|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-424 |
9.68e-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: 71.63 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 109 QLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQ 188
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 189 AQIKILEEKIDELNL-------KMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMI 261
Cdd:TIGR02168 761 AEIEELEERLEEAEEelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 262 SECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEM 341
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 342 KSRVHKYITEVSRWESlmaakekENQDLLDRFQMLHNRAEDwEVKAHQAEgesssvrlellsIDTERRHLRERVELLEKE 421
Cdd:TIGR02168 921 REKLAQLELRLEGLEV-------RIDNLQERLSEEYSLTLE-EAEALENK------------IEDDEEEARRRLKRLENK 980
|
...
gi 767930779 422 IQE 424
Cdd:TIGR02168 981 IKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
223-528 |
1.18e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 223 DKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMkimisecESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRS 302
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEEL-------EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 303 REIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRF-------QM 375
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerlES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 376 LHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQED 455
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767930779 456 EKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEF-ERVVVELENVKSESDLLKKQLSNERHTVKNLESLLA 528
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-344 |
1.51e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQttaphnivslMEKEKELALSDLRRIMAEKEALREK 81
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----------LSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 82 LEHIEEVSlfgkSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVagdsshqKTEVNSLRI 161
Cdd:TIGR02168 749 IAQLSKEL----TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-------RAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 162 VNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIA 241
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 242 NLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHK-ELDEVGRSREIAFKENRRLQDDLATM 320
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRL 977
|
330 340
....*....|....*....|....
gi 767930779 321 ARENQEISLELEAAVQEKEEMKSR 344
Cdd:TIGR02168 978 ENKIKELGPVNLAAIEEYEELKER 1001
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-456 |
1.72e-11 |
|
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: 67.40 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 176 RLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTE-KIANLQENLANKEKAV 254
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 255 AQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAA 334
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 335 VQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRER 414
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767930779 415 VELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDE 456
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-506 |
2.05e-11 |
|
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: 67.40 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 170 VDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKM-TSQDEEAHVMKktigvIDKEKDFLQETvdEKTEKIANLQENLA 248
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLeRLRREREKAER-----YQALLKEKREY--EGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 249 NKEKAVAQmkimISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKEN---------------RRL 313
Cdd:TIGR02169 238 QKEAIERQ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiaslersiAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 314 QDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGE 393
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 394 SSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIK 473
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350
....*....|....*....|....*....|...
gi 767930779 474 LDSGKDIMTQQLNSKNLEFERVVVELENVKSES 506
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-606 |
6.30e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 125 KETIESLENKLKVQAQKFSHVagdsshqKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLK 204
Cdd:COG1196 245 EAELEELEAELEELEAELAEL-------EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 205 MTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINS 284
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 285 LRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEK 364
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 365 ENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMS 444
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 445 RLEEELRHQEDEKATVLNDLSSLRElcikLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLE 524
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKI----RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 525 SLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEM 604
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
..
gi 767930779 605 RR 606
Cdd:COG1196 714 EE 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
234-469 |
1.44e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 234 DEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRL 313
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 314 QDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGE 393
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767930779 394 SSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRE 469
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-458 |
1.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 165 QLQRSVDDYQHRLSIKRgeLESAQAQIKILEEKIDELNLKMTSQDEEahvmkktIGVIDKEKDFLQETVDEKTEKIANLQ 244
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 245 ENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMAREN 324
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 325 QEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSI 404
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767930779 405 DTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKA 458
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-620 |
5.12e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 56 LMEKEKELALSDLRRIMAEKEALREKLEHIE---EVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLE 132
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEaelEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 133 NKLKVQAQKfshvagdsshqktevnslrivNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEA 212
Cdd:COG1196 302 QDIARLEER---------------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 213 HVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAA 292
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 293 HKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYI-TEVSRWESLMAAKEKENQDLLD 371
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 372 RFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEI---------QEHINAHHAYESQISSMAKA 442
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpldKIRARAALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 443 MSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMtqqlnsknlefERVVVELENVKSESDLLKKQLSNERHTVKN 522
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA-----------VTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 523 LESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQ 602
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570
....*....|....*...
gi 767930779 603 EMRRHGLATPPLSSTLRS 620
Cdd:COG1196 750 EEALEELPEPPDLEELER 767
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-526 |
4.49e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 35 EELSALRKESTQTTAphnIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEvslfgkseLEKTIEHLTCVNHQLESEK 114
Cdd:PRK02224 206 ERLNGLESELAELDE---EIERYEEQREQARETRDEADEVLEEHEERREELET--------LEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 115 YELKSKVLIMKETIESLENKLkvqaqkfSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKIL 194
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEER-------DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 195 EEKIDELnlkmtsqDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKET 274
Cdd:PRK02224 348 REDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 275 LVNRDREINSLRRQLDAAHKELDEVGRSRE-------------------IAFKENRR--LQDDLATMARENQEISLELEA 333
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvetIEEDRERVeeLEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 334 AVQEKeEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNR-------AEDWEVKAHQAEGESSSVRLELLSIDT 406
Cdd:PRK02224 501 AEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERaaeleaeAEEKREAAAEAEEEAEEAREEVAELNS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 407 ERRHLRERVELLEKeIQEHINAHHAYESQISSMAKAMSRLEEelrhQEDEKATVLNDLSS-LRELCIKLDsGKDIMTQQL 485
Cdd:PRK02224 580 KLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAE----LNDERRERLAEKRErKRELEAEFD-EARIEEARE 653
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767930779 486 NSKNLE--FERVVVELENVKSESDLLKKQLSNERHTVKNLESL 526
Cdd:PRK02224 654 DKERAEeyLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-343 |
6.75e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSNVKLLTAERDKLSVLYNEAqEELSALRKESTQTTAphnivSLMEKEKELALSDLRRIMAEKEALREK 81
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 82 LEHIEEVslfgKSELEKTIEHLTCVNHQL--------ESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQK 153
Cdd:TIGR02169 253 LEKLTEE----ISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 154 TEVNSLRIVNEQLQRSVDDYQhrlsikrGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETV 233
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 234 DEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRL 313
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350
....*....|....*....|....*....|
gi 767930779 314 QDDLATMARENQEISLELEAAVQEKEEMKS 343
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
21-606 |
8.38e-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: 58.91 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 21 AERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSL----MEKEKELALSDLRRIMAEKEALREKLEHIEEvslfGKSEL 96
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLevseLEEEIEELQKELYALANEISRLEQQKQILRE----RLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 97 EKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHR 176
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 177 LSIKRGELESAQAQIKILEEKIDELnlkmtSQDEEAHVMKKTigviDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQ 256
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERL-----QQEIEELLKKLE----EAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 257 MKIMISECESSVNQLKETLVNRDREINSLRRQLDaahkELDEVGRSREIAFKENRRLQDDLATMA---RENQEISLELEA 333
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQE----NLEGFSEGVKALLKNQSGLSGILGVLSeliSVDEGYEAAIEA 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 334 AVQEkeemksRVHKYITE-VSRWESLMAAKEKENQD-----LLDRFQMLHNRAEDWEVKAHQAEGESSSVRLE------- 400
Cdd:TIGR02168 542 ALGG------RLQAVVVEnLNAAKKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVkfdpklr 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 401 ---------LLSIDTERRHLRERVELLEKEI-------------------QEHINAHHAYESQISSMAKAMSRLEEELRH 452
Cdd:TIGR02168 616 kalsyllggVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 453 QEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRD 532
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767930779 533 KEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRR 606
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-525 |
1.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 164 EQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANL 243
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 244 QENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSReiafkenRRLQDDLATMARE 323
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-------ANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 324 NQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLhnraedwEVKAHQAEGESSSVRLELLS 403
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL-------EEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 404 IDTERRHLRERVELLEKEIQEHINAHHAYESQISSM-AKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLdsGKDImt 482
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL--ENKI-- 981
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767930779 483 QQLNSKNLEferVVVELENVKSESDLLKKQLSNERHTVKNLES 525
Cdd:TIGR02168 982 KELGPVNLA---AIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-556 |
4.18e-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: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 275 LVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKsrvhkyiTEVSR 354
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE-------AEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 355 WESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYES 434
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 435 QISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLS 514
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767930779 515 NERHTVKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLT 556
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-606 |
1.04e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQttaphnivslMEKEKELALSDLRRIMAEKEALREK 81
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 82 LEHIEEvslfGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRI 161
Cdd:TIGR02168 304 KQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 162 VNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELnlkmtSQDEEAHVMKKTigviDKEKDFLQETVDEKTEKIA 241
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL-----QQEIEELLKKLE----EAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 242 NLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDaahkELDEVGRSREIAFKENRRLQDDLATMA 321
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE----NLEGFSEGVKALLKNQSGLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 322 ---RENQEISLELEAAVQEkeemksRVHKYITE-VSRWESLMAAKEKENQD-----LLDRFQMLHNRAEDWEVKAHQAEG 392
Cdd:TIGR02168 527 eliSVDEGYEAAIEAALGG------RLQAVVVEnLNAAKKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 393 ESSSVRLE----------------LLSIDTERRHLRERVELLEKEI-------------------QEHINAHHAYESQIS 437
Cdd:TIGR02168 601 LGVAKDLVkfdpklrkalsyllggVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 438 SMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNER 517
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 518 HTVKNLESLLATNRDKEfhshltsHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYER 597
Cdd:TIGR02168 761 AEIEELEERLEEAEEEL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
....*....
gi 767930779 598 ERAIQEMRR 606
Cdd:TIGR02168 834 AATERRLED 842
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-470 |
1.38e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 116 ELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILE 195
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 196 EKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETL 275
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 276 VNRDREINSLRRQLDAAHKELDEVgrsreiafkenrrlQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRW 355
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSK--------------EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 356 ESLMAAKEKEnqdlLDRFQMLHNRAEDWEVKAHQAEgESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQ 435
Cdd:TIGR04523 537 ESKISDLEDE----LNKDDFELKKENLEKEIDEKNK-EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
330 340 350
....*....|....*....|....*....|....*
gi 767930779 436 ISSMAKAMSRLEEELRHQEDEKATVLNDLSSLREL 470
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-378 |
3.76e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 3 ERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTtaphnivSLMEKEKELALSDLRRIMAEKEALREKL 82
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-------GEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 83 EHIEEVSLFGKSELEKtiehltcvnhqLESEKYELKSKVLIMKETIESLENKLKvqAQKFSHVAGDSSHQKTEVNSLRIV 162
Cdd:TIGR02169 747 SSLEQEIENVKSELKE-----------LEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 163 NEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELnlkmtsqdeeahvmKKTIGVIDKEKDFLQETVDEKTEKIAN 242
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI--------------EKEIENLNGKKEELEEELEELEAALRD 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 243 LQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREiAFKENRRLQDDLATMAR 322
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEEELSLEDVQA 958
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767930779 323 ENQEISLELEA-------AVQEKEEMKSRVHKYitevsrwESLMAAKEKENQDLLDRFQMLHN 378
Cdd:TIGR02169 959 ELQRVEEEIRAlepvnmlAIQEYEEVLKRLDEL-------KEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-528 |
4.85e-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: 53.15 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 254 VAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEA 333
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 334 AVQEKEEmksrvhkYITEVSRWESLMAAKEKENQDLLDRfqMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRE 413
Cdd:TIGR02169 756 VKSELKE-------LEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 414 RVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFE 493
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260 270
....*....|....*....|....*....|....*
gi 767930779 494 RVVVELENVKSESDLLKKQLSNERHTVKNLESLLA 528
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-340 |
5.42e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRR----IMAEKEA 77
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 78 LREKLEHIEEVSLFGKSELEKTIEHLTCVN-HQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEV 156
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 157 NSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEK 236
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 237 TEKIANLQENLANKEKAVAQMkIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREiafkenrRLQDD 316
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGED-EEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD-------ELKEK 994
|
330 340
....*....|....*....|....
gi 767930779 317 LATMARENQEISLELEAAVQEKEE 340
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-528 |
8.92e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 235 EKTEKIANLQENLANKEKAVAQMKImisecessvNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQ 314
Cdd:TIGR02168 210 EKAERYKELKAELRELELALLVLRL---------EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 315 DDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFqmlhnraEDWEVKAHQAEGES 394
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL-------AELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 395 SSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKL 474
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767930779 475 DSGKDIMT-----QQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLA 528
Cdd:TIGR02168 434 ELKELQAEleeleEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-458 |
1.01e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 174 QHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKa 253
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS- 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 254 vaqmkiMISECESSVNQLKETLVNRDREINSLRRQLdaAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEA 333
Cdd:TIGR02169 759 ------ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 334 AVQEKEEMKSRVHKyitevsrWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRE 413
Cdd:TIGR02169 831 LEKEIQELQEQRID-------LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767930779 414 RVELLEKEIQEHinahhayESQISSMAKAMSRLEEELRHQEDEKA 458
Cdd:TIGR02169 904 KIEELEAQIEKK-------RKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-516 |
2.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAphNIVSLMEKEKELAlSDLRRIMAEKEALREK 81
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--DIARLEERRRELE-ERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 82 LEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQkfshvagdsshQKTEVNSLRI 161
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-----------ALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 162 VNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVmkktigvidkekdfLQETVDEKTEKIA 241
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE--------------LEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 242 NLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMA 321
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 322 RENQEISLELEAAVQEKEEMKSRVHKYITEVSRW--ESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVR- 398
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 399 LELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGK 478
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490 500 510
....*....|....*....|....*....|....*...
gi 767930779 479 DIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNE 516
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-594 |
3.37e-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: 50.45 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 311 RRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKahqa 390
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED---- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 391 egesssvrleLLSIDTERRHLRERVELLEKEIQEhinahhaYESQISSMAKAMSRLEEELRHQEDEKATvlNDLSSLREL 470
Cdd:TIGR02169 746 ----------LSSLEQEIENVKSELKELEARIEE-------LEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 471 CIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLAtnrdkefhshltshEKDTEIQL 550
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE--------------ELEEELEE 872
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767930779 551 LKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTER 594
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-372 |
4.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 167 QRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQEN 246
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 247 LANKEKAVAQM-----------KIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQD 315
Cdd:COG4942 99 LEAQKEELAELlralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767930779 316 DLATMARENQeislELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDR 372
Cdd:COG4942 179 LLAELEEERA----ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
282-532 |
6.12e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 282 INSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISlELEAAVQEKEEMKsrvhkyitevsrweslmAA 361
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-TLEAEIEDLRETI-----------------AE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 362 KEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAK 441
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 442 AMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVK 521
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250
....*....|.
gi 767930779 522 NLESLLATNRD 532
Cdd:PRK02224 430 ELEATLRTARE 440
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-345 |
1.08e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 4 RFEKYMEDIQ------SNVKLLTAERDKLSVLYNEAQEELSA--LRKESTQTTAPHNIVSLMEKEKELALSDlrrimAEK 75
Cdd:pfam15921 445 QMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAkkMTLESSERTVSDLTASLQEKERAIEATN-----AEI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 76 EALREKLEhieeVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQkfshvagdssHQKTe 155
Cdd:pfam15921 520 TKLRSRVD----LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ----------HGRT- 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 156 VNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDE 235
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 236 KTEKIANLQE-------NLANK----EKAVAQMKIMISECESSVNQLKETL--------------VNRDREINSLRRQLD 290
Cdd:pfam15921 665 SRNELNSLSEdyevlkrNFRNKseemETTTNKLKMQLKSAQSELEQTRNTLksmegsdghamkvaMGMQKQITAKRGQID 744
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767930779 291 AAHKELD-------EVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRV 345
Cdd:pfam15921 745 ALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-449 |
1.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 230 QETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKE 309
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 310 NRRLQDDLATMARENQEISLELEAAV---QEKEEMKSRVHKYITEVSRW-ESLMAAKEKENQDLLDRFQMLHNRAEDWEV 385
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767930779 386 KAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEE 449
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
59-284 |
3.03e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 59 KEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQ 138
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 139 AQKFSHVAGDSSHQKTEVNSLRIVNeqlQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKT 218
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767930779 219 IGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINS 284
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
269-605 |
4.80e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 269 NQLKETLVNRDR---EINSLRRQLDAAHKELDEVGRSREIAfKENRRLQDDLATmarenqeisLELEAAVQEKEEMKSRV 345
Cdd:TIGR02168 179 RKLERTRENLDRledILNELERQLKSLERQAEKAERYKELK-AELRELELALLV---------LRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 346 HKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEH 425
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 426 inahhayESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELcikldsgkdimTQQLNSKNLEFErvvVELENVKSE 505
Cdd:TIGR02168 329 -------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAE-----------LEELESRLEELE---EQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 506 SDLLKKQLSNERHTVKNLESLLatnrdkefhSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDA 585
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARL---------ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
330 340
....*....|....*....|
gi 767930779 586 LKRQISTERYERERAIQEMR 605
Cdd:TIGR02168 459 LEEALEELREELEEAEQALD 478
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-334 |
5.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 116 ELKSKVLIMKETIESLEnKLKVQAQKFSHVAGDSSHQKTEVNSLRIvnEQLQRSVDDYQHRLSIKRGELESAQAQIKILE 195
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 196 EKIDELnlkmTSQDEEAHVMKKTIGVIDKEKdfLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETL 275
Cdd:COG4913 316 ARLDAL----REELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767930779 276 vnrDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAA 334
Cdd:COG4913 390 ---AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-534 |
5.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 24 DKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVslfgKSELEKTIEHL 103
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 104 TCVNHQLESEKYELKSKVLIMKETIESLEnKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVD---DYQHRLSIK 180
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDelrEIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 181 RGELESAQAQIKILEEKIDELN-----------------------------------LKMTSQDEEAHVMKKTIGVIDKE 225
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEelkkklkelekrleeleerhelyeeakakkeelerLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 226 KDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISEC-----ESSVNQLKETLVNRDREINSLRRQL---DAAHKELD 297
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKELLEEYTAELKRIEKELkeiEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 298 EVGRSREIAFKENRRLQ------DDLATMARENQEISLE-LEAAVQEKEEMKSRVHKYITEVSRWEslmaakekenqDLL 370
Cdd:PRK03918 480 KELRELEKVLKKESELIklkelaEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLK-----------KEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 371 DRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTER-RHLRERVELLEKEIQEHINAHHAyESQISSMAKAMSRLEEE 449
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 450 LRHQEDEKATVLNDLSSLRELCIKLdsGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLAT 529
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
....*
gi 767930779 530 NRDKE 534
Cdd:PRK03918 706 REKAK 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-592 |
1.20e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 66 SDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENkLKVQAQKFSHV 145
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE-LENELNLLEKE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 146 AGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKE 225
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 226 KDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQ-----LKETLVNRDREINSLRRQLDAAHKELDEVG 300
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 301 RSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQdlldrfqmlhnra 380
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ------------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 381 edwevkahQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATV 460
Cdd:TIGR04523 409 --------QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 461 LNDLSSL-RELCIKLDsgkdiMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEfHSHL 539
Cdd:TIGR04523 481 KQNLEQKqKELKSKEK-----ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFEL 554
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 767930779 540 TSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQIST 592
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
175-580 |
1.38e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 175 HRLSIKRGELESAQAQIKILEEKIDElNLKMTSQDEEAHVMKKTIGV------IDKEKDFLQETvdeKTEKIANLQENLA 248
Cdd:COG5022 803 LSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIqkfgrsLKAKKRFSLLK---KETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 249 NKEKAVAQMKIMISEcessVNQLKETLVNRDREINSLRRQLDAAHKELDEVgRSREIAF----KENRRLQDDLATMAREN 324
Cdd:COG5022 879 LAERQLQELKIDVKS----ISSLKLVNLELESEIIELKKSLSSDLIENLEF-KTELIARlkklLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 325 -------------QEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRF-QMLHNRAEDWEVKAHQA 390
Cdd:COG5022 954 pelnklhevesklKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTkQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 391 EGES-SSVRLELLSIDTERRHLRERVELLEKEIQEHINA---HHAYESQISSMAKAMSRLEEELRHQEDEKATvlnDLSS 466
Cdd:COG5022 1034 IISSeSTELSILKPLQKLKGLLLLENNQLQARYKALKLRrenSLLDDKQLYQLESTENLLKTINVKDLEVTNR---NLVK 1110
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 467 LRELCIKLDS------GKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEFHSH-L 539
Cdd:COG5022 1111 PANVLQFIVAqmiklnLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYdE 1190
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767930779 540 TSHEKDTEIQLLKEKLtlseSKLTSQSRENTMLRAKVAQLQ 580
Cdd:COG5022 1191 KSKLSSSEVNDLKNEL----IALFSKIFSGWPRGDKLKKLI 1227
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
25-607 |
1.51e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 25 KLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKealREKLEHIEEVSLFGKSELEKTIEHlt 104
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES---RDKANQLEEKTKLQDENLKELIEK-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 105 cvNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLR----IVNEQLQRSVDDYQHRLSIK 180
Cdd:pfam05483 291 --KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsFVVTEFEATTCSLEELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 181 RGELESAQAQIKILEEKIDelnlKMTSQDEEAHVMKKTigvidkekdflQETVDEKTEKIANLQENLANKEKavaQMKIM 260
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQ----KKSSELEEMTKFKNN-----------KEVELEELKKILAEDEKLLDEKK---QFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 261 ISECESSVNQLKETLVNRDREINSLRRQLDAAH-------KELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEA 333
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKtseehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 334 AVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQM----LHNRAEDWEVKAHQAEGESSSVRLELLSIDTERR 409
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 410 HLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRElciKLDSGKDIMTQQLNSKN 489
Cdd:pfam05483 591 ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDNYQKEIEDKK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 490 LEFERVVVELENVKSESD----LLKKQLSNERHTVKNLESLLATNRdkefhshltsHEKDTEIQLLKEKLTLSESKLTSQ 565
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADeavkLQKEIDKRCQHKIAEMVALMEKHK----------HQYDKIIEERDSELGLYKNKEQEQ 737
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 767930779 566 SRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRRH 607
Cdd:pfam05483 738 SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
183-401 |
2.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 183 ELESAQAQIKILEEKIDELNLKMTSQdeeahvmKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMIS 262
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAAL-------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 263 ECESSVNQLKETLVNRDREINSLRRQLDAAH----KELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEK 338
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767930779 339 EEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLEL 401
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
186-372 |
2.93e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 186 SAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISE-- 263
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 264 -----CESSVNQLKETLVNRD-----REINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEA 333
Cdd:COG3883 93 ralyrSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 767930779 334 AVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDR 372
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-276 |
3.94e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSN---VKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNI-VSLMEKE---KELALSDLRRIMAE 74
Cdd:pfam15921 536 LKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEindRRLELQEFKILKDK 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 75 KEALREKLE------HIEEVSLFG------------KSELEKTIEHLTCVNHQLE--SEKYE-LKSKVLIMKETIESLEN 133
Cdd:pfam15921 616 KDAKIRELEarvsdlELEKVKLVNagserlravkdiKQERDQLLNEVKTSRNELNslSEDYEvLKRNFRNKSEEMETTTN 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 134 KLKVQAQKfshVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAH 213
Cdd:pfam15921 696 KLKMQLKS---AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKN 772
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767930779 214 VMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLV 276
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
59-605 |
5.45e-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: 43.24 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 59 KEKELALSDLRRIMAEKEALREKLeHIEEVSLFGK-SELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKV 137
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKL-QLEKVTTEAKiKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 138 QAQ---KFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDdyqhrlsikrGELESAQAQIKILEEKIDELNLKMTSQDEEAHV 214
Cdd:pfam01576 178 LSKlknKHEAMISDLEERLKKEEKGRQELEKAKRKLE----------GESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 215 MKKTIGVIDKEKDFLQETVDEKTEKIANLQENLAN----KEKAVAQMKIMISECESSVNQLKETL--VNRDREINSLRRQ 288
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESeraaRNKAEKQRRDLGEELEALKTELEDTLdtTAAQQELRSKREQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 289 -LDAAHKELDEVGRSREIAFKENRR--------LQDDLATMAR--------------ENQEISLELEAAVQEKEEMKSRV 345
Cdd:pfam01576 328 eVTELKKALEEETRSHEAQLQEMRQkhtqaleeLTEQLEQAKRnkanlekakqalesENAELQAELRTLQQAKQDSEHKR 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 346 HKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTerrHLRERVELLEKEIQEH 425
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES---QLQDTQELLQEETRQK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 426 INahhaYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLR---------------------ELCIKLDSGKDIMTQQ 484
Cdd:pfam01576 485 LN----LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaqlsdmkkkleedagtlealeEGKKRLQRELEALTQQ 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 485 LNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLE--------------SLLATNRDKEFHSHLTSHEKDTEIQL 550
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEkkqkkfdqmlaeekAISARYAEERDRAEAEAREKETRALS 640
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 767930779 551 LKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQI-STERYER--ERAIQEMR 605
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhELERSKRalEQQVEEMK 698
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-608 |
7.66e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 159 LRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILE------------------EKIDELNLKMTSQDEEAHVMKKTIG 220
Cdd:pfam12128 292 LRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhgafldadietaaadqEQLPSWQSELENLEERLKALTGKHQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 221 VIDKEKDFLQETVDEK-TEKIANLQENLAN-KEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKEL-- 296
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQnNRDIAGIKDKLAKiREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELkl 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 297 -------------------DEVGRSREI---AFKENRRLQDDLATM--ARENQEISL--------ELEAAVQEKEEM--- 341
Cdd:pfam12128 452 rlnqatatpelllqlenfdERIERAREEqeaANAEVERLQSELRQArkRRDQASEALrqasrrleERQSALDELELQlfp 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 342 --KSRVHKYITEVSRWESLMAAkekenqdLLDRfQMLHNRAEDWEVKAHQAEGESS--SVRLELLSIDTERRH-----LR 412
Cdd:pfam12128 532 qaGTLLHFLRKEAPDWEQSIGK-------VISP-ELLHRTDLDPEVWDGSVGGELNlyGVKLDLKRIDVPEWAaseeeLR 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 413 ERVELLEKEIQEHINAHHAYESQissMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSknlEF 492
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQ---LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE---RK 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 493 ERVVVELENVKSESDLLKKQLSNERHTVKNlESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTML 572
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKE-QKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
490 500 510
....*....|....*....|....*....|....*.
gi 767930779 573 RAKVAQLQTDYDALKRqISTERYERERAIQEMRRHG 608
Cdd:pfam12128 757 KRDLASLGVDPDVIAK-LKREIRTLERKIERIAVRR 791
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
162-605 |
9.55e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 162 VNEQLQRSVDDYQHRLsikrgELESAQAQIKIlEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTekia 241
Cdd:pfam15921 243 VEDQLEALKSESQNKI-----ELLLQQHQDRI-EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQN---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 242 nlqenlankekavAQMKIMISECESSVNQLKETLVNRDR----EINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDL 317
Cdd:pfam15921 313 -------------SMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 318 ----ATMARENQEISLELEAAVQ----------EKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDR-FQMLHNRAED 382
Cdd:pfam15921 380 qkllADLHKREKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERqMAAIQGKNES 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 383 WE-VKAHQAEGESSSVRL-----ELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRH---Q 453
Cdd:pfam15921 460 LEkVSSLTAQLESTKEMLrkvveELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 454 EDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLlatnRDK 533
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL----KDK 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 534 EFHSHLTSHEKDTEIQLLKEKLT------LSESKLTSQSRENTM-----LRAKVAQLQTDYDALKRQISTERYERERAIQ 602
Cdd:pfam15921 616 KDAKIRELEARVSDLELEKVKLVnagserLRAVKDIKQERDQLLnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
...
gi 767930779 603 EMR 605
Cdd:pfam15921 696 KLK 698
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
22-531 |
1.08e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 22 ERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLmekeKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIE 101
Cdd:pfam10174 203 QKEKENIHLREELHRRNQLQPDPAKTKALQTVIEM----KDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQME 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 102 HLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKR 181
Cdd:pfam10174 279 VYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 182 GELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQEnlankekAVAQMKIMI 261
Cdd:pfam10174 359 SFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE-------RVKSLQTDS 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 262 SECESSVNQLKETLVNRDREINSLRRQLDAAHKE-LDEVGRSReiafKENRRLQDDLATMARENQEISLELEAAVQEKEE 340
Cdd:pfam10174 432 SNTDTALTTLEEALSEKERIIERLKEQREREDRErLEELESLK----KENKDLKEKVSALQPELTEKESSLIDLKEHASS 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 341 MKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEgesssvRLELLSIDTERRhlRERVELLEK 420
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND------RIRLLEQEVARY--KEESGKAQA 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 421 EIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIK------LDSGKDIMTQQLNSKNLEFER 494
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKkgaqllEEARRREDNLADNSQQLQLEE 659
|
490 500 510
....*....|....*....|....*....|....*..
gi 767930779 495 VVVELENVKSESDLLKKQLSNERHTVKNLESLLATNR 531
Cdd:pfam10174 660 LMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-515 |
1.37e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 24 DKLSVLYNEAQEELSALRKEST----QTTAPHNI-VSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEK 98
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQQHQdrieQLISEHEVeITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 99 TIEHLtcvnhqleseKYELKSKVLIMKETIESLENKL----------KVQAQKFSHVAGDSSHQKTEV--------NSLR 160
Cdd:pfam15921 325 TVSQL----------RSELREAKRMYEDKIEELEKQLvlanselteaRTERDQFSQESGNLDDQLQKLladlhkreKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 161 IVNEQLQR----------SVDDYQHRLSIKRGELESAQAQIKILEE----KIDELNLKMTSQDEEAHVMKKTIGVIDKEK 226
Cdd:pfam15921 395 LEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 227 DFLQETVDEKTEK----------IANLQENLANKEKAVAQMKIMISECESSVN------------------------QLK 272
Cdd:pfam15921 475 EMLRKVVEELTAKkmtlessertVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelqhlknegdhlrnvqteceALK 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 273 ETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEV 352
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 353 SRW-----ESLMAAKE--KENQDLLDRFQM----LHNRAEDWEV-------KAHQAEGESSSVRLELLSIDTERRHLRER 414
Cdd:pfam15921 635 VKLvnagsERLRAVKDikQERDQLLNEVKTsrneLNSLSEDYEVlkrnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 415 VELLEKE----------IQEHINAHH----AYESQISSMAKAMSRLEEELRHQEDEKATvlndlsslrelcikldsgkdi 480
Cdd:pfam15921 715 LKSMEGSdghamkvamgMQKQITAKRgqidALQSKIQFLEEAMTNANKEKHFLKEEKNK--------------------- 773
|
570 580 590
....*....|....*....|....*....|....*
gi 767930779 481 MTQQLNSKNLEFERVVVELENVKSESDLLKKQLSN 515
Cdd:pfam15921 774 LSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
117-330 |
1.58e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 117 LKSKVLIMKETIESLENKLkvqaqkfSHVAGDSSHQKTEVNSLRIVNEQlqrSVDDYQHRLSIKRGELESAQAQIKILEE 196
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKI-------DHIQQQIKTYNKNIEEQRKKNGE---NIARKQNKYDELVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 197 KIdeLNLKMTSQDEEAHV---------MKKTIGVIDKEKDFLQE---------TVDEKTEKIANLQENLANKEKAVAQMK 258
Cdd:PHA02562 242 EL--LNLVMDIEDPSAALnklntaaakIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 259 IMISECESSVNQ----------LKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEIS 328
Cdd:PHA02562 320 TAIDELEEIMDEfneqskklleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELV 399
|
..
gi 767930779 329 LE 330
Cdd:PHA02562 400 KE 401
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-603 |
1.60e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 74 EKEALR-EKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMK--ETIESLENKLKVQAQKFSHVAGDSS 150
Cdd:PTZ00121 1239 AEEAKKaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 151 HQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIdKEKDFLQ 230
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK-KKADEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 231 ETVDEKTEKIANLQENLANKEKA-----VAQMKIMISECESSVNQLKETlvNRDREINSLRRQLDAAHKELDEVGRSREI 305
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 306 AFK-ENRRLQDDLATMARENQEISLELEAAVQEK----------EEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQ 374
Cdd:PTZ00121 1476 KKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkadeakkaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 375 MLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQE 454
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 455 DEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATN-RDK 533
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEaEEK 1715
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767930779 534 EFHSHLTSHEKDTEIQLLKEKLTLSESKLTS-QSRENTMLRAKVAQLQTDYDALKRQIsteRYERERAIQE 603
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAeEAKKDEEEKKKIAHLKKEEEKKAEEI---RKEKEAVIEE 1783
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-621 |
2.20e-03 |
|
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: 40.90 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 360 AAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHinahhayESQISSM 439
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-------EAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 440 AKAMSRLEEELRHQEDEKATVLNDLSSLrelcikldSGKDIMTQQLNSKNleFERVVVELENVKSESDLLKKQLSNERHT 519
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRL--------GRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 520 VKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQIstERYERER 599
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEA 236
|
250 260
....*....|....*....|..
gi 767930779 600 AIQEMRRHGLATPPLSSTLRSP 621
Cdd:COG4942 237 AAAAERTPAAGFAALKGKLPWP 258
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
152-337 |
2.44e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 152 QKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEE-----------AHVMKKT-- 218
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerreelgerARALYRSgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 219 --------------------IGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNR 278
Cdd:COG3883 101 svsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767930779 279 DREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQE 337
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
194-313 |
2.98e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 194 LEEKIDELNLKMtsQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLK- 272
Cdd:COG2433 378 IEEALEELIEKE--LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARs 455
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767930779 273 --ETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRL 313
Cdd:COG2433 456 eeRREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-384 |
5.53e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 2 LERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKEstqttaphnivslmEKEKELALSDLRRIMAEKEALREK 81
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER--------------EAELEATLRTARERVEEAEALLEA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 82 LEHIEEVSLFGKSELEKTIEhltcvnhQLESEKYELKSKVLIMKETIESLENKLKvqaqkfshVAGDSSHQKTEVNSLRI 161
Cdd:PRK02224 452 GKCPECGQPVEGSPHVETIE-------EDRERVEELEAELEDLEEEVEEVEERLE--------RAEDLVEAEDRIERLEE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 162 VNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEkdflQETVDEKTEKIA 241
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 242 NLQENLAnkekavaqmkiMISECESSVNQLKETLVNRDrEINSLRRQldaAHKELDEVGRSREIAFKENR--RLQDDLAT 319
Cdd:PRK02224 593 RIRTLLA-----------AIADAEDEIERLREKREALA-ELNDERRE---RLAEKRERKRELEAEFDEARieEAREDKER 657
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767930779 320 MARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLmAAKEKENQDLLDRFQMLHNRAEDWE 384
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL-RERREALENRVEALEALYDEAEELE 721
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-424 |
6.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 10 EDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVS 89
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 90 LFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRS 169
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 170 VDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTS------------------------------------------ 207
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaalllaglrglagavavligveaayeaaleaalaaalqni 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 208 QDEEAHVMKKTIGVIDKEKD----FLQETVDEKTEKIANLQENLANkEKAVAQMKIMISECESSVNQLKETLVNRDRE-- 281
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgratFLPLDKIRARAALAAALARGAI-GAAVDLVASDLREADARYYVLGDTLLGRTLVaa 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 282 -INSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMA 360
Cdd:COG1196 631 rLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767930779 361 AKEKENQDLLDRFQMLHNRAE----DWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQE 424
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEaereELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-340 |
6.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 186 SAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIanlqeNLANKEKAVAQMKIMISECE 265
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767930779 266 SSVNQLKEtlvnrdreinsLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEE 340
Cdd:COG4913 682 ASSDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
164-451 |
9.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 164 EQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANL 243
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 244 QENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARE 323
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930779 324 NQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLS 403
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767930779 404 IDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELR 451
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| |
