|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-279 |
1.01e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 12 RLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLkEHYQALQEE 91
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 92 SQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRV 171
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 172 TERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVcELQSGN 251
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEA 472
|
250 260
....*....|....*....|....*...
gi 2462552926 252 QQLEEQRVELVERLQAMLQAHWDEANQL 279
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-311 |
5.08e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR 105
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 106 EAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQ 185
Cdd:COG1196 294 LAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 186 AASLREHHRKQLQDLSGQHQQELASQLAQfkvemaerEERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERL 265
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQ--------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462552926 266 QAMLQAHWDEANQLLSTTLPPPNPQAPPAGPSSPGPQEPEKEERRV 311
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-276 |
9.77e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRccvlQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQL 81
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEEsQAQLEREKEKSQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEmslvQARYESQRIQLES 161
Cdd:COG1196 329 EEELEELEEE-LEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELAEE----LLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 162 ELAVQLEQRvtERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQ 241
Cdd:COG1196 401 QLEELEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270
....*....|....*....|....*....|....*
gi 2462552926 242 ArvcelqsgnQQLEEQRVELVERLQAMLQAHWDEA 276
Cdd:COG1196 479 L---------AELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-271 |
6.21e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEErQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQL 81
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEEsQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLES 161
Cdd:COG1196 368 LEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 162 ELAVQLEQrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQ 241
Cdd:COG1196 447 AAEEEAEL---EEEEEALLELLAELLEEAALLEAALAEL----LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
250 260 270
....*....|....*....|....*....|.
gi 2462552926 242 ARVC-ELQSGNQQLEEQRVELVERLQAMLQA 271
Cdd:COG1196 520 RGLAgAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-270 |
7.01e-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: 72.01 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 3 ALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE--HRELETLRAALEEERQTWAQQEHQ 80
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 81 LkehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLE 160
Cdd:TIGR02168 752 L----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 161 SEL--AVQLEQRVTERLAQAQESSLRQAASlrEHHRKQLQDLSGQHQQELAS---QLAQFKVEMAEREERQQQVAEdyEL 235
Cdd:TIGR02168 828 SLErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSE--EL 903
|
250 260 270
....*....|....*....|....*....|....*
gi 2462552926 236 RLAREQARvcELQSGNQQLEEQRVELVERLQAMLQ 270
Cdd:TIGR02168 904 RELESKRS--ELRRELEELREKLAQLELRLEGLEV 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-270 |
9.72e-12 |
|
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: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 40 CVLQEERDAARAGQLSEH-RELETLRAALEEERQtwaQQEH--QLKEHYQALQEesqAQLEREKEKSQREAQAAWETQHQ 116
Cdd:COG4913 216 YMLEEPDTFEAADALVEHfDDLERAHEALEDARE---QIELlePIRELAERYAA---ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 117 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYEsqriqlesELAVQLEQRVTERLAQAQE--SSLRQAASLREHHR 194
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELD--------ELEAQIRGNGGDRLEQLEReiERLERELEERERRR 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462552926 195 KQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEdyELRLAREQARvcELQSGNQQLEEQRVELVERLQAMLQ 270
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE--ELEALEEALA--EAEAALRDLRRELRELEAEIASLER 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-256 |
7.54e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQL 81
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLES 161
Cdd:COG1196 392 LRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 162 ELAVQLEQRVTERLAQAQESSLRQA-ASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYElrLARE 240
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLlLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL--AAAL 548
|
250
....*....|....*.
gi 2462552926 241 QARVCELQSGNQQLEE 256
Cdd:COG1196 549 QNIVVEDDEVAAAAIE 564
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-268 |
1.53e-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: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQL 81
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEEsqaqLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMslvqARYESQRIQLES 161
Cdd:TIGR02168 802 REALDELRAE----LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI----EELEELIEELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 162 ELAVQLEQR-VTERLAQAQESSLRQAASLREHHRKQLQDLSGQHqQELASQLAQFKVEMAE----REERQQQVAEDYELR 236
Cdd:TIGR02168 874 ELEALLNERaSLEEALALLRSELEELSEELRELESKRSELRREL-EELREKLAQLELRLEGlevrIDNLQERLSEEYSLT 952
|
250 260 270
....*....|....*....|....*....|..
gi 2462552926 237 LAREQARVCELQSGNQQLEEQRVELVERLQAM 268
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-280 |
2.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 20 TLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQAL------QEESQ 93
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanlerqLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 94 AQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR---IQLESELAVQLEQR 170
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 171 vtERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSG 250
Cdd:TIGR02168 403 --ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
250 260 270
....*....|....*....|....*....|..
gi 2462552926 251 NQQLEE--QRVELVERLQAMLQAHWDEANQLL 280
Cdd:TIGR02168 481 ERELAQlqARLDSLERLQENLEGFSEGVKALL 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-265 |
4.09e-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: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 25 RQALTLRLEAEQQRCCVLQEERDAARAgQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQ--AQLEREKEK 102
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDdlAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 103 SQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQRVTERLAQAQES 181
Cdd:COG4913 697 LEAELEEL---EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 182 SLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREE----RQQQVAED--------YELRLAREQARVCELQS 249
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylalLDRLEEDGlpeyeerfKELLNENSIEFVADLLS 853
|
250
....*....|....*.
gi 2462552926 250 gnqQLEEQRVELVERL 265
Cdd:COG4913 854 ---KLRRAIREIKERI 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
48-267 |
2.61e-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: 56.31 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 48 AARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQREAQaawETQHQLALVQSEVRRL 127
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 128 EGELDTARRERDALQLEMS-LVQARYESQRIQ-----LESELAVQLEQRVT--ERLAQAQESSLRQAASLREHHRKQLQD 199
Cdd:COG4942 89 EKEIAELRAELEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 200 LSGQHQQ--ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 267
Cdd:COG4942 169 LEAERAEleALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-279 |
2.82e-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: 57.00 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 29 TLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQ 108
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 109 aawETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAAS 188
Cdd:TIGR02169 748 ---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--IEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 189 LREHHRKQLQDLSgqhqQELASQLAQFKVEMAEREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVEL---VERL 265
Cdd:TIGR02169 823 RLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDEL 894
|
250
....*....|....
gi 2462552926 266 QAMLQAHWDEANQL 279
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-308 |
4.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 57 HRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQA-QLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTAR 135
Cdd:TIGR02168 195 LNELERQLKSLERQAEK-AERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 136 RERDALQLEMSLVQARYESQRIQLeSELAVQLeQRVTERLAQAQESSLRQAASLREHHRK---------QLQDLSGQHQQ 206
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEI-SRLEQQK-QILRERLANLERQLEELEAQLEELESKldelaeelaELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 207 ELASQLAQFKVEMAEREERQQQVaEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQaMLQAHWDEANQLLSTTLPP 286
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKK 429
|
250 260
....*....|....*....|..
gi 2462552926 287 PNPQAPPAGPSSPGPQEPEKEE 308
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-267 |
2.17e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 58 RELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQR--------EAQAAWETQHQLALVQSEVRRLEG 129
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLE-----RLRREREKAERyqallkekREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 130 ELDTARRERDALQLEMSLVQARYESQRIQLEsELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlQDLSGQHQQELA 209
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462552926 210 SQLAQFKVEMaereERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 267
Cdd:TIGR02169 322 ERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-264 |
5.85e-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: 52.76 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 56 EHRELETLRAALE---EERQTWAQQEHQLKEHYQALQEESQAQL-EREKEKSQREAQAAwETQHQLALVQSEVRRLEGEL 131
Cdd:TIGR02169 806 EVSRIEARLREIEqklNRLTLEKEYLEKEIQELQEQRIDLKEQIkSIEKEIENLNGKKE-ELEEELEELEAALRDLESRL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 132 DTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVTERLAQAQEsslrQAASLREHHRKQLQDLSGQHQQELASQ 211
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIE-----KKRKRLSELKAKLEA----LEEELSEIEDPKGEDEEIPEEELSLED 955
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462552926 212 LAQFKVEMAEREERQQQV----AEDYElrlaREQARVCELQSGNQQLEEQRVELVER 264
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVnmlaIQEYE----EVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
4-279 |
7.15e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 4 LNREQESARlQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALE------EERQTWAQQ 77
Cdd:COG3096 336 LNLVQTALR-QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqalDVQQTRAIQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 78 EHQ---------------------LKEHYQALQEESQAQLEREKEKSQR--EAQAAwETQHQLALvqSEVRRLEGELDTA 134
Cdd:COG3096 415 YQQavqalekaralcglpdltpenAEDYLAAFRAKEQQATEEVLELEQKlsVADAA-RRQFEKAY--ELVCKIAGEVERS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 135 RRERDALQLemslvQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDlsgqhQQELASQLAQ 214
Cdd:COG3096 492 QAWQTAREL-----LRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----AEELEELLAE 561
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462552926 215 FKvemAEREERQQQVAEDYELRLAREQARvcelqsgnQQLEEQRVELVERLQAMLQAHwDEANQL 279
Cdd:COG3096 562 LE---AQLEELEEQAAEAVEQRSELRQQL--------EQLRARIKELAARAPAWLAAQ-DALERL 614
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
26-266 |
7.82e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQRCCVLQEERDAARAgqlSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR 105
Cdd:pfam12128 261 SHLHFGYKSDETLIASRQEERQETSA---ELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 106 EAQAAWETQHQLALVQSEVRRLEGELdtarrerDALQLEMSLVQARYESQRIQLESELAVQLEqRVTERLAQAQESSLRQ 185
Cdd:pfam12128 338 DIETAAADQEQLPSWQSELENLEERL-------KALTGKHQDVTAKYNRRRSKIKEQNNRDIA-GIKDKLAKIREARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 186 AASLREHHRKQLQDLSGQHQQ----------ELASQLAQFKVEM----AEREERQQQVAEDYELRLAREQ-----ARVCE 246
Cdd:pfam12128 410 LAVAEDDLQALESELREQLEAgklefneeeyRLKSRLGELKLRLnqatATPELLLQLENFDERIERAREEqeaanAEVER 489
|
250 260
....*....|....*....|
gi 2462552926 247 LQSGNQQLEEQRVELVERLQ 266
Cdd:pfam12128 490 LQSELRQARKRRDQASEALR 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-179 |
8.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 1 MEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagQLSEHRELETLRAALEEERQTWAQQEHQ 80
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 81 LKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLE 160
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|....*....
gi 2462552926 161 SELAVQLEQRVTERLAQAQ 179
Cdd:COG4717 231 QLENELEAAALEERLKEAR 249
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
42-265 |
9.43e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 42 LQEERDAARAGQLSEHRELETLRAALEEERQTW--AQQEHQLKEHYQALQEESQAQL--EREKEKSQREAQAAWETQHQL 117
Cdd:PRK10929 32 LEQAKAAKTPAQAEIVEALQSALNWLEERKGSLerAKQYQQVIDNFPKLSAELRQQLnnERDEPRSVPPNMSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 118 ALVQSEV----RRLEGELDTARRERDALQLemsLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHH 193
Cdd:PRK10929 112 LQVSSQLleksRQAQQEQDRAREISDSLSQ---LPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462552926 194 RKQLQ--DLSGQHQQElasqLAQFKVEMAEReeRQQQVaeDYELRLAREQarvceLQSGNQQLEEQRVELVERL 265
Cdd:PRK10929 189 VDELElaQLSANNRQE----LARLRSELAKK--RSQQL--DAYLQALRNQ-----LNSQRQREAERALESTELL 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-279 |
2.74e-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: 50.15 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 87 ALQEESQAQLEREKEKSQREAQAA----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR---YESQRIQL 159
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELekelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 160 ESELAvQLEQRVTERLAQAQESS--------LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE 231
Cdd:COG4942 96 RAELE-AQKEELAELLRALYRLGrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462552926 232 DYELRLAREQARVCELqsgnQQLEEQRVELVERLQAMLQAHWDEANQL 279
Cdd:COG4942 175 ELEALLAELEEERAAL----EALKAERQKLLARLEKELAELAAELAEL 218
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
9-267 |
2.77e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 9 ESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE-HRELETLRAALEEERQTWAQQEHQLKEHYQA 87
Cdd:pfam12128 340 ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 88 LQEESQAQLEREK-----EKSQREAQAAW------------ETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQA 150
Cdd:pfam12128 420 LESELREQLEAGKlefneEEYRLKSRLGElklrlnqatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 151 RYESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLREHHRKQLQDLSgQHQQELAS--QLAQFKVEMAEREERQQQ 228
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRKEAPDWE-QSIGKVISpeLLHRTDLDPEVWDGSVGG 576
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462552926 229 VAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 267
Cdd:pfam12128 577 ELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
93-278 |
4.86e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 93 QAQLEREKEKSqREAQAAWE---TQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAV---- 165
Cdd:COG3206 181 EEQLPELRKEL-EEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 166 ---QLEQRVTERLAQAQESSLRQAASLREHH------RKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEdyelR 236
Cdd:COG3206 260 lqsPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA----Q 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462552926 237 LAREQARVCELQSGNQQLE--EQRVELVERLQAMLQAHWDEANQ 278
Cdd:COG3206 336 LAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEARL 379
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-281 |
4.93e-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: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELEtlraaLEEERQTWAQQEHQL 81
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE-----KEEEKLAQVLKENKE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEESQAQLEREKEKSQREAQAAWETQH----QLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRI 157
Cdd:pfam02463 277 EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVddeeKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 158 QLESELAVQL--EQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQfKVEMAEREERQQQVAEDYEL 235
Cdd:pfam02463 357 EEEELEKLQEklEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR-QLEDLLKEEKKEELEILEEE 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462552926 236 RLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHWDEANQLLS 281
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
4-279 |
8.24e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 4 LNREQEsARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALE------EERQTWAQQ 77
Cdd:PRK04863 337 LNLVQT-ALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqalDVQQTRAIQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 78 EHQLKehyQALQEESQ-------------AQLEREKEKSQREAQAAWETQHQLALVQ----------SEVRRLEGELDTA 134
Cdd:PRK04863 416 YQQAV---QALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayQLVRKIAGEVSRS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 135 RRERDALQLEmslvqARYESQRIQleselAVQLEQRvterlaQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQlAQ 214
Cdd:PRK04863 493 EAWDVARELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DE 555
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462552926 215 FKVEMAEREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHwDEANQL 279
Cdd:PRK04863 556 LEQLQEELEARL----ESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ-DALARL 615
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-195 |
8.63e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 7 EQESARLQQRERETLEEERQALTLRLEAEQQRCC-------------VLQEERDAARAgQLSEHR----ELETLRAALEE 69
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaeleekleELKEELESLEA-ELEELEaeleELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 70 ERQTWAQQEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQHQL--ALVQSEVRRLEGELDTARRERDALQLEMSL 147
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELER 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462552926 148 VQARYESQRIQLEselavQLEQRVTERLAQAQESSLRQAA--SLREHHRK 195
Cdd:TIGR02168 459 LEEALEELREELE-----EAEQALDAAERELAQLQARLDSleRLQENLEG 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
94-281 |
9.71e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 94 AQLEREKEKSQREAQAAWETQHQLALVQSEVR----RLEGELDTARRERDAL----QLEMSLVQARYES---QRIQLESE 162
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRqqleRLRREREKAERYQALLkekrEYEGYELLKEKEAlerQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 163 LAvQLEQRVTERLAQAQESSLR--QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMA-------EREERQQQVAE-- 231
Cdd:TIGR02169 246 LA-SLEEELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiaEKERELEDAEErl 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462552926 232 -DYELRLAREQARVCELQsgnQQLEEQRVElVERLQAMLQAHWDEANQLLS 281
Cdd:TIGR02169 325 aKLEAEIDKLLAEIEELE---REIEEERKR-RDKLTEEYAELKEELEDLRA 371
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
81-258 |
1.07e-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: 48.68 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 81 LKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLAlvqsevRRLEGELDTARRERDALQLEMSLVQARYESQRIQL- 159
Cdd:pfam12128 583 VKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQ------AAAEEQLVQANGELEKASREETFARTALKNARLDLr 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 160 -----ESELAVQLEQRVTERLAQAQESsLRQAAslrehhrKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYE 234
Cdd:pfam12128 657 rlfdeKQSEKDKKNKALAERKDSANER-LNSLE-------AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD 728
|
170 180
....*....|....*....|....*...
gi 2462552926 235 LRLAREQARVCELQSGN----QQLEEQR 258
Cdd:pfam12128 729 AQLALLKAAIAARRSGAkaelKALETWY 756
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-225 |
1.11e-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: 48.22 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQL 81
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEESQAQLEREKEKSQREAQAAwetqHQLALVQSEVRRLEGELDTARRERDALQlemsLVQARYESQRIQLES 161
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELA----ALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462552926 162 ELAVQLEQRVT-ERLAQAQESSLRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREER 225
Cdd:COG4942 179 LLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
89-271 |
1.26e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 89 QEESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLE 168
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 169 QRVT----ERLAQAQESS--LRQAASLR---EHHRKQLQDlsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRLAR 239
Cdd:COG3883 98 SGGSvsylDVLLGSESFSdfLDRLSALSkiaDADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|..
gi 2462552926 240 EQARVCELQSGNQQLEEQRVELVERLQAMLQA 271
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-279 |
1.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 111 WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQ------RVTERLAQAQESS- 182
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASaereiaELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 183 -LRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREERQQQV---AEDYELRLAREQARVCELQSGNQQLEEQR 258
Cdd:COG4913 686 dLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELqdrLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|.
gi 2462552926 259 VELVERLQAMLQAHWDEANQL 279
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-185 |
3.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 7 EQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlsehrELETLRAALEEERQTWAQQEHQLKEHYQ 86
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA-------ELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 87 ALQEESQAQLER-EKEKSQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAv 165
Cdd:COG4913 331 QIRGNGGDRLEQlEREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA- 408
|
170 180
....*....|....*....|
gi 2462552926 166 qlEQRVTERLAQAQESSLRQ 185
Cdd:COG4913 409 --EAEAALRDLRRELRELEA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-279 |
3.60e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCV------LQEERDAARAGQLSEHRELETLRAAlEEERQtwA 75
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeakkaAEAKKKADEAKKAEEAKKADEAKKA-EEAKK--A 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 76 QQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEV-RRLEGELDTARRERDALQLEMSLVQARY-E 153
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKaE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 154 SQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLR---EHHRKQLQDLSGQHQQElasqlaQFKVEMAEREERQQQVA 230
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKAEED------KKKAEEAKKAEEDEKKA 1690
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462552926 231 EDYELRLAREQARVCELqsgnQQLEEQRVELVERLQAMLQAHWDEANQL 279
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
98-267 |
3.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 98 REKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQ 177
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 178 AQES--SLRQAASLREHHRKQLQDLSGQH---QQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQ 252
Cdd:COG4717 144 LPERleELEERLEELRELEEELEELEAELaelQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*
gi 2462552926 253 QLEEQRVELVERLQA 267
Cdd:COG4717 224 ELEEELEQLENELEA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3-268 |
4.07e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 3 ALNREQESARLQQRERETLEEERQALTLRLEAE------------QQRCCVLQEERDAARAGQLSEHRELETLRAALEEE 70
Cdd:pfam17380 343 AMERERELERIRQEERKRELERIRQEEIAMEISrmrelerlqmerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 71 RQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQreaqaawETQHQLA-LVQSEVRRLEGELDTARRERDalqlemslvQ 149
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERAREMERVRLEEQ-------ERQQQVErLRQQEEERKRKKLELEKEKRD---------R 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 150 ARYESQRIQLeselavqLEQRVTERlaqaqesslRQAASLREHHRKQLQDlsgqhqqelasqlaqfkvemaEREERQQQV 229
Cdd:pfam17380 487 KRAEEQRRKI-------LEKELEER---------KQAMIEEERKRKLLEK---------------------EMEERQKAI 529
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462552926 230 AEDYELRLAREQARVCELQSGNQQLEEQRVELVE---RLQAM 268
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQMRKATEersRLEAM 571
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
56-280 |
4.20e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 56 EHRELETLRAALEEERQTWAQQEHQLKEHYQALQ----------EESQAQLEREKEksqREAQAAWETQHQLALVQSEVR 125
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanllaDETLADRLEELR---EELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 126 RLEGELDTARR---ERDALQLEMSLVQARYESQRIQLESelAVQLEQRVT--------ERLAQAQESS------LRQAAS 188
Cdd:COG3096 921 QLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFA--LSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 189 LREHHRKQLQDLSGQHQ---QELAS----------QLAQFKVEMAEREERQQQVAEdyelrlAREQARVCELQSGNQQLE 255
Cdd:COG3096 999 ARREAREQLRQAQAQYSqynQVLASlkssrdakqqTLQELEQELEELGVQADAEAE------ERARIRRDELHEELSQNR 1072
|
250 260
....*....|....*....|....*
gi 2462552926 256 EQRVELvERLQAMLQAHWDEANQLL 280
Cdd:COG3096 1073 SRRSQL-EKQLTRCEAEMDSLQKRL 1096
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-258 |
6.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAAlEEERQTwaqQEHQL 81
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA-EEKKKA---DEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEs 161
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE- 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 162 elavqlEQRVTERLAQAQESSLRQAASLR--EHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDY----EL 235
Cdd:PTZ00121 1389 ------EKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeEA 1462
|
250 260
....*....|....*....|...
gi 2462552926 236 RLAREQARVCElqSGNQQLEEQR 258
Cdd:PTZ00121 1463 KKKAEEAKKAD--EAKKKAEEAK 1483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-279 |
6.91e-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: 46.21 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 22 EEERQALTLRLEAEQQRCCVLQEERDaaragqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE 101
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLE-----------ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 102 KSQREAQaawETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQEs 181
Cdd:TIGR02169 319 DAEERLA---KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR--DELKDYRE- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 182 SLRQAASLREHHRKQLQDLsGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVEL 261
Cdd:TIGR02169 393 KLEKLKREINELKRELDRL-QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
250
....*....|....*...
gi 2462552926 262 vERLQAMLQAHWDEANQL 279
Cdd:TIGR02169 472 -YDLKEEYDRVEKELSKL 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
26-180 |
1.07e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHyQALQEESQAQLERekEKSQR 105
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGN--VRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 106 EAQAAwetQHQLALVQSEVRRLE-------GELDTARRERDALQLEMSLVQARYESQRIQLESELAvQLEQRVTERLAQA 178
Cdd:COG1579 90 EYEAL---QKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKAELDEELA-ELEAELEELEAER 165
|
..
gi 2462552926 179 QE 180
Cdd:COG1579 166 EE 167
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2-246 |
1.70e-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: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQ--------EERDAARAGQLSEHRELETLRAALEEERQT 73
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 74 WAQQEHQLKEHYQALQ----EESQAQLEREKEKSQRE--AQAAWETQHQLALvQSEVRRLEGELDTARRERDALQLEMSL 147
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIREisCQQHTLTQHIHTL-QQQKTTLTQKLQSLCKELDILQREQAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 148 VQARYESQRIqLESELAV-----QLEQRVTERLAQAQESSLrQAASLREHHRKQLQdlsgQHQQELASQLAQFKVeMAER 222
Cdd:TIGR00618 412 IDTRTSAFRD-LQGQLAHakkqqELQQRYAELCAAAITCTA-QCEKLEKIHLQESA----QSLKEREQQLQTKEQ-IHLQ 484
|
250 260
....*....|....*....|....
gi 2462552926 223 EERQQQVAEDYELRLAREQARVCE 246
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-279 |
1.78e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 90 EESQAQLEREKEKSQREAQaawetqhqLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLeSELAVQLEQ 169
Cdd:TIGR02168 667 KTNSSILERRREIEELEEK--------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 170 rvterlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVaEDYELRLAREQARVCELQS 249
Cdd:TIGR02168 738 ------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRA 810
|
170 180 190
....*....|....*....|....*....|
gi 2462552926 250 GNQQLEEQRVELVERLQAMLQAHWDEANQL 279
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRL 840
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
116-244 |
2.16e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 44.07 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 116 QLALVQSEVRRLEGELDTARRERDALQ-------------LEMSLVqARYESQRIQLESELAvQLEQRVTE---RLAQAQ 179
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFRnrngildpeataeALLQLI-ATLEGQLAELEAELA-ALRSYLSPnspQVRQLR 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462552926 180 esslRQAASLREHHRKQLQDLSGQHQQE-LASQLAQFKVEMAEREERQQQvaedYELRLAR-EQARV 244
Cdd:COG3524 256 ----RRIAALEKQIAAERARLTGASGGDsLASLLAEYERLELEREFAEKA----YTSALAAlEQARI 314
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
86-282 |
3.19e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 86 QALQEESQ-AQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDtaRRerdaLQLEMSLVQARYESQRIQLESElA 164
Cdd:PRK10929 110 EILQVSSQlLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIE--RR----LQTLGTPNTPLAQAQLTALQAE-S 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 165 VQLEQRVTE-RLAQAQESSLRQAASLR-EHHRKQLQDLSGQhQQELASQLAQFKVEMAERE-ERQQQVAEDY-------- 233
Cdd:PRK10929 183 AALKALVDElELAQLSANNRQELARLRsELAKKRSQQLDAY-LQALRNQLNSQRQREAERAlESTELLAEQSgdlpksiv 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462552926 234 -ELRLAREQArvcelQSGNQQleEQRVELVERLQAMLQAHWDEANQLLST 282
Cdd:PRK10929 262 aQFKINRELS-----QALNQQ--AQRMDLIASQQRQAASQTLQVRQALNT 304
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-214 |
3.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 1 MEALNREQESARLQQRERETlEEERQALTLRLEAEQQRCCVLQEERDAARAGQlsEHRELETLRAALEEERQTWAQQEHQ 80
Cdd:COG4913 234 FDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 81 LKEhyqaLQEESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERD-------ALQLEMSLVQARYE 153
Cdd:COG4913 311 LER----LEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRArleallaALGLPLPASAEEFA 383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462552926 154 SQRIQLESELAV--QLEQRVTERLAQAqESSLRQAASLREHHRKQLQDLSG------QHQQELASQLAQ 214
Cdd:COG4913 384 ALRAEAAALLEAleEELEALEEALAEA-EAALRDLRRELRELEAEIASLERrksnipARLLALRDALAE 451
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
26-282 |
3.63e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQrccVLQEERDAARAGQLSEHRELETLRAALEEERQT--WAQQEHQLKEHYQALQEESQAQLEREKEKS 103
Cdd:TIGR00618 197 ELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQShaYLTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 104 QREA-------------QAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQR 170
Cdd:TIGR00618 274 AQEAvleetqerinrarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 171 VTERLAQAQESSLR-----QAASLREHHRKQLQDLSGQHQQE--LASQLAQFKVEMA--------EREERQQQVAEDYEL 235
Cdd:TIGR00618 354 EIHIRDAHEVATSIreiscQQHTLTQHIHTLQQQKTTLTQKLqsLCKELDILQREQAtidtrtsaFRDLQGQLAHAKKQQ 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462552926 236 RLAREQARVCELQSGNQQLEEQrveLVERLQAMLQAHWDEANQLLST 282
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQT 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
26-242 |
3.66e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQRCCVLQEERDAARAGQ--LSEH----RELETLRAALeeerQTWAQQEHQLKEHYQAL---QEESQAQL 96
Cdd:COG3096 882 QANLLADETLADRLEELREELDAAQEAQafIQQHgkalAQLEPLVAVL----QSDPEQFEQLQADYLQAkeqQRRLKQQI 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 97 EREKEKSQREAQAAWE-TQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES---QRIQLES------ELAVQ 166
Cdd:COG3096 958 FALSEVVQRRPHFSYEdAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqVLASLKSsrdakqQTLQE 1037
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462552926 167 LEQRVTERLAQAQESSLRQAASlrehHRKQLQDLSGQHQQ---ELASQLAQFKVEMAEREERQQQVAEDYelRLAREQA 242
Cdd:COG3096 1038 LEQELEELGVQADAEAEERARI----RRDELHEELSQNRSrrsQLEKQLTRCEAEMDSLQKRLRKAERDY--KQEREQV 1110
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-277 |
3.87e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 42 LQEERDAARAGQLSEHRELETLRAALEEERQTWAQ-------QEHQLKEHYQALQE--ESQAQLEREKEKSqREAQAAWE 112
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEdrERVEELEAELEDL-EEEVEEVE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 113 TQHQLAlvqSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLES--ELAVQLEQRVTERLAQAQEssLRQAAslr 190
Cdd:PRK02224 496 ERLERA---EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEElrERAAELEAEAEEKREAAAE--AEEEA--- 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 191 EHHRKQLQDLSGQhQQELASQLaqfkvEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAmLQ 270
Cdd:PRK02224 568 EEAREEVAELNSK-LAELKERI-----ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE-LE 640
|
....*..
gi 2462552926 271 AHWDEAN 277
Cdd:PRK02224 641 AEFDEAR 647
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
31-281 |
4.54e-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: 43.63 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 31 RLEAE----QQRCCVLQEERDAARAGQLSEHRELETLRAALEEERqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQRE 106
Cdd:pfam01576 212 KLEGEstdlQEQIAELQAQIAELRAQLAKKEEELQAALARLEEET---AQKNNALKKIRELEAQISELQEDLESERAARN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 107 AqaawetqhqlalVQSEVRRLEGELDTARRERDAlQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEsslrqa 186
Cdd:pfam01576 289 K------------AEKQRRDLGEELEALKTELED-TLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQE------ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 187 asLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQ---------QQVAEDYELRLAREQARVCELQSGNQQLEEQ 257
Cdd:pfam01576 350 --MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelqaelrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
250 260
....*....|....*....|....
gi 2462552926 258 RVELVERLQAmLQAHWDEANQLLS 281
Cdd:pfam01576 428 RAELAEKLSK-LQSELESVSSLLN 450
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
59-269 |
4.68e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 59 ELETLRAALEEERQTWAQQEHQL-------KEHYQALQ---------EESQA-QLEREKEKSQREAQAAWETQHQLALVQ 121
Cdd:COG3096 442 YLAAFRAKEQQATEEVLELEQKLsvadaarRQFEKAYElvckiagevERSQAwQTARELLRRYRSQQALAQRLQQLRAQL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 122 SEVRRLEGELDTARRERDALQL----------EMSLVQARYESQRIQLESELAVQLEQRVTER----LAQAQESSLRQAA 187
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQrigqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRqqleQLRARIKELAARA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 188 SLREHHRKQLQDLSGQHQQELAS--QLAQFKVEMAEReERQQQVAEDyELRLAREQ--ARVCELQSGNQQLEEQRVELVE 263
Cdd:COG3096 602 PAWLAAQDALERLREQSGEALADsqEVTAAMQQLLER-EREATVERD-ELAARKQAleSQIERLSQPGGAEDPRLLALAE 679
|
....*.
gi 2462552926 264 RLQAML 269
Cdd:COG3096 680 RLGGVL 685
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
42-179 |
5.33e-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: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 42 LQEERDAARAGQLSEHRELETLRAALEEerqtwaqqehqLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 121
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462552926 122 SEVRRLEGELdtaRRERDALQLEMSLVQARYESQRIQL---------ESELAVQLEQrVTERLAQAQ 179
Cdd:pfam09787 121 EELRYLEEEL---RRSKATLQSRIKDREAEIEKLRNQLtsksqssssQSELENRLHQ-LTETLIQKQ 183
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
104-271 |
6.68e-04 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 42.66 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 104 QREAQAAWetQHQLALVQSEVR-RLEGELDTARRER---DALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAq 179
Cdd:pfam04632 158 RARLRARL--RDALRLAAAALAgAPGAEAFEAARLRlaaDILALEALRSHAAFESPRGRARARALRRLLARMLALLPRL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 180 eSSLRQaaslrehHRKQLQDLSGQHQQELASQLAqfkvEMAEREERQQqvAEDYELRLAREQARVCELQSGNQQLEEQRV 259
Cdd:pfam04632 235 -RSLAR-------LLARLRTEGAGTVPELAALLD----ELAAWEAALA--AEALQAALAALRARLRALRPALPLDFDTAA 300
|
170
....*....|..
gi 2462552926 260 ELVERLQAMLQA 271
Cdd:pfam04632 301 ELLARLADLLAE 312
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-275 |
1.02e-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: 41.06 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 116 QLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLE------SELAVQLEQrVTERLAQAQE-----SSLR 184
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEdlekeiKRLELEIEE-VEARIKKYEEqlgnvRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 185 QAASLR---EHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVEL 261
Cdd:COG1579 90 EYEALQkeiESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
170
....*....|....
gi 2462552926 262 VERLQAMLQAHWDE 275
Cdd:COG1579 169 AAKIPPELLALYER 182
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-278 |
1.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 43 QEERDAARAGQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ- 121
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKk 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 122 -SEVRRLEGELDTARRE--RDALQL----EMSLVQARYESQRIQLESELAVQL-----EQRVTERLAQAQESSLRQAASL 189
Cdd:PTZ00121 1628 aEEEKKKVEQLKKKEAEekKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAkkaeeDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 190 RehhRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDyELRLAREQARvcELQSGNQQLEEQRVELVERLQAML 269
Cdd:PTZ00121 1708 K---KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKK--KIAHLKKEEEKKAEEIRKEKEAVI 1781
|
....*....
gi 2462552926 270 QAHWDEANQ 278
Cdd:PTZ00121 1782 EEELDEEDE 1790
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
43-267 |
1.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 43 QEERDAARAGQLSEHRE-LETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEK------SQREAQAAwETQH 115
Cdd:PRK02224 459 QPVEGSPHVETIEEDRErVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREdleeliAERRETIE-EKRE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 116 QLALVQSEVRRLEGELDTARRERDALQLEMSLVQ---ARYESQRIQLESELAvQLEqRVTERLAQAQEssLRQAASLREH 192
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKLAELKERIE-SLE-RIRTLLAAIAD--AEDEIERLRE 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462552926 193 HRKQLQDLSGQHQQELAsqlaqfkvemaEREERQQQVAEDYElrlareQARVCELQSGNQQLEEQRVELVERLQA 267
Cdd:PRK02224 614 KREALAELNDERRERLA-----------EKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-214 |
1.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 42 LQEERDAARAgQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQA--------QLEREKEKSQREAQAAWET 113
Cdd:COG4717 76 LEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqeleALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 114 QHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvTERLAQAQESslrqaaslREHH 193
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL-EEELEEAQEE--------LEEL 225
|
170 180
....*....|....*....|..
gi 2462552926 194 RKQLQDLSGQHQ-QELASQLAQ 214
Cdd:COG4717 226 EEELEQLENELEaAALEERLKE 247
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
42-219 |
1.35e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 42 LQEERDAArAGQLSEHRELETLRAALEEERQTWAQQEHQLKEH------YQALQEESQAQLEREKEKSQREAQAAwetqh 115
Cdd:COG1842 39 LVEARQAL-AQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlaREALERKAELEAQAEALEAQLAQLEE----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 116 QLALVQSEVRRLEGELDTARRERDALQlemslvqARYESQRIQ---------LESELAV----QLEQRVTERLAQAQESS 182
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLK-------ARAKAAKAQekvnealsgIDSDDATsaleRMEEKIEEMEARAEAAA 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462552926 183 -LRQAASLREhhrkQLQDLSGQHqqELASQLAQFKVEM 219
Cdd:COG1842 186 eLAAGDSLDD----ELAELEADS--EVEDELAALKAKM 217
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
3-261 |
1.46e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 3 ALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVL-QEERDAARAGQLSEHRELET-LRAALEEERQTWAQQEHQ 80
Cdd:PRK10246 258 EASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWErIQEQSAALAHTRQQIEEVNTrLQSTMALRARIRHHAAKQ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 81 LKEHYQALQEESQAQLEREKEKSQREAQAAWETQ-HQLALVQSEVRRLEGELDTARRERDAL-QLEMSLVqaryesqriq 158
Cdd:PRK10246 338 SAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLT---------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 159 lESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAedyelrla 238
Cdd:PRK10246 408 -ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLA-------- 478
|
250 260
....*....|....*....|...
gi 2462552926 239 rEQARVCELQSGNQQLEEQRVEL 261
Cdd:PRK10246 479 -DVKTICEQEARIKDLEAQRAQL 500
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-264 |
1.51e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRA----ALEEERQTWAQQ 77
Cdd:pfam02463 693 EILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRlkkeEKEEEKSELSLK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 78 EHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRE----RDALQLEMSLVQARYE 153
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEeeleELALELKEEQKLEKLA 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 154 SQRIQLESELAVQLEQR----VTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQV 229
Cdd:pfam02463 853 EEELERLEEEITKEELLqellLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
250 260 270
....*....|....*....|....*....|....*
gi 2462552926 230 AEDYELRLAREQARVCELQSGNQQLEEQRVELVER 264
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-141 |
1.96e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 1 MEALNREQESARLQQRERETLEEERQALTLRLEAEQQRccVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQ 80
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE--AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462552926 81 LKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRR--LEGELDTARRERDAL 141
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLeeLERELERLEREIEAL 779
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
26-270 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQRCCVLQEERDAARAGQLSE---HRELETLraALEEERQTWAQQEHQlkehyqalQEESQAQLEREKEK 102
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLtalHALQLTL--TQERVREHALSIRVL--------PKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 103 SQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESS 182
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 183 LR-QAASLREHHRKQLQDLSG--QHQQELASQLAQfkvEMAEREERQQQVAEDYEL-RLAREQARVCELQSGNQQLEEQR 258
Cdd:TIGR00618 765 NNnEEVTAALQTGAELSHLAAeiQFFNRLREEDTH---LLKTLEAEIGQEIPSDEDiLNLQCETLVQEEEQFLSRLEEKS 841
|
250
....*....|..
gi 2462552926 259 VELVERLQAMLQ 270
Cdd:TIGR00618 842 ATLGEITHQLLK 853
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-267 |
2.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQE-ERDAARAGQLSEH-RELETLRAALEEERQTWAQQEH 79
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERlEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 80 QLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARY----ESQ 155
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliAAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 156 RIQLESELAVQLEQRVT--------ERLAQAQESSLRQAASLREHHRKQLQDLSGQ---HQQELASQLAQFKVEMAEREE 224
Cdd:COG4717 258 LLALLGLGGSLLSLILTiagvlflvLGLLALLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPE 337
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462552926 225 RQQQVAEDY-ELRLAREQARVCELQSGNQQLEEQRVELVERLQA 267
Cdd:COG4717 338 ELLELLDRIeELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
64-177 |
2.66e-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: 38.39 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 64 RAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE---KSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDA 140
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqNYERELVLHAEDIKALQALREELNELKAEIAELKAEAES 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462552926 141 LQLEMSLVQARYESQRIQLESELAvQLEQRVTERLAQ 177
Cdd:pfam07926 83 AKAELEESEESWEEQKKELEKELS-ELEKRIEDLNEQ 118
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
22-312 |
3.33e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 22 EEERQALT-----------LRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQE 90
Cdd:pfam02463 172 KEALKKLIeetenlaeliiDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 91 E---SQAQLEREKEKSQR-------EAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR--------- 151
Cdd:pfam02463 252 EiesSKQEIEKEEEKLAQvlkenkeEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEkkkaekelk 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 152 -YESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQfkvEMAEREERQQQVA 230
Cdd:pfam02463 332 kEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE---ELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 231 EDYELRLAREQARVCELQSGNQQLEEQRvELVERLQAMLQAHWDEANQLLSTTLPPPNPQAPPAGPSSPGPQEPEKEERR 310
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEE-ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
..
gi 2462552926 311 VW 312
Cdd:pfam02463 488 LL 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-268 |
3.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 26 QALTLRLEAEQQRCCVLQEERDAARAG--QLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKS 103
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 104 QREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEssl 183
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE--- 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 184 RQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREqarvcelqsgnQQLEEQRVELVE 263
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL-----------EELERELERLER 774
|
....*
gi 2462552926 264 RLQAM 268
Cdd:COG1196 775 EIEAL 779
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
30-261 |
4.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 30 LRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEE---SQAQLEREKEKSQRE 106
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEleqLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 107 AQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES--QRIQLESELAVQLEQRVTERLAQAQESSLR 184
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAElqSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462552926 185 QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVEL 261
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-269 |
4.23e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 2 EALNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQL 81
Cdd:pfam02463 737 ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE---KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 82 KEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELdtarrerdaLQLEMSLVQARYESQRIQLES 161
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI---------TKEELLQELLLKEEELEEQKL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 162 ELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlqdlSGQHQQELASQLAQFKVEmaEREERQQQVAEDYELRLAREQ 241
Cdd:pfam02463 885 KDELESKEEKEKEEKKELEEESQKLNLLEEKENE-----IEERIKEEAEILLKYEEE--PEELLLEEADEKEKEENNKEE 957
|
250 260
....*....|....*....|....*...
gi 2462552926 242 ARVcelqsgNQQLEEQRVELVERLQAML 269
Cdd:pfam02463 958 EEE------RNKRLLLAKEELGKVNLMA 979
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1-167 |
4.77e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 1 MEALNREQESAR--------------LQQRERETLEEERQALTLRLEAEQQRCCVLQ---EERDAARAGQLSE---HREL 60
Cdd:pfam17380 422 MEQIRAEQEEARqrevrrleeerareMERVRLEEQERQQQVERLRQQEEERKRKKLElekEKRDRKRAEEQRRkilEKEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 61 ETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEgeldtarrerdA 140
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-----------A 570
|
170 180
....*....|....*....|....*..
gi 2462552926 141 LQLEMSLVQARYESQRIQLESELAVQL 167
Cdd:pfam17380 571 MEREREMMRQIVESEKARAEYEATTPI 597
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
99-244 |
5.34e-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: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 99 EKEKSQREAQAAwETQHQLALVQSEVRRLE---GELDTARRERDALQLEMSLVQARYESQRIQLESelaVQLEQRVTERL 175
Cdd:pfam00529 57 QAALDSAEAQLA-KAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ---AQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462552926 176 AQAQESSLRQAASLREhHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARV 244
Cdd:pfam00529 133 APIGGISRESLVTAGA-LVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-265 |
5.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 31 RLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQaQLEREKEKSQREAQAA 110
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE-EAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 111 WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLE-----SELAVQLEQRVTERLAQAqESSLRQ 185
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfLEELREERDELREREAEL-EATLRT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 186 AASLREHHRKQL---------QDLSG-----------QHQQELASQLAQFKVEMAEREERQQQVAEdyelrlareqarVC 245
Cdd:PRK02224 438 ARERVEEAEALLeagkcpecgQPVEGsphvetieedrERVEELEAELEDLEEEVEEVEERLERAED------------LV 505
|
250 260
....*....|....*....|
gi 2462552926 246 ELQSGNQQLEEQRVELVERL 265
Cdd:PRK02224 506 EAEDRIERLEERREDLEELI 525
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-268 |
5.77e-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: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 30 LRLEAEQQRCCVlQEERD-AARAGQLSEHReletlRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREA- 107
Cdd:pfam01576 716 LRLEVNMQALKA-QFERDlQARDEQGEEKR-----RQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAa 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 108 -QAAWETQHQLALVQSEVRRLEGELDTARRERDALqlemsLVQAR--------YESQRIQLESELAV---QLEQRVTER- 174
Cdd:pfam01576 790 nKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----LAQSKesekklknLEAELLQLQEDLAAserARRQAQQERd 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 175 -LAQAQESSLRQAASLREHHRkQLQDLSGQHQQELASQlaQFKVEM-AEREERQQQVAEDYELRLAREQARVCELQSGNQ 252
Cdd:pfam01576 865 eLADEIASGASGKSALQDEKR-RLEARIAQLEEELEEE--QSNTELlNDRLRKSTLQVEQLTTELAAERSTSQKSESARQ 941
|
250
....*....|....*.
gi 2462552926 253 QLEEQRVELVERLQAM 268
Cdd:pfam01576 942 QLERQNKELKAKLQEM 957
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
86-277 |
6.33e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 86 QALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQ-LEMSLVQARYESQRIQlesela 164
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKdDNDEETRETLSTLSLR------ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 165 vQLEQRVTERLAQAQE--SSLRQAASLrehhrkqlqdLSGQHQQelaSQLAQfkVEMAEREERQQQV--------AEDYE 234
Cdd:PRK11281 125 -QLESRLAQTLDQLQNaqNDLAEYNSQ----------LVSLQTQ---PERAQ--AALYANSQRLQQIrnllkggkVGGKA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462552926 235 LRLAREQARVCELQSGNQQLEEQRVELV--ERLQAMLQAHWDEAN 277
Cdd:PRK11281 189 LRPSQRVLLQAEQALLNAQNDLQRKSLEgnTQLQDLLQKQRDYLT 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
42-231 |
6.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 42 LQEERDAARagqlSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLErekeksqREAQAAWETQHQLALVQ 121
Cdd:COG4913 697 LEAELEELE----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-------ALLEERFAAALGDAVER 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552926 122 SEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLE--QRVTERLAQAQESSLrqaASLREHHRKQLQD 199
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLEslPEYLALLDRLEEDGL---PEYEERFKELLNE 842
|
170 180 190
....*....|....*....|....*....|..
gi 2462552926 200 LSGQHQQELASQLAQfkvemaEREERQQQVAE 231
Cdd:COG4913 843 NSIEFVADLLSKLRR------AIREIKERIDP 868
|
|
| |
