|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-470 |
8.66e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.54 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 116 QSLQTRVLELQQQLAVAvaADRKKDTMIEQLDKTLArvvegwnrheaERTEVLRGLQEEHQAAELTRSKQQETVTRLEQS 195
Cdd:COG1196 216 RELKEELKELEAELLLL--KLRELEAELEELEAELE-----------ELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 196 LSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQ 275
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 276 QEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 355
Cdd:COG1196 363 AEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 356 IQLESELAVQLEQrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELR 435
Cdd:COG1196 442 EALEEAAEEEAEL---EEEEEALLELLAELLEEAALLEAALAEL----LEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350
....*....|....*....|....*....|....*.
gi 1213953200 436 LAREQARVC-ELQSGNQQLEEQRVELVERLQAMLQA 470
Cdd:COG1196 515 LLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-478 |
8.35e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 137 RKKDTMiEQLDKT---LARVvegwnrhEAERTEV---LRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESA 210
Cdd:COG1196 173 RKEEAE-RKLEATeenLERL-------EDILGELerqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 211 RLQQRERETLEEerqaltlRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLkEHYQALQEE 290
Cdd:COG1196 245 EAELEELEAELE-------ELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 291 SQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRV 370
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 371 TERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVcELQSGN 450
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEA 472
|
330 340
....*....|....*....|....*...
gi 1213953200 451 QQLEEQRVELVERLQAMLQAHWDEANQL 478
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-399 |
4.39e-14 |
|
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: 76.63 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 109 KHCERHIQSLQTRVLELQQQLAVAvaadRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQET 188
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAEL----RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 189 VTRLEQSLSEAMEALNREQESARLQQRERETLEEE-------RQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELET 261
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeeLKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 262 LRAALEEERQTWAQQEHQLK------EHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 335
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 336 ERDALQLEMSLVQARY---ESQRIQLESELAV--QLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 399
Cdd:TIGR02168 916 ELEELREKLAQLELRLeglEVRIDNLQERLSEeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-510 |
6.01e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 225 QALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR 304
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 305 EAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQ 384
Cdd:COG1196 294 LAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 385 AASLREHHRKQLQDLSGQHQQELASQLAQfkvemaerEERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERL 464
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQ--------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1213953200 465 QAMLQAHWDEANQLLSTTLPPPNPPAPPAGPSSPGPQEPEKEERRV 510
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-469 |
7.07e-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: 72.78 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 195 SLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE--HRELETLRAALEEERQT 272
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 273 WAQQEHQLkehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYE 352
Cdd:TIGR02168 745 LEERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 353 SQRIQLESEL--AVQLEQRVTERLAQAQESSLRQAASlrEHHRKQLQDLSGQHQQELAS---QLAQFKVEMAEREERQQQ 427
Cdd:TIGR02168 821 NLRERLESLErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEAllnERASLEEALALLRSELEE 898
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1213953200 428 VAEdyELRLAREQARvcELQSGNQQLEEQRVELVERLQAMLQ 469
Cdd:TIGR02168 899 LSE--ELRELESKRS--ELRRELEELREKLAQLELRLEGLEV 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-470 |
1.40e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 239 CVLQEERDAARAGQLSEH-RELETLRAALEEERQtwaQQEH--QLKEHYQALQEesqAQLEREKEKSQREAQAAWETQHQ 315
Cdd:COG4913 216 YMLEEPDTFEAADALVEHfDDLERAHEALEDARE---QIELlePIRELAERYAA---ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 316 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQrvTERLAQAQESSLRQAASLREHHRKQ 395
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 396 LQDLSGQHQ------QELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 469
Cdd:COG4913 368 LAALGLPLPasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
.
gi 1213953200 470 A 470
Cdd:COG4913 448 A 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-454 |
3.19e-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: 67.39 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 161 EAERTEVLRGLQEEHQAAELT------------RSKQQETVTRLEQSLSEAMEALNREQES---ARLQQRERETLEEERQ 225
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllvlrleelreeLEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 226 ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqRE 305
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL--EA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 306 AQAAWETQhqlalvqseVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVtERLAQAQESslrQA 385
Cdd:TIGR02168 366 ELEELESR---------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-----RLEDRR-ERLQQEIEE---LL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213953200 386 ASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE------DYELRLAREQARVCELQSGNQQLE 454
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaldAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-463 |
1.72e-10 |
|
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: 65.09 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 91 PPDFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEgwnrheaERTEVLRG 170
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 171 LQEEHQAAELTRSKQQEtvtrLEQSLSEAMEALNREQES-ARLQQRERETLEEERQALTLRLEAEQQRccvlQEERDAAR 249
Cdd:TIGR02169 746 LSSLEQEIENVKSELKE----LEARIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKLEEEVSR----IEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 250 AGQLSEhreLETLRAALEEERQTWAQQEHQLKEHYQALQEEsQAQLEREKEKSQREaqaawetqhqLALVQSEVRRLEGE 329
Cdd:TIGR02169 818 EQKLNR---LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-IENLNGKKEELEEE----------LEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 330 LDTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVTERLAQAQEsslrQAASLREHHRKQLQDLSGQHQQELAS 409
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIE-----KKRKRLSELKAKLEA----LEEELSEIEDPKGEDEEIPEEELSLE 954
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953200 410 QLAQFKVEMAEREERQQQV----AEDYElrlaREQARVCELQSGNQQLEEQRVELVER 463
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVnmlaIQEYE----EVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-462 |
1.36e-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: 62.01 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 162 AERTEVLRgLQEEHQAAELTRSKQQETVTRLEQSLSEA---MEALNREQESARLQQRERETLEEERQALTLRLEAEQQRC 238
Cdd:TIGR02169 671 SEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 239 cvlQEERDAARAgqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqreaqaawetqhqlal 318
Cdd:TIGR02169 750 ---EQEIENVKS-------ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK----------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 319 VQSEVRRLEGELDTARRERDALQLEMslvqaRYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLRE--HHRKQL 396
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEK-----EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleELEAAL 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 397 QDLSGQHqQELASQLAQFKVEMAEREERQQQVAEDYEL---RLAREQARVCELQSGNQQLEEQRVELVE 462
Cdd:TIGR02169 878 RDLESRL-GDLKKERDELEAQLRELERKIEELEAQIEKkrkRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
245-470 |
2.45e-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: 61.23 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 245 RDAARAGQLSEHRELETLRAALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVR 324
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 325 RLEGELDTARRERDALQLEMSLVQAR---YESQRIQLESELAVQLEQRVT--ERLAQAQEsslrQAASLREHH---RKQL 396
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEEleAQIEQLKE----ELKALREALdelRAEL 812
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1213953200 397 QDLSG-QHQQELASQLAQFKVEMAERE-ERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQA 470
Cdd:TIGR02168 813 TLLNEeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
146-478 |
4.69e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 146 LDKTLARVVEGWNRHEAERTEVLRG---LQEEHQAAELTRSKQQETVTR--------------LEQSLSEAMEALNREQE 208
Cdd:PRK04863 263 ITESTNYVAADYMRHANERRVHLEEaleLRRELYTSRRQLAAEQYRLVEmarelaelneaesdLEQDYQAASDHLNLVQT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 209 sARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALE------EERQTWAQQEHQLKe 282
Cdd:PRK04863 343 -ALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqalDVQQTRAIQYQQAV- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 283 hyQALQEESQ-------------AQLEREKEKSQREAQAAWETQHQLALVQ----------SEVRRLEGELDTARRERDA 339
Cdd:PRK04863 421 --QALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayQLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 340 LQLEmslvqARYESQRIQleselAVQLEQRvterlaQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQlAQFKVEMA 419
Cdd:PRK04863 499 RELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQE 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 420 EREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHwDEANQL 478
Cdd:PRK04863 562 ELEARL----ESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ-DALARL 615
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
224-464 |
5.55e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 224 RQALTLRLEAEQQRCCVLQEERDAARAgQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQ--AQLEREKEK 301
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDdlAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 302 SQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQRVTERLAQAQES 380
Cdd:COG4913 697 LEAELEEL---EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 381 SLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREE----RQQQVAED--------YELRLAREQARVCELQS 448
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylalLDRLEEDGlpeyeerfKELLNENSIEFVADLLS 853
|
250
....*....|....*.
gi 1213953200 449 gnqQLEEQRVELVERL 464
Cdd:COG4913 854 ---KLRRAIREIKERI 866
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
90-466 |
1.32e-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: 58.70 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 90 NPPDFQGLRDA---LDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKdtmIEQLDKTLARVVEGWNRHEAERTE 166
Cdd:pfam12128 239 IRPEFTKLQQEfntLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQL---LRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 167 VLRGLQEEHQAAEltrskqqetvTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRccvlQEERD 246
Cdd:pfam12128 316 AVAKDRSELEALE----------DQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK----YNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 247 AARAGQLSehRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREK-----EKSQREAQAAW----------- 310
Cdd:pfam12128 382 SKIKEQNN--RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKlefneEEYRLKSRLGElklrlnqatat 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 311 -ETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLR 389
Cdd:pfam12128 460 pELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--SALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 390 EHHRKQLQDLSgQHQQELAS--QLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 466
Cdd:pfam12128 538 HFLRKEAPDWE-QSIGKVISpeLLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-466 |
2.05e-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: 57.08 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 247 AARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQREAQaawETQHQLALVQSEVRRL 326
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 327 EGELDTARRERDALQLEMS-LVQARYESQRIQ-----LESELAVQLEQRVT--ERLAQAQESSLRQAASLREHHRKQLQD 398
Cdd:COG4942 89 EKEIAELRAELEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 399 LSGQHQQ--ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 466
Cdd:COG4942 169 LEAERAEleALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-445 |
2.94e-08 |
|
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: 57.67 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 107 RRKHCERHIQSLQTRVLELQQQLAVAVAADRKK-DTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQ 185
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSlHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 186 QETVTRLEQSLSEAMEALNREQEsARLQQRERETLEEERQALTLRLEAEQQRCCVLQ--------EERDAARAGQLSEHR 257
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQL-LKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 258 ELETLRAALEEERQTWAQQEHQLKEHYQALQ----EESQAQLEREKEKSQRE--AQAAWETQHQLALvQSEVRRLEGELD 331
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIREisCQQHTLTQHIHTL-QQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 332 TARRERDALQLEMSLVQARYESQRIqLESELAV-----QLEQRVTERLAQAQESSLrQAASLREHHRKQLQdlsgQHQQE 406
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRD-LQGQLAHakkqqELQQRYAELCAAAITCTA-QCEKLEKIHLQESA----QSLKE 470
|
330 340 350
....*....|....*....|....*....|....*....
gi 1213953200 407 LASQLAQFKVeMAEREERQQQVAEDYELRLAREQARVCE 445
Cdd:TIGR00618 471 REQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCG 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-478 |
2.96e-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: 57.77 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 228 TLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQ 307
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 308 aawETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAAS 387
Cdd:TIGR02169 748 ---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--IEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 388 LREHHRKQLQDLSgqhqQELASQLAQFKVEMAEREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVEL---VERL 464
Cdd:TIGR02169 823 RLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDEL 894
|
250
....*....|....
gi 1213953200 465 QAMLQAHWDEANQL 478
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
174-467 |
6.24e-08 |
|
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: 56.29 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 174 EHQAAeLTRSKQQETVTRLEQS-LSEAMEALNREQESAR-LQQRERETLEEERQALTLRleAEQQRCcVLQEERDAARAG 251
Cdd:pfam17380 279 QHQKA-VSERQQQEKFEKMEQErLRQEKEEKAREVERRRkLEEAEKARQAEMDRQAAIY--AEQERM-AMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 252 QLSEHRELETLRA---ALEEERQ---TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRR 325
Cdd:pfam17380 355 QEERKRELERIRQeeiAMEISRMrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 326 LEGELDTARRERdalqlEMSLVQARyESQRIQLESELAVQLEQRVTERLAQAQESSLRQAAslREHHRKQLQDLSGQHQQ 405
Cdd:pfam17380 435 REVRRLEEERAR-----EMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA--EEQRRKILEKELEERKQ 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213953200 406 ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVE---RLQAM 467
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEersRLEAM 571
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
162-480 |
8.72e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 162 AERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQreretleeerQALTlRLEaEQQRCCVL 241
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQ----------QAVQ-ALE-KARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 242 qEERDAARAGQlsehrELETLRAALEEERQTWAQQEHQL-------KEHYQALQ---------EESQA-QLEREKEKSQR 304
Cdd:COG3096 432 -PDLTPENAED-----YLAAFRAKEQQATEEVLELEQKLsvadaarRQFEKAYElvckiagevERSQAwQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 305 EAQAAWETQHQLALVQSEVRRLEGELDTARRerdaLQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQ 384
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQL--EELEEQAAEAVEQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 385 AASLReHHRKQLQDLSGQHQQ------ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRV 458
Cdd:COG3096 580 RSELR-QQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQ 654
|
330 340
....*....|....*....|..
gi 1213953200 459 ELVERLQAMLQAHWDEANQLLS 480
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLA 676
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-481 |
9.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 39 SERREEDSFDSDSTATLLNTRPLQDLSPSSSAQALEELFPRYTSLRPGPPLNPPDFQGLRDALDSEHTRRKHCERHIQSL 118
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 119 QTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEvlrgLQEEHQAAELTRSKQQETVTRLEQSLSE 198
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN----AEDFLEELREERDELREREAELEATLRT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 199 AMEALNreqESARLQQR---------------ERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE-HRELETL 262
Cdd:PRK02224 438 ARERVE---EAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIERL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 263 RAALEEERQTWAQQEHQLKEHYQALQE--ESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERDAL 340
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEElrERAAELEAEAEEKREAAAEAEE---EAEEAREEVAELNSKLAELKERIESL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 341 QLEMSLVQARYEsqriqLESELAVQLEQRvtERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFkvemae 420
Cdd:PRK02224 592 ERIRTLLAAIAD-----AEDEIERLREKR--EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERA------ 658
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953200 421 rEERQQQVAEDY-ELRLARE--QARVCELQSGNQQLE---EQRVELVERLQAmLQAHWDEANQLLST 481
Cdd:PRK02224 659 -EEYLEQVEEKLdELREERDdlQAEIGAVENELEELEelrERREALENRVEA-LEALYDEAEELESM 723
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-483 |
1.01e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 93 DFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVA------VAADRKKDTMIEQLDKTLARVVEgWNRHEAERTE 166
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPERLEELEERLEE-LRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 167 VLRGLQEEHQ----AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQ 242
Cdd:COG4717 168 LEAELAELQEeleeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 243 EERDAARAGQLSehrELETLRAALEEERQTWA------------QQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAW 310
Cdd:COG4717 248 ARLLLLIAAALL---ALLGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 311 ETQHQLALVQS-----EVRRLEGELDTARRERDALQLEMSLvqARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQA 385
Cdd:COG4717 325 LAALGLPPDLSpeellELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVEDEEELRAALEQAEE--YQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 386 ASLREHHRKQLQDLSGQHQQ--------ELASQLAQFKVEMAEREERQQQVAEdyelRLAREQARVCELQSGN--QQLEE 455
Cdd:COG4717 401 KEELEELEEQLEELLGELEEllealdeeELEEELEELEEELEELEEELEELRE----ELAELEAELEQLEEDGelAELLQ 476
|
410 420
....*....|....*....|....*...
gi 1213953200 456 QRVELVERLQAMLQAHwdEANQLLSTTL 483
Cdd:COG4717 477 ELEELKAELRELAEEW--AALKLALELL 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-467 |
1.53e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 97 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV---VEGWNRHEAERTEVLRGLQE 173
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEEEEEEALEEAAEEEAELEE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 174 EHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQ---------------------------- 225
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaalllaglrglagavavligveaay 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 226 --ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRE--LETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEK 301
Cdd:COG1196 537 eaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 302 SQREAQAAWE-TQHQLALVQSEVRRLEGELDTARRERDALQL----------EMSLVQARYESQRIQLESELAVQLEQRV 370
Cdd:COG1196 617 VLGDTLLGRTlVAARLEAALRRAVTLAGRLREVTLEGEGGSAggsltggsrrELLAALLEAEAELEELAERLAEEELELE 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 371 TERLAQAQEsslRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREqarvcelqsgn 450
Cdd:COG1196 697 EALLAEEEE---ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----------- 762
|
410
....*....|....*..
gi 1213953200 451 QQLEEQRVELVERLQAM 467
Cdd:COG1196 763 EELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-466 |
2.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 257 RELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQR--------EAQAAWETQHQLALVQSEVRRLEG 328
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLE-----RLRREREKAERyqallkekREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 329 ELDTARRERDALQLEMSLVQARYESQRIQLEsELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlQDLSGQHQQELA 408
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953200 409 SQLAQFKVEMaereERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 466
Cdd:TIGR02169 322 ERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
137-457 |
5.42e-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: 53.69 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 137 RKKDTMIEQLDKTLARVVEGWN-RHEAERTEVLRGLQEEHQAAEltrskqqetvtRLEQSLSEAMEALNREQESARLQQR 215
Cdd:pfam12128 375 AKYNRRRSKIKEQNNRDIAGIKdKLAKIREARDRQLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 216 ERETLEEERQA-------LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR--------------AALEEERQTWA 274
Cdd:pfam12128 444 SRLGELKLRLNqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARkrrdqasealrqasRRLEERQSALD 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 275 QQEHQL------------------------------------------------------KEHYQALQEESQAQLEREKE 300
Cdd:pfam12128 524 ELELQLfpqagtllhflrkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 301 KSQREAQAAWETQHQLAlvqsevRRLEGELDTARRERDALQLEMSLVQARYESQRIQL------ESELAVQLEQRVTERL 374
Cdd:pfam12128 604 ERLDKAEEALQSAREKQ------AAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdeKQSEKDKKNKALAERK 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 375 AQAQEsSLRQAAslrehhrKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGN---- 450
Cdd:pfam12128 678 DSANE-RLNSLE-------AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAkael 749
|
....*..
gi 1213953200 451 QQLEEQR 457
Cdd:pfam12128 750 KALETWY 756
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-378 |
5.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 198 EAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagQLSEHRELETLRAALEEERQTWAQQE 277
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 278 HQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQ 357
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|.
gi 1213953200 358 LESELAVQLEQRVTERLAQAQ 378
Cdd:COG4717 229 LEQLENELEAAALEERLKEAR 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-477 |
9.52e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 161 EAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQR----ERETLEEERQALTLRLEAEQQ 236
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 237 RCcvlQEERDAARAGQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQL 316
Cdd:PTZ00121 1547 KA---DELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 317 ALVQ--SEVRRLEGELDTARRE--RDALQL----EMSLVQARYESQRIQLESELAVQL-----EQRVTERLAQAQESSLR 383
Cdd:PTZ00121 1623 EELKkaEEEKKKVEQLKKKEAEekKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAkkaeeDEKKAAEALKKEAEEAK 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 384 QAASLRehhRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDyELRLAREQARvcELQSGNQQLEEQRVELVER 463
Cdd:PTZ00121 1703 KAEELK---KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKK--KIAHLKKEEEKKAEEIRKE 1776
|
330
....*....|....
gi 1213953200 464 LQAMLQAHWDEANQ 477
Cdd:PTZ00121 1777 KEAVIEEELDEEDE 1790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-424 |
1.01e-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: 51.69 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 185 QQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRA 264
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 265 ALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwetqHQLALVQSEVRRLEGELDTARRERDALQlem 344
Cdd:COG4942 98 ELEA-------QKEELAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 345 sLVQARYESQRIQLESELAVQLEQRVT-ERLAQAQESSLRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREE 423
Cdd:COG4942 164 -ALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
.
gi 1213953200 424 R 424
Cdd:COG4942 242 R 242
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
241-464 |
1.80e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.98 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 241 LQEERDAARAGQLSEHRELETLRAALEEERQTW--AQQEHQLKEHYQALQEESQAQL--EREKEKSQREAQAAWETQHQL 316
Cdd:PRK10929 32 LEQAKAAKTPAQAEIVEALQSALNWLEERKGSLerAKQYQQVIDNFPKLSAELRQQLnnERDEPRSVPPNMSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 317 ALVQSEV----RRLEGELDTARRERDALQLemsLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHH 392
Cdd:PRK10929 112 LQVSSQLleksRQAQQEQDRAREISDSLSQ---LPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213953200 393 RKQLQ--DLSGQHQQElasqLAQFKVEMAEReeRQQQVaeDYELRLAREQarvceLQSGNQQLEEQRVELVERL 464
Cdd:PRK10929 189 VDELElaQLSANNRQE----LARLRSELAKK--RSQQL--DAYLQALRNQ-----LNSQRQREAERALESTELL 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-313 |
1.89e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 111 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVT 190
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 191 RLEQsLSEAMEALNREQEsaRLQQRERETLEEERQaLTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEER 270
Cdd:TIGR02169 393 KLEK-LKREINELKRELD--RLQEELQRLSEELAD-LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1213953200 271 qtwaQQEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQ 313
Cdd:TIGR02169 469 ----QELYDLKEEYDRVEKE-LSKLQRELAEAEAQARASEERV 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-478 |
2.45e-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: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 286 ALQEESQAQLEREKEKSQREAQAA----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR---YESQRIQL 358
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELekelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 359 ESELAvQLEQRVTERLAQAQESS--------LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE 430
Cdd:COG4942 96 RAELE-AQKEELAELLRALYRLGrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1213953200 431 DYELRLAREQARVCELqsgnQQLEEQRVELVERLQAMLQAHWDEANQL 478
Cdd:COG4942 175 ELEALLAELEEERAAL----EALKAERQKLLARLEKELAELAAELAEL 218
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-480 |
2.76e-06 |
|
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: 51.33 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 101 LDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKdtmieQLDKTLArvvegwnrhEAErtevLRGLQEEHQAAEL 180
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-----QLEKVTT---------EAK----IKKLEEDILLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 181 TRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELE 260
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 261 TLRAALEEERQTWAQQEHQLKEHYQALQEESQAQleREKEKSQREAQAawetqhQLALVQSEVRRLEGELDTARRERDAL 340
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQK--NNALKKIRELEA------QISELQEDLESERAARNKAEKQRRDL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 341 QLEMSLVQARYES--QRIQLESELAVQLEQRVTErLAQAQESSLRQaaslrehHRKQLQDLSGQHQQ---ELASQLAQFK 415
Cdd:pfam01576 298 GEELEALKTELEDtlDTTAAQQELRSKREQEVTE-LKKALEEETRS-------HEAQLQEMRQKHTQaleELTEQLEQAK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 416 -----------------VEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAmLQAHWDEANQL 478
Cdd:pfam01576 370 rnkanlekakqalesenAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSL 448
|
..
gi 1213953200 479 LS 480
Cdd:pfam01576 449 LN 450
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
93-468 |
5.83e-06 |
|
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: 49.97 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 93 DFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVV--------EGWNRHEAER 164
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEiqelqekaESELAKEEIL 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 165 TEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQEsaRLQQRERETLEEERQALTLRLEAEQQRCCVLQEE 244
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELK--LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 245 RDAA----RAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 320
Cdd:pfam02463 774 KELAeereKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 321 SEVRRLEGELdtarrerdaLQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlqdlS 400
Cdd:pfam02463 854 EELERLEEEI---------TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE-----I 919
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953200 401 GQHQQELASQLAQFKVEmaEREERQQQVAEDYELRLAREQARVcelqsgNQQLEEQRVELVERLQAML 468
Cdd:pfam02463 920 EERIKEEAEILLKYEEE--PEELLLEEADEKEKEENNKEEEEE------RNKRLLLAKEELGKVNLMA 979
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
288-470 |
6.41e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 288 QEESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLE 367
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 368 QRVT----ERLAQAQESS--LRQAASLR---EHHRKQLQDlsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRLAR 438
Cdd:COG3883 98 SGGSvsylDVLLGSESFSdfLDRLSALSkiaDADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|..
gi 1213953200 439 EQARVCELQSGNQQLEEQRVELVERLQAMLQA 470
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-467 |
7.72e-06 |
|
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: 49.79 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 101 LDSEHTRRKhCERHIQSLQTRVLELQQQLAVAVAADRKKDtmiEQLDKTLARVVEgwnrHEAERTEVLRGLQE-EHQAAE 179
Cdd:pfam01576 204 QELEKAKRK-LEGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARLEE----ETAQKNNALKKIRElEAQISE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 180 LTRSKQQETVTR-----LEQSLSEAMEALNREQESarlqqreretleeerqalTLRLEAEQQRccvLQEERDaaragqls 254
Cdd:pfam01576 276 LQEDLESERAARnkaekQRRDLGEELEALKTELED------------------TLDTTAAQQE---LRSKRE-------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 255 ehRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTAR 334
Cdd:pfam01576 327 --QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 335 RERDALQLEMSLVQARY---ESQRIQLESELA-VQLE-QRVTERLAQAQESSLRQAASLREHHrKQLQDLSGQHQQE--- 406
Cdd:pfam01576 405 HKRKKLEGQLQELQARLsesERQRAELAEKLSkLQSElESVSSLLNEAEGKNIKLSKDVSSLE-SQLQDTQELLQEEtrq 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213953200 407 ---LASQLAQFKvemAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRVELVERLQAM 467
Cdd:pfam01576 484 klnLSTRLRQLE---DERNSLQEQLEEEEEAKRNVER----QLSTLQAQLSDMKKKLEEDAGTL 540
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-466 |
7.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 142 MIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARlQQRERETLE 221
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELR-EELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 222 EERQALTLRLEAEQQRCCVLQEERDAARAgqlsEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEK 301
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 302 SQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARY----ESQRIQLESELAVQLEQRVT------ 371
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliAAALLALLGLGGSLLSLILTiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 372 --ERLAQAQESSLRQAASLREHHRKQLQDLSGQ---HQQELASQLAQFKVEMAEREERQQQVAEDY-ELRLAREQARVCE 445
Cdd:COG4717 281 lvLGLLALLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIeELQELLREAEELE 360
|
330 340
....*....|....*....|.
gi 1213953200 446 LQSGNQQLEEQRVELVERLQA 466
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGV 381
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
293-480 |
8.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 293 AQLEREKEKSQREAQAAWETQHQLALVQSEVR----RLEGELDTARRERDAL----QLEMSLVQARYES---QRIQLESE 361
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRqqleRLRREREKAERYQALLkekrEYEGYELLKEKEAlerQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 362 LAvQLEQRVTERLAQAQESSLR--QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMA-------EREERQQQVAE-- 430
Cdd:TIGR02169 246 LA-SLEEELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiaEKERELEDAEErl 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1213953200 431 -DYELRLAREQARVCELQsgnQQLEEQRVElVERLQAMLQAHWDEANQLLS 480
Cdd:TIGR02169 325 aKLEAEIDKLLAEIEELE---REIEEERKR-RDKLTEEYAELKEELEDLRA 371
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
148-470 |
9.54e-06 |
|
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: 49.58 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 148 KTLARVVEGWNRHEAERTEVLRGLQ-EEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQA 226
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 227 LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLER-EKEKSQRE 305
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKLERRKVDDEEKLKESEKEKKKaEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 306 AQAAwETQHQLALVQ-SEVRRLEGELDTARRERDALQLEMSLV--QARYESQRIQLESELAVQLEQRVTE--------RL 374
Cdd:pfam02463 335 EEIE-ELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLakKKLESERLSSAAKLKEEELELKSEEekeaqlllEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 375 AQAQESSLR----QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRL-AREQARVCELQSG 449
Cdd:pfam02463 414 ARQLEDLLKeekkEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvKLQEQLELLLSRQ 493
|
330 340
....*....|....*....|.
gi 1213953200 450 NQQLEEQRVELVERLQAMLQA 470
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLA 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
172-463 |
9.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 172 QEEHQAAELTRSKQQETVTRLEQS---------------------------LSEAMEALNREQESARLQQRERETLEEER 224
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAeekaeaaekkkeeakkkadaakkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 225 QALTLRLEAEQQRCC-----VLQEERDAARAGQLSEH-RELETLRAALEEERQTwaqQEHQLKEHYQALQEESQAQLERE 298
Cdd:PTZ00121 1419 KADEAKKKAEEKKKAdeakkKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEA 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 299 KEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSlvQARYESQRIQLESELAVQLEQRVTERLAQAQ 378
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 379 E---SSLRQAASLREHHRKQLQDLSGQHQQElasqlAQFKVEMAEREERQQQVAEdyELRLAREQARVCELQSGNQQLEE 455
Cdd:PTZ00121 1574 EdknMALRKAEEAKKAEEARIEEVMKLYEEE-----KKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEK 1646
|
....*...
gi 1213953200 456 QRVELVER 463
Cdd:PTZ00121 1647 KKAEELKK 1654
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
107-366 |
1.05e-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: 48.97 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 107 RRKHCERHIQSLQTRVLEL--QQQLAVAVAADRKKDTMIEQLDKTLARVvegwnRHEAERTEVLRGLQEEHQAAELTRSK 184
Cdd:pfam17380 346 RERELERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERV-----RQELEAARKVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 185 QQETVtRLEQSLSEAMEALNREQESARLQQRERETLEEERQALT-LRLEAEQQRCCVLQ---EERDAARAGQLSE---HR 257
Cdd:pfam17380 421 EMEQI-RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVErLRQQEEERKRKKLElekEKRDRKRAEEQRRkilEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 258 ELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEgeldtarrer 337
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE---------- 569
|
250 260
....*....|....*....|....*....
gi 1213953200 338 dALQLEMSLVQARYESQRIQLESELAVQL 366
Cdd:pfam17380 570 -AMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-441 |
1.05e-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: 49.18 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 166 EVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALnreQESARLQqreretleeeRQALTLRLEAEQQRCCVLQEER 245
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL---QLLNKLL----------PQANLLADETLADRLEELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 246 DAARAGQ--LSEH----RELETLRAALeeerQTWAQQEHQLKEHYQAL---QEESQAQLEREKEKSQREAQAAWE-TQHQ 315
Cdd:COG3096 903 DAAQEAQafIQQHgkalAQLEPLVAVL----QSDPEQFEQLQADYLQAkeqQRRLKQQIFALSEVVQRRPHFSYEdAVGL 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 316 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES---QRIQLES------ELAVQLEQRVTERLAQAQESSLRQAA 386
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqVLASLKSsrdakqQTLQELEQELEELGVQADAEAEERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953200 387 SlrehHRKQLQDLSGQHQQ---ELASQLAQFKVEMAEREERQQQVAEDYelRLAREQA 441
Cdd:COG3096 1059 I----RRDELHEELSQNRSrrsQLEKQLTRCEAEMDSLQKRLRKAERDY--KQEREQV 1110
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-374 |
1.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 98 RDALDSEHTRRK---HCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARvvegwnrHEAERTEVLRGLQEE 174
Cdd:PRK02224 491 VEEVEERLERAEdlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 175 HQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDaaragqls 254
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE-------- 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 255 EHRELEtlrAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAawetqhqlalVQSEVRRLEgeldTAR 334
Cdd:PRK02224 635 RKRELE---AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA----------VENELEELE----ELR 697
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1213953200 335 RERDALQLEMSLVQARYESQRiQLES---ELAVQLEQRVTERL 374
Cdd:PRK02224 698 ERREALENRVEALEALYDEAE-ELESmygDLRAELRQRNVETL 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-384 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 171 LQEEHQAAEltrsKQQETVTRLEQsLSEAMEALNREQESARLQQReretleeerQALTLRLEAEQQRCCVLQEERDAARA 250
Cdd:COG4913 237 LERAHEALE----DAREQIELLEP-IRELAERYAAARERLAELEY---------LRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 251 gqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLER-EKEKSQREAQAAwETQHQLALVQSEVRRLEGE 329
Cdd:COG4913 303 -------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELE-ERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1213953200 330 LDTARRERDALQLEMSLVQARYESQRIQLESELAvqlEQRVTERLAQAQESSLRQ 384
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEA 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-471 |
1.20e-05 |
|
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: 49.20 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 108 RKHCERHIQSLQTRVLELQQQLA--VAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQ 185
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 186 Q--ETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR 263
Cdd:TIGR00618 386 QqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 264 AALEEERQTWAQQE---------HQLKEHYQALQEESQAQLEREKEKSQREAQAAWET----------QHQLALVQSEVR 324
Cdd:TIGR00618 466 QSLKEREQQLQTKEqihlqetrkKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpltrrmqrgEQTYAQLETSEE 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 325 RLEGELDTARRERDALQLEMSLVQ-------------------ARYESQRIQ----LESELAVQLEQRVTERLAQAQESS 381
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQqsfsiltqcdnrskedipnLQNITVRLQdlteKLSEAEDMLACEQHALLRKLQPEQ 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 382 LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQvaedyELRLAREQARVCELQSGNQQLEEQRVELV 461
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP-----KELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
410
....*....|
gi 1213953200 462 ERLQAMLQAH 471
Cdd:TIGR00618 701 QCQTLLRELE 710
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
292-477 |
1.64e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 292 QAQLEREKEKSqREAQAAWE---TQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAV---- 364
Cdd:COG3206 181 EEQLPELRKEL-EEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 365 ---QLEQRVTERLAQAQESSLRQAASLREHH------RKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEdyelR 435
Cdd:COG3206 260 lqsPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA----Q 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1213953200 436 LAREQARVCELQSGNQQLE--EQRVELVERLQAMLQAHWDEANQ 477
Cdd:COG3206 336 LAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEARL 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
124-399 |
1.83e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 124 ELQQQLAVAVAADRKKdtmIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 203
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 204 NREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagqlsEHRELETLRAALEEERqtwaQQEHQLKEh 283
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEK----KAAEALKK- 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 284 yqalQEESQAQLEREKEKSQREAQAAWETQHqlalvQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELA 363
Cdd:PTZ00121 1697 ----EAEEAKKAEELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270
....*....|....*....|....*....|....*.
gi 1213953200 364 VQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 399
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
94-478 |
2.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 94 FQGLRDALDSEHTRRKhcerhIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVL----R 169
Cdd:COG4913 274 LEYLRAALRLWFAQRR-----LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereiE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 170 GLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCC----VLQEER 245
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelrELEAEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 246 DAARAGQLSEHRELETLRAALEE-----------------------------ER-------------------------- 270
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEalgldeaelpfvgelievrpeeerwrgaiERvlggfaltllvppehyaaalrwvnrl 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 271 ---------------------------------------QTWAQQEhqLKEHYQALQEESQAQLEREK------------ 299
Cdd:COG4913 509 hlrgrlvyervrtglpdperprldpdslagkldfkphpfRAWLEAE--LGRRFDYVCVDSPEELRRHPraitragqvkgn 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 300 ----EKSQREAQAA-----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQ- 368
Cdd:COG4913 587 gtrhEKDDRRRIRSryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASa 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 369 -----RVTERLAQAQESS--LRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREERQQQV---AEDYELRLAR 438
Cdd:COG4913 667 ereiaELEAELERLDASSddLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELqdrLEAAEDLARL 745
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1213953200 439 EQARVCELQSGNQQLEEQRVELVERLQAMLQAHWDEANQL 478
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
116-326 |
3.07e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 116 QSLQTRVLELQQQLAVAVAADRKkdtmIEQLDKTLARVVEGWNRHEAERT--EVLRGLQEE-HQAAELTRSKQQetVTRL 192
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQ----FEQAYQLVRKIAGEVSRSEAWDVarELLRRLREQrHLAEQLQQLRMR--LSEL 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 193 EQSLSEAMEAlNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQT 272
Cdd:PRK04863 526 EQRLRQQQRA-ERLLAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213953200 273 wAQQEHQLKEHYQALQEES--------------QAQLEREKEKSQREAQAAWETQHqlalVQSEVRRL 326
Cdd:PRK04863 602 -APAWLAAQDALARLREQSgeefedsqdvteymQQLLERERELTVERDELAARKQA----LDEEIERL 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-610 |
3.16e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 97 LRDALDSEHTRRKHCERHIQSLQTrvlELQQQLAVAVAADRKKDTMIEQLDKTLARVvegwnrheAERTEVLRGLQEEHQ 176
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLEKVSSLTAQL--------ESTKEMLRKVVEELT 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 177 AAELTRSKQQETVTRLEQSLSEAMEALnrEQESARLQQRERETLEEERQALTLRLEAEQQRCcvLQEERDAARAGQLSEH 256
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAI--EATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 257 RELETLRAALEEERQTWAQQEHQLKehyqALQEEsQAQLEREKEKSQREAQaawetqhqlalvqsEVRRLEGELDTARRE 336
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAG----AMQVE-KAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRE 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 337 RDA----LQLE-MSLVQAryESQRIQLESELAVQLEQRVTErlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQL 411
Cdd:pfam15921 623 LEArvsdLELEkVKLVNA--GSERLRAVKDIKQERDQLLNE--VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 412 AQFKVEMAEREERQQ-------------QVAEDYELRLAREQARVCELQSGNQQLEEQRVElVERLQAMLQAHWDEANQL 478
Cdd:pfam15921 699 MQLKSAQSELEQTRNtlksmegsdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN-ANKEKHFLKEEKNKLSQE 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 479 LSTTlpPPNPPAPPAGPSSPGPQEPEKEERrvwtMPPMAVALKPVLQQSREARD----ELPGAPPVLCSSSSDLSLLLGP 554
Cdd:pfam15921 778 LSTV--ATEKNKMAGELEVLRSQERRLKEK----VANMEVALDKASLQFAECQDiiqrQEQESVRLKLQHTLDVKELQGP 851
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 555 SFQSQHSFQPLEPKP---DLTSSTAGAFSALGAFHPDHRAERPFPEEDPGPDGEGLLKQ 610
Cdd:pfam15921 852 GYTSNSSMKPRLLQPasfTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQE 910
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-355 |
4.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 124 ELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAErtevLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 203
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 204 NREQESARlQQRERETLEEERQALTLRLEAEQqrccVLQEERDAARAGQLSEHR--ELETLRAALEEERQTWAQQEHQLK 281
Cdd:COG4942 100 EAQKEELA-ELLRALYRLGRQPPLALLLSPED----FLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213953200 282 EHYQALQEESQAQLEREKEKSQREAqaawetqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 355
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
255-479 |
4.90e-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: 47.25 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 255 EHRELETLRAALEEERQTWAQQEHQLKEHYQALQ----------EESQAQLEREKEksqREAQAAWETQHQLALVQSEVR 324
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanllaDETLADRLEELR---EELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 325 RLEGELDTARR---ERDALQLEMSLVQARYESQRIQLESelAVQLEQRVT--------ERLAQAQESS------LRQAAS 387
Cdd:COG3096 921 QLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFA--LSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 388 LREHHRKQLQDLSGQHQ---QELAS----------QLAQFKVEMAEREERQQQVAEdyelrlAREQARVCELQSGNQQLE 454
Cdd:COG3096 999 ARREAREQLRQAQAQYSqynQVLASlkssrdakqqTLQELEQELEELGVQADAEAE------ERARIRRDELHEELSQNR 1072
|
250 260
....*....|....*....|....*
gi 1213953200 455 EQRVELvERLQAMLQAHWDEANQLL 479
Cdd:COG3096 1073 SRRSQL-EKQLTRCEAEMDSLQKRL 1096
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-468 |
5.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 112 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV--VEGWNRHEAERTEVLRGLQEEHQAAEltrSKQQETV 189
Cdd:PRK04863 382 EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEEL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 190 TRLEQSLSEAMEALNREQESARLQQreretleeerqaltlRLEAEQQRccvlQEERDAARagqlsehrelETLRAAleEE 269
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVR---------------KIAGEVSR----SEAWDVAR----------ELLRRL--RE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 270 RQTWAQQEHQLKEHYQALQEESQAQleREKEKSQREAQAAWETQHQLAlvqSEVRRLEGELDTarrERDALQLEMSLVQA 349
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDE---DELEQLQEELEA---RLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 350 RYESQRIQLEselavQLEQRVTERLAQAQESSLRQAASlrehhrKQLQDLSGQHqQELASQLAQFKVEMAEREERQQQVA 429
Cdd:PRK04863 580 RRMALRQQLE-----QLQARIQRLAARAPAWLAAQDAL------ARLREQSGEE-FEDSQDVTEYMQQLLERERELTVER 647
|
330 340 350
....*....|....*....|....*....|....*....
gi 1213953200 430 EDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAML 468
Cdd:PRK04863 648 DELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
99-457 |
5.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 99 DALDSEHTRRKHCERHIQSLQtRVLELQQQLAVAVAADRKKdtmIEQLDK--TLARVVEGWNRHEAERTEVLRGLQEEHQ 176
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAAR-KAEEVRKAEELRKAEDARK---AEAARKaeEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 177 AAELTRSKQQETVTRLEQSLSEA-MEALNREQESARLQQREretleeerQALTLRlEAEqqrccvlqEERDAARAGQLSE 255
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEArMAHFARRQAAIKAEEAR--------KADELK-KAE--------EKKKADEAKKAEE 1300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 256 HRELETLRAALEEERQTwaqqehqlkehyqalqEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 335
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKA----------------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 336 ERDALQLEMSLVQARYESQRIQLEselavqlEQRVTERLAQAQESSLRQAASLR--EHHRKQLQDLSGQHQQELASQLAQ 413
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAE-------EKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAK 1437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1213953200 414 FKVEMAEREERQQQVAEDY----ELRLAREQARVCElqSGNQQLEEQR 457
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAkkaeEAKKKAEEAKKAD--EAKKKAEEAK 1483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-430 |
5.29e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 97 LRDALDSEHTRRKH-CERHIQSLQTRVLELQQQLAvavaadrKKDTMIEQLDKTLARVVEgwnRHEAERTEVLRGLQEEH 175
Cdd:TIGR02169 220 KREYEGYELLKEKEaLERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 176 QAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlse 255
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 256 hrELETLRAALEEERqtwaqqehqlKEHYQALQEESQAQLEREKEKSQREaqaawETQHQLALVQSEVRRLEGELdtarr 335
Cdd:TIGR02169 365 --ELEDLRAELEEVD----------KEFAETRDELKDYREKLEKLKREIN-----ELKRELDRLQEELQRLSEEL----- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 336 erdaLQLEMSLvqARYESQRIQLESEL-AVQLEQRvterlaqAQESSLRQAASLREHHRKQLQDLSgQHQQELASQLAQF 414
Cdd:TIGR02169 423 ----ADLNAAI--AGIEAKINELEEEKeDKALEIK-------KQEWKLEQLAADLSKYEQELYDLK-EEYDRVEKELSKL 488
|
330
....*....|....*.
gi 1213953200 415 KVEMAEREERQQQVAE 430
Cdd:TIGR02169 489 QRELAEAEAQARASEE 504
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
313-474 |
6.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 313 QHQLALVQSEVRRLEGELDTARRERDALQLEmsLVQARYESQRIQLESELAVQLEQRVTERLAQAqeSSLRQAASLR--- 389
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQkei 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 390 EHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 469
Cdd:COG1579 99 ESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
....*
gi 1213953200 470 AHWDE 474
Cdd:COG1579 178 ALYER 182
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
97-425 |
8.36e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 97 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAAdrkkdtmIEQLDKTLARVVegwNRHEAERTEVLRGLQEEHQ 176
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA-------LKNARLDLRRLF---DEKQSEKDKKNKALAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 177 AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETL---------EEERQALTLRLEAEQQRCCVLQEERDA 247
Cdd:pfam12128 679 SANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVvegaldaqlALLKAAIAARRSGAKAELKALETWYKR 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 248 ARAGQ-------LSEHRELETLRAALEEErqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 320
Cdd:pfam12128 759 DLASLgvdpdviAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 321 SEVRRLEGELDTARRERDALQLEMS--LVQARYESQRIQL--ESELAVQLEQRVTERLAQAQEsSLRQAASLREHHRKQL 396
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQVRLSenLRGLRCEMSKLATlkEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYV 913
|
330 340
....*....|....*....|....*....
gi 1213953200 397 QDLSGQHQQELASQLAQFKVEMAEREERQ 425
Cdd:pfam12128 914 EHFKNVIADHSGSGLAETWESLREEDHYQ 942
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-340 |
1.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 104 EHTRRKHCERHIQSLqtRVLELQQQLAVAVAADRKKDTMIEQLDKTlarvvegwnRHEAERTEVLRGLQEEHQAAELTRS 183
Cdd:PTZ00121 1572 AEEDKNMALRKAEEA--KKAEEARIEEVMKLYEEEKKMKAEEAKKA---------EEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 184 KQQETVTRLEQSLSEamealnREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAaragqlSEHRELETLR 263
Cdd:PTZ00121 1641 KEAEEKKKAEELKKA------EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA------EEAKKAEELK 1708
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953200 264 AALEEERQTwAQQEHQLKEHYQALQEesqaQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDAL 340
Cdd:PTZ00121 1709 KKEAEEKKK-AEELKKAEEENKIKAE----EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
171-452 |
1.05e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 171 LQEEHQAAELTRSKQQE---------TVTRLEQSLSEAMEALNreqESARLQQRERETLEEERQALTLRLEAEQQRCCVL 241
Cdd:PRK10929 112 LQVSSQLLEKSRQAQQEqdrareisdSLSQLPQQQTEARRQLN---EIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 242 QEERDAAragQLSEH--RELETLRAALEEERQtwaqqeHQLKEHYQALQEESQAQlerekekSQREAQAAWETQHQLAlv 319
Cdd:PRK10929 189 VDELELA---QLSANnrQELARLRSELAKKRS------QQLDAYLQALRNQLNSQ-------RQREAERALESTELLA-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 320 qsevrrlEGELDTARRERDALQLEMSLVQA-RYESQRIQLeseLAVQleqrvtERLAQAQESSLRQAAS-LREHH----- 392
Cdd:PRK10929 251 -------EQSGDLPKSIVAQFKINRELSQAlNQQAQRMDL---IASQ------QRQAASQTLQVRQALNtLREQSqwlgv 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213953200 393 --------RKQLQDLSGQHQ-QELASQLAQFKV------EMAEREERQQQVAEDYELRLAREQARVCELQSGNQQ 452
Cdd:PRK10929 315 snalgealRAQVARLPEMPKpQQLDTEMAQLRVqrlryeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQR 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-387 |
1.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 93 DFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQ 172
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 173 ------EEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERD 246
Cdd:COG4717 280 flvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 247 AARAGQLSEHRELETLRAALE-------EERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQhqLALV 319
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEEL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 320 QSEVRRLEGELDTARRERDALQLEMSLV---------QARYESQRIQLESE--------LAVQLEQRVTERLAQAQESSL 382
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLeedgelaelLQELEELKAELRELaeewaalkLALELLEEAREEYREERLPPV 517
|
....*
gi 1213953200 383 RQAAS 387
Cdd:COG4717 518 LERAS 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-350 |
1.43e-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: 45.44 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 118 LQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEhqaaeltrSKQQETVTRLEQSLS 197
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE--------RKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 198 EAMEALNREQESarlqqreretLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQE 277
Cdd:TIGR02169 364 EELEDLRAELEE----------VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213953200 278 HQLKEhYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR 350
Cdd:TIGR02169 434 AKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-478 |
1.91e-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: 45.05 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 289 EESQAQLEREKEKSQREAQaawetqhqLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLeSELAVQLEQ 368
Cdd:TIGR02168 667 KTNSSILERRREIEELEEK--------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 369 rvterlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVaEDYELRLAREQARVCELQS 448
Cdd:TIGR02168 738 ------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRA 810
|
170 180 190
....*....|....*....|....*....|
gi 1213953200 449 GNQQLEEQRVELVERLQAMLQAHWDEANQL 478
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRL 840
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
151-460 |
2.23e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 151 ARVVEgwnRHEAERTEvLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLR 230
Cdd:PRK10246 187 AMVFE---QHKSARTE-LEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 231 LEAEQQrccVLQEERDAAR----------AGQLSEHRE-LETLRAALEEERQTWAQQEHQLKEHYQALQEESQ-AQLERE 298
Cdd:PRK10246 263 QQALQQ---ALAAEEKAQPqlaalslaqpARQLRPHWErIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHhAAKQSA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 299 KEKSQREAQAAWETQH------------------QLALVQSEVRRLEGELDTARRERDAL-QLEMSLVqaryesqriqlE 359
Cdd:PRK10246 340 ELQAQQQSLNTWLAEHdrfrqwnnelagwraqfsQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLT-----------A 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 360 SELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAedyelrlarE 439
Cdd:PRK10246 409 DEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLA---------D 479
|
330 340
....*....|....*....|.
gi 1213953200 440 QARVCELQSGNQQLEEQRVEL 460
Cdd:PRK10246 480 VKTICEQEARIKDLEAQRAQL 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
225-481 |
2.39e-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: 44.96 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 225 QALTLRLEAEQQrccVLQEERDAARAGQLSEHRELETLRAALEEERQT--WAQQEHQLKEHYQALQEESQAQLEREKEKS 302
Cdd:TIGR00618 197 ELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQShaYLTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 303 QREA-------------QAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQR 369
Cdd:TIGR00618 274 AQEAvleetqerinrarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 370 VTERLAQAQESSLR-----QAASLREHHRKQLQDLSGQHQQE--LASQLAQFKVEMA--------EREERQQQVAEDYEL 434
Cdd:TIGR00618 354 EIHIRDAHEVATSIreiscQQHTLTQHIHTLQQQKTTLTQKLqsLCKELDILQREQAtidtrtsaFRDLQGQLAHAKKQQ 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1213953200 435 RLAREQARVCELQSGNQQLEEQrveLVERLQAMLQAHWDEANQLLST 481
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQT 477
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
97-482 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 97 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAvavaadrKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRglQEEHQ 176
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-------TKEQIHLQETRKKAVVLARLLELQEEPCPLCG--SCIHP 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 177 AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEH 256
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 257 RELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLErEKEKSQREAQA-AWETQHQLALVQSEVR------RLEGE 329
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH-LQQCSQELALKlTALHALQLTLTQERVRehalsiRVLPK 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 330 LDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAAslrehhrkQLQDLSGQ---HQQE 406
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS--------LGSDLAARedaLNQS 744
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 407 LASQLAQFKVEMAEREERQQQVAEDY---ELRLAREQARVCELQSGNQQLEEqRVELVERLQAMLQAHWDEANQLLSTT 482
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVtaaLQTGAELSHLAAEIQFFNRLREE-DTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-309 |
2.83e-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: 43.98 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 112 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLArvvegwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 191
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------AQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 192 LEQSLsEAMEALNREQESarlQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQ 271
Cdd:COG4942 134 AVRRL-QYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 1213953200 272 TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAA 309
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
112-372 |
3.25e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 112 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQ-------LDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSK 184
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQlkeqlqlLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 185 QQETVTRLEQSLSeameALNREQES-ARLQQreretleeERQALTLRLEAEQQRCCVLQE--ERDAA-----RAGQLSEH 256
Cdd:COG3096 915 HGKALAQLEPLVA----VLQSDPEQfEQLQA--------DYLQAKEQQRRLKQQIFALSEvvQRRPHfsyedAVGLLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 257 REL-ETLRAALEEERQTWAQQEHQLKehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 335
Cdd:COG3096 983 SDLnEKLRARLEQAEEARREAREQLR---QAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1213953200 336 ERDALQLEMSLVQAR---YESQRIQLESELAvQLEQRVTE 372
Cdd:COG3096 1060 RRDELHEELSQNRSRrsqLEKQLTRCEAEMD-SLQKRLRK 1098
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
153-309 |
3.54e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 153 VVEGWNRHE-----AERTEVLRGLQEEHQAAELtRSKQQETVTRLEQslseamealnREQESARLQQRERETLEEERQAL 227
Cdd:PRK09510 60 VVEQYNRQQqqqksAKRAEEQRKKKEQQQAEEL-QQKQAAEQERLKQ----------LEKERLAAQEQKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 228 TLRLEAEQQRccvlQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQA---LQEESQAQLERE-KEKSQ 303
Cdd:PRK09510 129 LKQKQAEEAA----AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAkkkAEAEAAAKAAAEaKKKAE 204
|
....*.
gi 1213953200 304 REAQAA 309
Cdd:PRK09510 205 AEAKKK 210
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
315-443 |
4.30e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 315 QLALVQSEVRRLEGELDTARRERDALQ-------------LEMSLVqARYESQRIQLESELAvQLEQRVTE---RLAQAQ 378
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFRnrngildpeataeALLQLI-ATLEGQLAELEAELA-ALRSYLSPnspQVRQLR 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953200 379 esslRQAASLREHHRKQLQDLSGQHQQE-LASQLAQFKVEMAEREERQQQvaedYELRLAR-EQARV 443
Cdd:COG3524 256 ----RRIAALEKQIAAERARLTGASGGDsLASLLAEYERLELEREFAEKA----YTSALAAlEQARI 314
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-457 |
6.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 104 EHTRRKHCERHIQSLQtRVLELQQQLAVAVAADRKKDT-----MIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAA 178
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNeeirkFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 179 ELTRSKQQETVTRLEQSLSEAMEA--LNREQESARlqqreretleeeRQALTLRLEAEqqrccvlqEERDAARAGQLSEH 256
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAK------------KKADAAKKKAE--------EAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 257 RELETLRAALEEERQTWAQQEhqlkehyqalQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGEldtaRRE 336
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKE----------EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA----KKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 337 RDALQLEMSLVQARYESQRIQLESELAVQLEQRVTErlAQAQESSLRQAASLR--EHHRKQLQDLSGQHQQELASQLAQF 414
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKK 1497
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1213953200 415 KVEMAEREERQQQVAEdyELRLAREQARVCELQSGnqqlEEQR 457
Cdd:PTZ00121 1498 KADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKA----EEAK 1534
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
241-378 |
6.93e-04 |
|
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: 42.44 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 241 LQEERDAARAGQLSEHRELETLRAALEEerqtwaqqehqLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 320
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953200 321 SEVRRLEGELdtaRRERDALQLEMSLVQARYESQRIQL---------ESELAVQLEQrVTERLAQAQ 378
Cdd:pfam09787 121 EELRYLEEEL---RRSKATLQSRIKDREAEIEKLRNQLtsksqssssQSELENRLHQ-LTETLIQKQ 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
132-467 |
9.73e-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: 42.85 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 132 AVAADRKKDTMIEQLDKTLARVVEgwNRHEAERTEvlRGLQEEHQaaELTRSKqqETVTRLEQSLSEAMEALNREQESAR 211
Cdd:pfam01576 627 AEAEAREKETRALSLARALEEALE--AKEELERTN--KQLRAEME--DLVSSK--DDVGKNVHELERSKRALEQQVEEMK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 212 LQQRERETLEEERQALTLRLEAEQQRCCVlQEERD-AARAGQLSEHReletlRAALEEERQTWAQQEHQLKEHYQALQEE 290
Cdd:pfam01576 699 TQLEELEDELQATEDAKLRLEVNMQALKA-QFERDlQARDEQGEEKR-----RQLVKQVRELEAELEDERKQRAQAVAAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 291 SQAQLEREKEKSQREA--QAAWETQHQLALVQSEVRRLEGELDTARRERDALqlemsLVQAR--------YESQRIQLES 360
Cdd:pfam01576 773 KKLELDLKELEAQIDAanKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----LAQSKesekklknLEAELLQLQE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 361 ELAV---QLEQRVTER--LAQAQESSLRQAASLREHHRkQLQDLSGQHQQELASQlaQFKVEM-AEREERQQQVAEDYEL 434
Cdd:pfam01576 848 DLAAserARRQAQQERdeLADEIASGASGKSALQDEKR-RLEARIAQLEEELEEE--QSNTELlNDRLRKSTLQVEQLTT 924
|
330 340 350
....*....|....*....|....*....|...
gi 1213953200 435 RLAREQARVCELQSGNQQLEEQRVELVERLQAM 467
Cdd:pfam01576 925 ELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
241-418 |
1.07e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 241 LQEERDAArAGQLSEHRELETLRAALEEERQTWAQQEHQLKEH------YQALQEESQAQLEREKEKSQREAQAAwetqh 314
Cdd:COG1842 39 LVEARQAL-AQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlaREALERKAELEAQAEALEAQLAQLEE----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 315 QLALVQSEVRRLEGELDTARRERDALQlemslvqARYESQRIQ---------LESELAV----QLEQRVTERLAQAQESS 381
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLK-------ARAKAAKAQekvnealsgIDSDDATsaleRMEEKIEEMEARAEAAA 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1213953200 382 -LRQAASLREhhrkQLQDLSGQHqqELASQLAQFKVEM 418
Cdd:COG1842 186 eLAAGDSLDD----ELAELEADS--EVEDELAALKAKM 217
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
99-481 |
1.27e-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: 42.43 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 99 DALDSEHTRRkhCERHIQSLQTRVLELQQQLAvavAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAA 178
Cdd:pfam07111 294 DSLEPEFPKK--CRSLLNRWREKVFALMVQLK---AQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 179 ELTRSkqqeTVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCcvlqeERDAARAGQLSEH-- 256
Cdd:pfam07111 369 EVERM----SAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV-----EQAVARIPSLSNRls 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 257 ---RELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVRRL--EGELD 331
Cdd:pfam07111 440 yavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA-ELQLSAHLIQQEVGRAreQGEAE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 332 TARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQaaslREHHRKQLQDLSGQHQQELASQL 411
Cdd:pfam07111 519 RQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQ----QEIYGQALQEKVAEVETRLREQL 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213953200 412 AQFKVEMAE-REERQQQVAEDYEL--RLAREQARVCELQsgnQQLEEQRVELVERLQAMLQAHWDEANQLLST 481
Cdd:pfam07111 595 SDTKRRLNEaRREQAKAVVSLRQIqhRATQEKERNQELR---RLQDEARKEEGQRLARRVQELERDKNLMLAT 664
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
303-470 |
1.31e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 42.27 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 303 QREAQAAWetQHQLALVQSEVR-RLEGELDTARRER---DALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAq 378
Cdd:pfam04632 158 RARLRARL--RDALRLAAAALAgAPGAEAFEAARLRlaaDILALEALRSHAAFESPRGRARARALRRLLARMLALLPRL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 379 eSSLRQaaslrehHRKQLQDLSGQHQQELASQLAqfkvEMAEREERQQqvAEDYELRLAREQARVCELQSGNQQLEEQRV 458
Cdd:pfam04632 235 -RSLAR-------LLARLRTEGAGTVPELAALLD----ELAAWEAALA--AEALQAALAALRARLRALRPALPLDFDTAA 300
|
170
....*....|..
gi 1213953200 459 ELVERLQAMLQA 470
Cdd:pfam04632 301 ELLARLADLLAE 312
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-317 |
1.74e-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: 41.97 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 111 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEH---QAAELTRSKQQE 187
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaelEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 188 TVTRLEQ---SLSEAMEALNREQESARLQ----QRERETLEEERQALTLRL-EAEQQRCCVLQEERDAARAGQLSEHREL 259
Cdd:TIGR02168 380 QLETLRSkvaQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 260 ETLRAALEEERQTWAQQEHQLKEHYQALQE--ESQAQLEREKEKSQREAQAAWETQHQLA 317
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
107-399 |
1.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 107 RRKHCERHIQSLQTRVLELQQQLAvavAADRKKDTMIEQLD--KTLARVVEGWNRHEAERTEvLRGLQEEHQAAELTRS- 183
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLE---ALEAELDALQERREalQRLAEYSWDEIDVASAERE-IAELEAELERLDASSDd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 184 --KQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELET 261
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 262 LRAALEEERQTWAQQEHQL-----------KEHYQALQEESQAQLER-----------------EKEKSQREAQAAWETQ 313
Cdd:COG4913 767 LRENLEERIDALRARLNRAeeeleramrafNREWPAETADLDADLESlpeylalldrleedglpEYEERFKELLNENSIE 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 314 HQLALVQsevrRLEGELDTARRERDalQLEMSLVQARYESQR-IQLE-SELAVQLEQRVTERLAQAQESSLRQAASLREH 391
Cdd:COG4913 847 FVADLLS----KLRRAIREIKERID--PLNDSLKRIPFGPGRyLRLEaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
....*...
gi 1213953200 392 HRKQLQDL 399
Cdd:COG4913 921 RFAALKRL 928
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
263-376 |
2.38e-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: 38.77 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 263 RAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE---KSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDA 339
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqNYERELVLHAEDIKALQALREELNELKAEIAELKAEAES 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1213953200 340 LQLEMSLVQARYESQRIQLESELAvQLEQRVTERLAQ 376
Cdd:pfam07926 83 AKAELEESEESWEEQKKELEKELS-ELEKRIEDLNEQ 118
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
97-424 |
2.67e-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: 41.49 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 97 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAvAVAADRKKDTMIEQLdktlarvVEGWNRHEAERTEVLRGLQEEHQ 176
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN-RSKEDIPNLQNITVR-------LQDLTEKLSEAEDMLACEQHALL 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 177 -AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE 255
Cdd:TIGR00618 619 rKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 256 HRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR-EAQAAWETQHQ-----------LALVQ--S 321
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARteahfnnneevTAALQtgA 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 322 EVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERlAQAQESSLRQAASLREHHRKQLQDLSG 401
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE-EQFLSRLEEKSATLGEITHQLLKYEEC 857
|
330 340
....*....|....*....|...
gi 1213953200 402 QHQQElasQLAQFKVEMAEREER 424
Cdd:TIGR00618 858 SKQLA---QLTQEQAKIIQLSDK 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
116-377 |
2.77e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 116 QSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKtLARVVEGWNRHEAERTEVLRGLQEEHQAaeltrskqqETVTRLEQS 195
Cdd:COG3096 451 QQATEEVLELEQKLSVADAARRQFEKAYELVCK-IAGEVERSQAWQTARELLRRYRSQQALA---------QRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 196 LSEAMEALNREQESARLQQreretleeerqaltlrleaeqqRCCVLQeerdaarAGQLSEHRELETLRAALEEERQTWAQ 275
Cdd:COG3096 521 LAELEQRLRQQQNAERLLE----------------------EFCQRI-------GQQLDAAEELEELLAELEAQLEELEE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 276 QEHQLKEHYQALQEESQAQLEREKEKSQREaqAAWETqhqlalVQSEVRRLEGELDTARRERDALQLEMSlVQARYESQR 355
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARA--PAWLA------AQDALERLREQSGEALADSQEVTAAMQ-QLLEREREA 642
|
250 260
....*....|....*....|....
gi 1213953200 356 IQLESELAVQLEQ--RVTERLAQA 377
Cdd:COG3096 643 TVERDELAARKQAleSQIERLSQP 666
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
112-358 |
3.37e-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: 40.82 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 112 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQL-----DKT-LARVVEGWNRHEAERTEVLRG----LQEEHQAAElt 181
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELrielrDKTaQAEALERQLAAETEQNRALEEenkaLREEAQAAE-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 182 rskqqETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEaeqqrccvlqeERDAARAGQLSEHRELET 261
Cdd:pfam19220 153 -----KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLA-----------ELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 262 LRAALEEERQtwaQQEHQLKEHYQALQEESQAQLEREKEKSQREA---QAAWETQHQLALVQSEVRRLEGELDTARRERD 338
Cdd:pfam19220 217 QLAAEQAERE---RAEAQLEEAVEAHRAERASLRMKLEALTARAAateQLLAEARNQLRDRDEAIRAAERRLKEASIERD 293
|
250 260
....*....|....*....|
gi 1213953200 339 ALQLEMSLVQARYESQRIQL 358
Cdd:pfam19220 294 TLERRLAGLEADLERRTQQF 313
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
277-442 |
3.43e-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: 39.91 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 277 EHQLKEHYQALQEesqaqLEREKEKSQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRI 356
Cdd:COG1579 23 EHRLKELPAELAE-----LEDELAALEARLEAA---KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 357 QLESELAvqleqrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYE-LR 435
Cdd:COG1579 95 QKEIESL--------KRRISDLEDEILELMERIEELEEELAEL----EAELAELEAELEEKKAELDEELAELEAELEeLE 162
|
....*..
gi 1213953200 436 LAREQAR 442
Cdd:COG1579 163 AEREELA 169
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
297-465 |
4.37e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 297 REKEKSQREAQAAWETQHQLALV------QSEVRRLEGE-LDTARRERDALQLEMslvQARYESQRIQLESELAVQLEQR 369
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVerkrreQEEQRRLQQEqLERAEKMREELELEQ---QRRFEEIRLRKQRLEEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 370 VTERLAQAQESSLRQAASLR-EHHRKQLQDLSGQHQQElasqlaqfkveMAEREERQQQVAEDYELRLAREQARVCELQs 448
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQqEEFRRKLQELQRKKQQE-----------EAERAEAEKQRQKELEMQLAEEQKRLMEMA- 472
|
170
....*....|....*..
gi 1213953200 449 gnqqlEEQRVELVERLQ 465
Cdd:pfam15709 473 -----EEERLEYQRQKQ 484
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
112-392 |
5.17e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 112 ERHIQSLQTRVLELQQQLAVAVAADRKK-DTMIEQLDKTLARVVEGWNRHEAErtevLRGLQEEHQAAEltrsKQQETVT 190
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE----LDNLRLAAEDFR----QKYEDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 191 RLEQSLSEAMEALNREQESARLQQREretleeerqaLTLRLEAEQQRCCVL----QEERDAARAGQLSEHRELET----- 261
Cdd:pfam00038 96 NLRTSAENDLVGLRKDLDEATLARVD----------LEAKIESLKEELAFLkknhEEEVRELQAQVSDTQVNVEMdaark 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 262 --LRAALEEERqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDA 339
Cdd:pfam00038 166 ldLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKAS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1213953200 340 LQLEMSLVQARYESQRIQLESELAvQLEqrvtERLAQAQESSLRQaasLREHH 392
Cdd:pfam00038 243 LERQLAETEERYELQLADYQELIS-ELE----AELQETRQEMARQ---LREYQ 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
168-433 |
5.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 168 LRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDA 247
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 248 ARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLE 327
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 328 GELDTARRERDALqLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQEL 407
Cdd:COG4372 214 RELAEELLEAKDS-LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260
....*....|....*....|....*.
gi 1213953200 408 ASQLAQFKVEMAEREERQQQVAEDYE 433
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALL 318
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-466 |
8.00e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 172 QEEHQAAELTRSKQQETVTRLEQSLSEAmealnrEQESARLQQReretleeeRQALTLRLEAEQQRCCVLQEERD--AAR 249
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKEL------EKKHQQLCEE--------KNALQEQLQAETELCAEAEEMRArlAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 250 AGQLSEhrELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLEREKEKSQReaqaaweTQHQLALVQSEVRRLEGE 329
Cdd:pfam01576 70 KQELEE--ILHELESRLEEEEER-SQQLQNEKKKMQQHIQDLEEQLDEEEAARQK-------LQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 330 LDTARRERDALQLEMSLVQARYESQRIQL--ESELAVQLEQRVT--ERLAQAQESSLRQAASLREHHRKQLQDLSGQ--- 402
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLaeEEEKAKSLSKLKNkhEAMISDLEERLKKEEKGRQELEKAKRKLEGEstd 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1213953200 403 -HQQ--ELASQLAQFKVEMAEREERQQqvaeDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 466
Cdd:pfam01576 220 lQEQiaELQAQIAELRAQLAKKEEELQ----AALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
298-443 |
8.68e-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: 39.33 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213953200 298 EKEKSQREAQAAwETQHQLALVQSEVRRLE---GELDTARRERDALQLEMSLVQARYESQRIQLESelaVQLEQRVTERL 374
Cdd:pfam00529 57 QAALDSAEAQLA-KAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ---AQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1213953200 375 AQAQESSLRQAASLREhHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARV 443
Cdd:pfam00529 133 APIGGISRESLVTAGA-LVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| |
