKAEEDKK 1405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 287 QAASLR--EHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDY----ELRLAREQARVCElqSGNQQLEEQR 360
Cdd:PTZ00121 1406 KADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeEAKKKAEEAKKAD--EAKKKAEEAK 1483
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
15-275 |
5.28e-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: 43.79 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQ-------LDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSK 87
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQlkeqlqlLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 88 QQETVTRLEQSLSeameALNREQES-ARLQQreretleeERQALTLRLEAEQQRCCVLQE--ERDAA-----RAGQLSEH 159
Cdd:COG3096 915 HGKALAQLEPLVA----VLQSDPEQfEQLQA--------DYLQAKEQQRRLKQQIFALSEvvQRRPHfsyedAVGLLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 160 REL-ETLRAALEEERQTWAQQEHQLKehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 238
Cdd:COG3096 983 SDLnEKLRARLEQAEEARREAREQLR---QAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034598051 239 ERDALQLEMSLVQAR---YESQRIQLESELAvQLEQRVTE 275
Cdd:COG3096 1060 RRDELHEELSQNRSRrsqLEKQLTRCEAEMD-SLQKRLRK 1098
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
64-363 |
5.55e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 64 EAERTEVLRGLQ----EEHQAAELTRSKQQET--VTRLEqslsEAMEALNREQESARLQQRERETLEEERQALTLRLEAE 137
Cdd:PRK10246 215 PEQVQSLTASLQvltdEEKQLLTAQQQQQQSLnwLTRLD----ELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 138 QQRCCVL-QEERDAARAGQLSEHRELET-LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWET 215
Cdd:PRK10246 291 QLRPHWErIQEQSAALAHTRQQIEEVNTrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 216 Q-HQLALVQSEVRRLEGELDTARRERDAL-QLEMSLVqaryesqriqlESELAVQLEQRVTERLAQAQESSLRQAASLRE 293
Cdd:PRK10246 371 QfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLT-----------ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 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 |
7.19e-04 |
|
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: 43.04 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 206 QREAQAAWetQHQLALVQSEVR-RLEGELDTARRER---DALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAq 281
Cdd:pfam04632 158 RARLRARL--RDALRLAAAALAgAPGAEAFEAARLRlaaDILALEALRSHAAFESPRGRARARALRRLLARMLALLPRL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 282 eSSLRQaaslrehHRKQLQDLSGQHQQELASQLAqfkvEMAEREERQQqvAEDYELRLAREQARVCELQSGNQQLEEQRV 361
Cdd:pfam04632 235 -RSLAR-------LLARLRTEGAGTVPELAALLD----ELAAWEAALA--AEALQAALAALRARLRALRPALPLDFDTAA 300
|
170
....*....|..
gi 1034598051 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 |
7.22e-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: 43.02 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 90 ETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHR--ELETLRA 167
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH---LNLVQTALRQQEKIERYqeDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 168 ALEEERQTWAQQEHQLKEHYQALQeesQAQLEREKEKSQ-REAQAAWETQHQLAL-VQSEVRRLEgeldTARRERDALQL 245
Cdd:COG3096 362 RLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSLKSQlADYQQALDVQQTRAIqYQQAVQALE----KARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 246 EMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASL---------REHHRKQLQDLSGQH--QQELASQL 314
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELvckiageveRSQAWQTARELLRRYrsQQALAQRL 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598051 315 AQFKVEMAE---REERQQQV---AEDYELRLAREQARVCELQSGNQQLEEQRVELVERL------QAMLQAHWDEANQ 380
Cdd:COG3096 515 QQLRAQLAEleqRLRQQQNAerlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqRSELRQQLEQLRA 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
15-328 |
8.45e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKD-------TMIEQLDKTLARVvegWNRHEAERTEVLRGLQEEHQAAELTRSK 87
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASreetfarTALKNARLDLRRL---FDEKQSEKDKKNKALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 88 QQETVTRLEQSLSEAMEALNREQESARLQQRERETL---------EEERQALTLRLEAEQQRCCVLQEERDAARAGQ--- 155
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVvegaldaqlALLKAAIAARRSGAKAELKALETWYKRDLASLgvd 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 156 ----LSEHRELETLRAALEEErqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEG 231
Cdd:pfam12128 767 pdviAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRA 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 232 ELDTARRERDALQLEMS--LVQARYESQRIQL--ESELAVQLEQRVTERLAQAQEsSLRQAASLREHHRKQLQDLSGQHQ 307
Cdd:pfam12128 843 KLEMERKASEKQQVRLSenLRGLRCEMSKLATlkEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHFKNVIA 921
|
330 340
....*....|....*....|.
gi 1034598051 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 |
1.04e-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: 41.67 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 144 LQEERDAARAGQLSEHRELETLRAALEEerqtwaqqehqLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 223
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034598051 224 SEVRRLEGELdtaRRERDALQLEMSLVQARYESQRIQL---------ESELAVQLEQrVTERLAQAQ 281
Cdd:pfam09787 121 EELRYLEEEL---RRSKATLQSRIKDREAEIEKLRNQLtsksqssssQSELENRLHQ-LTETLIQKQ 183
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-384 |
1.31e-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: 42.26 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 128 QALTLRLEAEQQrccVLQEERDAARAGQLSEHRELETLRAALEEERQT--WAQQEHQLKEHYQALQEESQAQLEREKEKS 205
Cdd:TIGR00618 197 ELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQShaYLTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 206 QREA-------------QAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQR 272
Cdd:TIGR00618 274 AQEAvleetqerinrarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 273 VTERLAQAQESSLR-----QAASLREHHRKQLQDLSGQHQQE--LASQLAQFKVEMA--------EREERQQQVAEDYEL 337
Cdd:TIGR00618 354 EIHIRDAHEVATSIreiscQQHTLTQHIHTLQQQKTTLTQKLqsLCKELDILQREQAtidtrtsaFRDLQGQLAHAKKQQ 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034598051 338 RLAREQARVCELQSGNQQLEEQrveLVERLQAMLQAHWDEANQLLST 384
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQT 477
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
56-212 |
1.44e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 56 VVEGWNRHE-----AERTEVLRGLQEEHQAAELtRSKQQETVTRLEQslseamealnREQESARLQQRERETLEEERQAL 130
Cdd:PRK09510 60 VVEQYNRQQqqqksAKRAEEQRKKKEQQQAEEL-QQKQAAEQERLKQ----------LEKERLAAQEQKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 131 TLRLEAEQQRccvlQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQA---LQEESQAQLERE-KEKSQ 206
Cdd:PRK09510 129 LKQKQAEEAA----AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAkkkAEAEAAAKAAAEaKKKAE 204
|
....*.
gi 1034598051 207 REAQAA 212
Cdd:PRK09510 205 AEAKKK 210
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
10-384 |
1.49e-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: 42.05 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 10 FPQHCERHIQSLQTRVLELQQQLAvavAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSkqq 89
Cdd:pfam07111 300 FPKKCRSLLNRWREKVFALMVQLK---AQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERM--- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 90 eTVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCcvlqeERDAARAGQLSEH-----RELET 164
Cdd:pfam07111 374 -SAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV-----EQAVARIPSLSNRlsyavRKVHT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 165 LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVRRL--EGELDTARRERDA 242
Cdd:pfam07111 448 IKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA-ELQLSAHLIQQEVGRAreQGEAERQQLSEVA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 243 LQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQaaslREHHRKQLQDLSGQHQQELASQLAQFKVEMA 322
Cdd:pfam07111 527 QQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQ----QEIYGQALQEKVAEVETRLREQLSDTKRRLN 602
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598051 323 EREERQQQVAedyeLRLAREQARVCELQSGNQQL----EEQRVELVERLQAMLQAHWDEANQLLST 384
Cdd:pfam07111 603 EARREQAKAV----VSLRQIQHRATQEKERNQELrrlqDEARKEEGQRLARRVQELERDKNLMLAT 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-302 |
2.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 18 IQSLQTRVLELQQQLAVA----VAADRKKDTMIEQLD--KTLARVVEGWNRHEAERTEvLRGLQEEHQAAELTRS---KQ 88
Cdd:COG4913 612 LAALEAELAELEEELAEAeerlEALEAELDALQERREalQRLAEYSWDEIDVASAERE-IAELEAELERLDASSDdlaAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 89 QETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAA 168
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 169 LEEERQTWAQQEHQL-----------KEHYQALQEESQAQLER-----------------EKEKSQREAQAAWETQHQLA 220
Cdd:COG4913 771 LEERIDALRARLNRAeeeleramrafNREWPAETADLDADLESlpeylalldrleedglpEYEERFKELLNENSIEFVAD 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 221 LVQsevrRLEGELDTARRERDalQLEMSLVQARYESQR-IQLE-SELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQ 298
Cdd:COG4913 851 LLS----KLRRAIREIKERID--PLNDSLKRIPFGPGRyLRLEaRPRPDPEVREFRQELRAVTSGASLFDEELSEARFAA 924
|
....
gi 1034598051 299 LQDL 302
Cdd:COG4913 925 LKRL 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-220 |
2.84e-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: 41.20 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 14 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEH---QAAELTRSKQQE 90
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaelEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 91 TVTRLEQ---SLSEAMEALNREQESARLQ----QRERETLEEERQALTLRL-EAEQQRCCVLQEERDAARAGQLSEHREL 162
Cdd:TIGR02168 380 QLETLRSkvaQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 163 ETLRAALEEERQTWAQQEHQLKEHYQALQE--ESQAQLEREKEKSQREAQAAWETQHQLA 220
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
144-321 |
3.70e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.42 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 144 LQEERDAArAGQLSEHRELETLRAALEEERQTWAQQEHQLKEH------YQALQEESQAQLEREKEKSQREAQAAwetqh 217
Cdd:COG1842 39 LVEARQAL-AQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlaREALERKAELEAQAEALEAQLAQLEE----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 218 QLALVQSEVRRLEGELDTARRERDALQlemslvqARYESQRIQ---------LESELAV----QLEQRVTERLAQAQESS 284
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLK-------ARAKAAKAQekvnealsgIDSDDATsaleRMEEKIEEMEARAEAAA 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034598051 285 -LRQAASLREhhrkQLQDLSGQHqqELASQLAQFKVEM 321
Cdd:COG1842 186 eLAAGDSLDD----ELAELEADS--EVEDELAALKAKM 217
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
166-279 |
6.26e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 37.62 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 166 RAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE---KSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDA 242
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqNYERELVLHAEDIKALQALREELNELKAEIAELKAEAES 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034598051 243 LQLEMSLVQARYESQRIQLESELAvQLEQRVTERLAQ 279
Cdd:pfam07926 83 AKAELEESEESWEEQKKELEKELS-ELEKRIEDLNEQ 118
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
15-261 |
6.35e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.67 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 15 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQL-----DKT-LARVVEGWNRHEAERTEVLRG----LQEEHQAAElt 84
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELrielrDKTaQAEALERQLAAETEQNRALEEenkaLREEAQAAE-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 85 rskqqETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEaeqqrccvlqeERDAARAGQLSEHRELET 164
Cdd:pfam19220 153 -----KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLA-----------ELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 165 LRAALEEERQtwaQQEHQLKEHYQALQEESQAQLEREKEKSQREA---QAAWETQHQLALVQSEVRRLEGELDTARRERD 241
Cdd:pfam19220 217 QLAAEQAERE---RAEAQLEEAVEAHRAERASLRMKLEALTARAAateQLLAEARNQLRDRDEAIRAAERRLKEASIERD 293
|
250 260
....*....|....*....|
gi 1034598051 242 ALQLEMSLVQARYESQRIQL 261
Cdd:pfam19220 294 TLERRLAGLEADLERRTQQF 313
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
35-370 |
6.68e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 35 AVAADRKKDTMIEQLDKTLARVVEgwNRHEAERTEvlRGLQEEHQaaELTRSKqqETVTRLEQSLSEAMEALNREQESAR 114
Cdd:pfam01576 627 AEAEAREKETRALSLARALEEALE--AKEELERTN--KQLRAEME--DLVSSK--DDVGKNVHELERSKRALEQQVEEMK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 115 LQQRERETLEEERQALTLRLEAEQQRCCVlQEERD-AARAGQLSEHReletlRAALEEERQTWAQQEHQLKEHYQALQEE 193
Cdd:pfam01576 699 TQLEELEDELQATEDAKLRLEVNMQALKA-QFERDlQARDEQGEEKR-----RQLVKQVRELEAELEDERKQRAQAVAAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 194 SQAQLEREKEKSQREA--QAAWETQHQLALVQSEVRRLEGELDTARRERDALqlemsLVQAR--------YESQRIQLES 263
Cdd:pfam01576 773 KKLELDLKELEAQIDAanKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----LAQSKesekklknLEAELLQLQE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 264 ELAV---QLEQRVTER--LAQAQESSLRQAASLREHHRkQLQDLSGQHQQELASQlaQFKVEM-AEREERQQQVAEDYEL 337
Cdd:pfam01576 848 DLAAserARRQAQQERdeLADEIASGASGKSALQDEKR-RLEARIAQLEEELEEE--QSNTELlNDRLRKSTLQVEQLTT 924
|
330 340 350
....*....|....*....|....*....|...
gi 1034598051 338 RLAREQARVCELQSGNQQLEEQRVELVERLQAM 370
Cdd:pfam01576 925 ELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
180-344 |
6.94e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 180 EHQLKEHYQALQEesqaqLEREKEKSQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRI 259
Cdd:COG1579 23 EHRLKELPAELAE-----LEDELAALEARLEAA---KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 260 QLESELAvqleqrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRL 339
Cdd:COG1579 95 QKEIESL--------KRRISDLEDEILELMERIEELEEELAEL----EAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*
gi 1034598051 340 AREQA 344
Cdd:COG1579 163 AEREE 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-290 |
7.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 12 QHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQ------EEHQAAELTR 85
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlglLALLFLLLAR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 86 SKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETL 165
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 166 RAALE-------EERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQhqLALVQSEVRRLEGELDTARR 238
Cdd:COG4717 376 LAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELRE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034598051 239 ERDALQLEMSLV---------QARYESQRIQLESE--------LAVQLEQRVTERLAQAQESSLRQAAS 290
Cdd:COG4717 454 ELAELEAELEQLeedgelaelLQELEELKAELRELaeewaalkLALELLEEAREEYREERLPPVLERAS 522
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
201-346 |
8.88e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.94 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 201 EKEKSQREAQAAwETQHQLALVQSEVRRLE---GELDTARRERDALQLEMSLVQARYESQRIQLESelaVQLEQRVTERL 277
Cdd:pfam00529 57 QAALDSAEAQLA-KAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ---AQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034598051 278 AQAQESSLRQAASLREhHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARV 346
Cdd:pfam00529 133 APIGGISRESLVTAGA-LVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
188-379 |
9.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 188 QALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQ-LEMSLVQARYESQRIQlesela 266
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKdDNDEETRETLSTLSLR------ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598051 267 vQLEQRVTERLAQAQE--SSLRQAASLrehhrkqlqdLSGQHQQelaSQLAQfkVEMAEREERQQQV--------AEDYE 336
Cdd:PRK11281 125 -QLESRLAQTLDQLQNaqNDLAEYNSQ----------LVSLQTQ---PERAQ--AALYANSQRLQQIrnllkggkVGGKA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034598051 337 LRLAREQARVCELQSGNQQLEEQRVELV--ERLQAMLQAHWDEAN 379
Cdd:PRK11281 189 LRPSQRVLLQAEQALLNAQNDLQRKSLEgnTQLQDLLQKQRDYLT 233
|
|
| |
