|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-472 |
8.30e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 307 AAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE 382
Cdd:COG1196 313 ELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSE----- 457
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElleea 472
|
250 260
....*....|....*....|
gi 1958671317 458 -----EIEKLRQEVDQLKGR 472
Cdd:COG1196 473 alleaALAELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-492 |
9.77e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQqgAGIRDGVAEEEEtvdlgpkrlwkdDTGRVEELQGLLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELE--AELEELEAELAE------------LEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 238 QNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 318 LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnIEEHLRQLEG 397
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 398 QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRlsEEIEKLRQEVDQLKGRGGPFV 477
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAA 513
|
330
....*....|....*
gi 1958671317 478 DGIHSRSHVGSTADV 492
Cdd:COG1196 514 LLLAGLRGLAGAVAV 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-469 |
2.60e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 85 RELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrqaqspsgvssevevLKALKSLFEHHKAL 164
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ---------------ISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 165 DEKVRERLRAALERVTTLEEQLAGAHQQVsalqqgAGIRDGVAEEEEtvdlgpkrlwkddtgRVEELQGLLEKQNYELSQ 244
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERL------EEAEEELAEAEA---------------EIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 325 ELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:TIGR02168 881 ERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671317 405 elaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR02168 944 ---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDL 1012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-472 |
5.92e-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: 66.24 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 218 KRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEE----LSGKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 369 AELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-----REKMN------EDHNKRLSDTVDRL------L 431
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelKEELEdlraelEEVDKEFAETRDELkdyrekL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958671317 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-469 |
1.26e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 241 ELSQARERLVTLSatVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQRE----ATSIH 316
Cdd:TIGR02168 221 ELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 317 DL-------NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIE 389
Cdd:TIGR02168 299 RLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 390 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ-LHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELER 458
|
.
gi 1958671317 469 L 469
Cdd:TIGR02168 459 L 459
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-470 |
3.09e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 34 LDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSmcreQLLEREEEISELKAERNNTRL 113
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 114 LLEHLEclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAlDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:PRK03918 353 RLEELE---ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 194 SALQQGAGI----RDGVAEEEEtvdlgpKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSaTVTELEEDLGTARR- 268
Cdd:PRK03918 429 EELKKAKGKcpvcGRELTEEHR------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLKEl 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 269 -DLIKS--EELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKES----LHRQCEE 338
Cdd:PRK03918 502 aEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEE 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 339 KARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQreKMNED 418
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEE 659
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671317 419 HNKRLSDTVDRL------LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 660 EYEELREEYLELsrelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-409 |
3.18e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 37 REKLLESLRESQETLvatqSRLQDALHERD-QLQR-HLNSALPQEFATLTRELSmcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168 174 RKETERKLERTRENL----DRLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR02168 248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 195 ALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSE 274
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 275 ELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS-----IHDLNDKLENELANKESLHRQCEEKARHLQELLEV 349
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 350 AEQKLQQTMRKaetlpevEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:TIGR02168 473 AEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-473 |
5.29e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 247 ERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRdLREALAQKEDMEERITTLekRYLAAQREATSIHDLNDKLENEL 326
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 327 ANKESLHRQCEEKARHLQELLEVAEQKLQQtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671317 407 ARVRQRekmnedhnkrlsdtVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRG 473
Cdd:COG4913 383 AALRAE--------------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-472 |
5.31e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 20 ADADANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196 408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 180 TTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLgpKRLWKDDTGRVEELQGLLEKqnYELSQARERLVTLSATVTEL 259
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLRGLAGAVAVLIGVEAA--YEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 260 EEDLGTARRDLIKSEE-------LSGKHQRDLREALAQKEDMEERITTLEkryLAAQREATSIHDLNDKLENELANKESL 332
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVA---SDLREADARYYVLGDTLLGRTLVAARL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 333 HRQCEEKARHLQELLEV---AEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 633 EAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958671317 410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-468 |
6.02e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDgvAEEEETVDlgpkrlwkdDTGRVEELQGLLEKQ 238
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE---------EAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 239 NYELSQARERLVTLSATVTELE-----EDLGTARRDLIKSEELSgKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671317 394 QlEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEEKgrLSEEIEKLRQEVDQ 468
Cdd:PTZ00121 1737 K-EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDK 1798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-474 |
1.15e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 304 RylaaqreatsIHDLNDKLEnELANKESLHRQCEEKA---RHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTK 380
Cdd:PRK03918 267 R----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 381 AEERHGNIEEHLRQLE---GQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHLKErmaALEEKGRLSE 457
Cdd:PRK03918 336 KEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTG-------LTPEKLEKELEE---LEKAKEEIEE 405
|
250
....*....|....*..
gi 1958671317 458 EIEKLRQEVDQLKGRGG 474
Cdd:PRK03918 406 EISKITARIGELKKEIK 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-470 |
1.68e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEkRYL 306
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 307 AAQREAtsIHDLNDKL-ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALtkaEERH 385
Cdd:TIGR02169 775 HKLEEA--LNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL---KEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 386 GNIEEHLRQLEGQLEEKNQELARVRQREKmneDHNKRLSDtvdrlLSESNERLQLHLKErmaALEEKGRLSEEIEKLRQE 465
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALR---DLESRLGD-----LKKERDELEAQLRE---LERKIEELEAQIEKKRKR 918
|
....*
gi 1958671317 466 VDQLK 470
Cdd:TIGR02169 919 LSELK 923
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-469 |
5.40e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 101 ISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVT 180
Cdd:PRK02224 222 IERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 181 TLEEQLAGAHQQVSALQQGAGIRDGvaeEEETVDLGPKRLWKDDtgrvEELQGLLEKQNYELSQARERLVTLSATVTELE 260
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 261 EDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 341 RHLQELLEVAEQKlqQTMRKAETLPEVEAEL--SQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmned 418
Cdd:PRK02224 433 ATLRTARERVEEA--EALLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL------ 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958671317 419 hnKRLSDTVDRLLsESNERLQLHLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 505 --VEAEDRIERLE-ERREDLEELIAERRETIEEK---RERAEELRERAAEL 549
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-470 |
7.05e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.37 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 146 SEVEVLKALKSLFEHHKALDEKVRERL--RAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKD 223
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 224 DTGRVEELQglLEKQNYELSQARERLVTLSATVTELEEDLGTARRDliKSEELsgkhQRDLREALAQKEDMEERittlEK 303
Cdd:pfam17380 346 RERELERIR--QEERKRELERIRQEEIAMEISRMRELERLQMERQQ--KNERV----RQELEAARKVKILEEER----QR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 304 RYLAAQREATSIhdlndKLENELANKESLHRQCEEKARHLQELLEvAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEE 383
Cdd:pfam17380 414 KIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRL-EEQERQQQV---ERLRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 384 RHGNIEEHLRQ-LEGQLEEKNQELARVRQREKM----NEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEE 451
Cdd:pfam17380 485 DRKRAEEQRRKiLEKELEERKQAMIEEERKRKLlekeMEERQKAIYEEERRREAEEERRKQQEMEERrriqeqmRKATEE 564
|
330
....*....|....*....
gi 1958671317 452 KGRLsEEIEKLRQEVDQLK 470
Cdd:pfam17380 565 RSRL-EAMEREREMMRQIV 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-472 |
7.69e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 26 FEQLMVNMLDER-EKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRElsmcreqllereeeISEL 104
Cdd:COG4913 285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE--------------IERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 105 KAERNNTRLLLEHLECLVsrheRSLRMTVvkrqaqsPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4913 351 ERELEERERRRARLEALL----AALGLPL-------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 185 QLAGAHQQVSALQQGAG--------IRD------GVAEEE-----ETVDLGPK-RLWKD--------------------- 223
Cdd:COG4913 420 ELRELEAEIASLERRKSniparllaLRDalaealGLDEAElpfvgELIEVRPEeERWRGaiervlggfaltllvppehya 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 224 ---------------DTGRVEEL-----------QGLLEKQNYELSQARERLVTLSATVTEL-----EEDLGTARRD--- 269
Cdd:COG4913 500 aalrwvnrlhlrgrlVYERVRTGlpdperprldpDSLAGKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPRAitr 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 270 --LIKSEelSGKHQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHL 343
Cdd:COG4913 580 agQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREAL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 344 QELLEV--AEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK 421
Cdd:COG4913 651 QRLAEYswDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958671317 422 RLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-418 |
8.34e-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: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 36 EREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALpqEFATLTRELsmcreqlleREEEISELKAERNNTRLLL 115
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 116 EHLECLVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSA 195
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 196 LQQGAgiRDGVAEEEET-VDLGPKRLWKDD-TGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLiks 273
Cdd:TIGR02169 313 KEREL--EDAEERLAKLeAEIDKLLAEIEElEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL--- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 274 eelsgkhqRDLREALAQ-KEDMEERITTLEKRYLAAQREATSIHDLNdkleNELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02169 388 --------KDYREKLEKlKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671317 353 KLQQTmrkaetlpeveaelsqrIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:TIGR02169 456 KLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-472 |
1.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALqqgagiRDGVAEEEETvdlgpkrlw 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELKEL--------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 222 KDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLgtarrdliksEELSGKHQRdLREALAQKEDMEERITTL 301
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----------KELEEKEER-LEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 302 EKRYLAAQrEATSIHDLNDKLENELANKESlhrqceEKarhLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKA 381
Cdd:PRK03918 358 EERHELYE-EAKAKKEELERLKKRLTGLTP------EK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 382 EER-----------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKERM 446
Cdd:PRK03918 428 IEElkkakgkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQL 505
|
330 340 350
....*....|....*....|....*....|....*
gi 1958671317 447 AALEEK---------GRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK03918 506 KELEEKlkkynleelEKKAEEYEKLKEKLIKLKGE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-484 |
1.17e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 146 SEVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALqqgagiRDGVAEEEETVDlgpkrlwkDDT 225
Cdd:TIGR02168 223 RELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIE--------ELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 226 GRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 306 LAAqreatsiHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEerh 385
Cdd:TIGR02168 368 EEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 386 gnieehlrqLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQL-----HLKERMAALEEKGR----LS 456
Cdd:TIGR02168 438 ---------LQAELEELEEELEELQEEL---ERLEEALEELREELEEAEQALDAAerelaQLQARLDSLERLQEnlegFS 505
|
330 340
....*....|....*....|....*...
gi 1958671317 457 EEIEKLRQEVDQLKGRGGPFVDGIHSRS 484
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLSELISVDE 533
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-412 |
1.28e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 36 EREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLL 115
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 116 EHL-ECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQ 192
Cdd:COG1196 477 AALaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEAALAAALQNIVVEDD 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 193 VSALQQGAGI---RDGVAEEEETVDLGPKRLWKDDTGRVEELQGLL----EKQNYELSQARERLVTLSATVTELEEDLGT 265
Cdd:COG1196 557 EVAAAAIEYLkaaKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvasDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 266 AR------RDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:COG1196 637 RRavtlagRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKN-------QELARVRQR 412
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnllaiEEYEELEER 796
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-407 |
2.18e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 229 EELQGLLEKQNY--ELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELSQRIAALTKAEERHG 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|.
gi 1958671317 387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579 149 EELAELEAELEELEAEREELA 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-475 |
2.35e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 261 EDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 341 RHLQEL----------LEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE---ERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:PRK03918 238 EEIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671317 408 RVRQREKMNEDHNKRLSDTVDRLlsESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-640 |
4.74e-08 |
|
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: 57.05 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 21 DADANFEQLMVNMLDErEKLLESLREsqeTLVATQSRLQDALHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGIRDGVAEEEETVD-------------------- 214
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLDdqlqklladlhkrekelsle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 215 -LGPKRLWKDDTG--------------------RVE--------ELQGLLEKQNYELSQARERLVTLSATVTELEEDLGT 265
Cdd:pfam15921 397 kEQNKRLWDRDTGnsitidhlrrelddrnmevqRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEM 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 266 ARRDLiksEELSGKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESL 332
Cdd:pfam15921 477 LRKVV---EELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 333 HRQCEEKARHLQELLEVAEQKLQ---QTMRKAETL----PEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEknQE 405
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGAMqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD--LE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 406 LARVrqreKMNEDHNKRLSDTVDRllseSNERLQLhLKERMAALEEKGRLSEEIEKLRQEVDQlkgrggpfvdgiHSRSH 485
Cdd:pfam15921 632 LEKV----KLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEVLKRNFRN------------KSEEM 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 486 VGSTADVRFSLSTAAhvpPGLHRRYTALREESAKDWKPAPLPgvlaatttpafdsdpeisdvdedepgglVGTQVDVISP 565
Cdd:pfam15921 691 ETTTNKLKMQLKSAQ---SELEQTRNTLKSMEGSDGHAMKVA----------------------------MGMQKQITAK 739
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671317 566 GGHSDA-QTLAMMLQEQLDAINQEIRMIQEEKE--STELRAEEIETRVTSGSMEALNLTQLRKRGSIPTSLTALSLAS 640
Cdd:pfam15921 740 RGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNklSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-409 |
1.62e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 61 ALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLeclvsrheRSLRMTVVKRQAQS 140
Cdd:COG1196 230 LLLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA--------QAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 141 PSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRL 220
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 221 WKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 301 LEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEVAEQKLQQTMRKAE----TLPEVEAELSQRI 375
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAGLRGLAgavaVLIGVEAAYEAAL 540
|
330 340 350
....*....|....*....|....*....|....
gi 1958671317 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
234-470 |
1.78e-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: 55.03 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 234 LLEKQNyELSQARERLVTLSATVTELEEDLGTARRDliKSEELSGKHQRDLREALAQKEDMEERITTLEKrylaaqreat 313
Cdd:TIGR04523 269 LSEKQK-ELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNK---------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 314 SIHDLND---KLENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTmrkaETLPEVEAELSQRIaalTKAEERHG 386
Cdd:TIGR04523 336 IISQLNEqisQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKI---QNQEKLNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS--DTVDRLLSESNERLQLHLKERMAALEekgrlsEEIEKLRQ 464
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqDSVKELIIKNLDNTRESLETQLKVLS------RSINKIKQ 482
|
....*.
gi 1958671317 465 EVDQLK 470
Cdd:TIGR04523 483 NLEQKQ 488
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
1.98e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGIRDGVAEEEETVD--LGPKRLWKDDT--GRVEELqgllEKQ 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEEL----REE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 239 NYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELsgkhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 902 LDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR----KAETLPEVEAELSQ-RIAALTKAEE 383
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSsrdaKQQTLQELEQELEElGVQADAEAEE 1055
|
250 260 270
....*....|....*....|....*....|.
gi 1958671317 384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-465 |
2.31e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 241 ELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLND 320
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 321 KLENELANKESLHRQCEEKarhlqelLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnieehLRQLEGQLE 400
Cdd:COG4942 105 ELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671317 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-474 |
2.81e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 35 DEREKLLESLRESQETLVA---TQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:PRK02224 227 EQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 112 RL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQLA 187
Cdd:PRK02224 306 DAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 188 GAHQQVSALQ-QGAGIRDGVAEEEETVDLGPKRLwkddtgrvEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:PRK02224 374 EAREAVEDRReEIEELEEEIEELRERFGDAPVDL--------GNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 267 RR---------------------DLIKSEELSGKHQRDLREALAQKEDMEERITTLEKrYLAAQREATSIHDLNDKLENE 325
Cdd:PRK02224 446 EAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 326 LANKESL----HRQCEEKARHLQELLEVAEQK---LQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLrqleGQ 398
Cdd:PRK02224 525 IAERRETieekRERAEELRERAAELEAEAEEKreaAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL----AA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 399 LEEKNQELARVRQREK----MNEDHNKRLSDTVDR---LLSESNE-RLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK02224 601 IADAEDEIERLREKREalaeLNDERRERLAEKRERkreLEAEFDEaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
....
gi 1958671317 471 GRGG 474
Cdd:PRK02224 681 AEIG 684
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-430 |
3.04e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 229 EELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnI 388
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958671317 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-472 |
3.78e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 246 RERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE 325
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 326 LANKESLHR-------QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:TIGR02169 753 IENVKSELKelearieELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 394 QLEGQLEEKNQEL-ARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 833 KEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL-----EELEAALRD---LESRLGDLKKERDELEAQLRELERK 904
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-465 |
5.54e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 222 KDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERIttl 301
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--- 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 302 ekrylaAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL-TK 380
Cdd:TIGR02169 789 ------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 381 AEERHGNIEEHLRQLEgQLEEKNQELARVRqrekmnEDHNKRLSDTVDRL--LSESNERLQLHLKERMAALEEKGRLSEE 458
Cdd:TIGR02169 863 KEELEEELEELEAALR-DLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSELKAKLEALEEELSE 935
|
....*..
gi 1958671317 459 IEKLRQE 465
Cdd:TIGR02169 936 IEDPKGE 942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-469 |
6.92e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 34 LDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHL-NSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 113 LLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAH-- 190
Cdd:COG4717 167 ELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAle 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 191 QQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDD------TGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLG 264
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 265 TARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATsihdLNDKLENELANKESLHRQCEEKARHLQ 344
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE----IAALLAEAGVEDEEELRAALEQAEEYQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 345 ELLEVAEQKLQQTMRKAETLPEVEAELSqriaaLTKAEERHGNIEEHLRQLEGQLEEKNQELARvrqrekmnedhnkrls 424
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREELAE---------------- 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958671317 425 dtvdrllsesnerlqlhLKERMAALEEKGRLSE---EIEKLRQEVDQL 469
Cdd:COG4717 458 -----------------LEAELEQLEEDGELAEllqELEELKAELREL 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
183-470 |
7.47e-07 |
|
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: 52.81 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 183 EEQLAGAHQQVSALQQGAGIRDGVAEEEETV-----DLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVT 257
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 258 ELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEerITTLEKRYLAAQREATSIHDLNDKLENELANKESLHrqce 337
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 338 ekARHLQELLEVAEQkLQQTMRKA-----ETLPEVEAELSQRIAALTKAE-------ERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:pfam15921 316 --MRQLSDLESTVSQ-LRSELREAkrmyeDKIEELEKQLVLANSELTEARterdqfsQESGNLDDQLQKLLADLHKREKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNER-----------------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
..
gi 1958671317 469 LK 470
Cdd:pfam15921 473 TK 474
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
177-469 |
1.07e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 177 ERVTTLEEQLAGAHQQVSALQQG-AGIRDGVAEEEETVDLGPKRlwkddtgrvEELQGLLEKQNYELSQARERLVTLSAT 255
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERlERAEDLVEAEDRIERLEERR---------EDLEELIAERRETIEEKRERAEELRER 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 256 VTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEkrylaaqreatsihdlndKLENELANKESLHRQ 335
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE------------------RIRTLLAAIADAEDE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 336 CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKM 415
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA 685
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958671317 416 NEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 686 VENELEELEE----------------LRERREALENR---VEALEALYDEAEEL 720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
1.33e-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: 52.38 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 33 MLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169 760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 185 QLAGAHQQvsALQQGAGIRDGVAEEEETVDlgpkrlwkDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLG 264
Cdd:TIGR02169 830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 265 TARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ 344
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958671317 345 ELLEVAEqKLQQTMRKAETLPEVEAELSQRIAALTK 380
Cdd:TIGR02169 980 EYEEVLK-RLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-469 |
1.43e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 253 SATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDKLENELANKESL 332
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671317 413 EKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
31-415 |
1.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 31 VNMLDEREKLLESLRESQETL------VATQSRLQDALHERDQLQRHLNSaLPQEFATLTRELsmcreqllereeeisel 104
Cdd:COG4717 94 QEELEELEEELEELEAELEELreelekLEKLLQLLPLYQELEALEAELAE-LPERLEELEERL----------------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 105 kAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4717 156 -EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 185 QLAGAH--QQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDD------TGRVEELQGLLEKQNYELSQARERLVTLSATV 256
Cdd:COG4717 235 ELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 257 TELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQC 336
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 337 EEKARHLQELLEVAEQ-----KLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLE--EKNQELARV 409
Cdd:COG4717 395 EEYQELKEELEELEEQleellGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAEL 474
|
....*.
gi 1958671317 410 RQREKM 415
Cdd:COG4717 475 LQELEE 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-351 |
1.88e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 112 RLLLEHLECLVSRHERslrMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR-----ERLRAALERVTTLEEQL 186
Cdd:COG4913 228 DALVEHFDDLERAHEA---LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 187 AGAHQQVSALQQGagiRDGVAEEEETVDlgpKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:COG4913 305 ARLEAELERLEAR---LDALREELDELE---AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 267 RRDLiksEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLE--------NELANKESLHRQCEE 338
Cdd:COG4913 379 AEEF---AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipaRLLALRDALAEALGL 455
|
250
....*....|....*.
gi 1958671317 339 KARHLQ---ELLEVAE 351
Cdd:COG4913 456 DEAELPfvgELIEVRP 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
272-470 |
2.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 272 KSEELSGKHQRDLREALAQKEDMEERIttlekrylaaqREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEEL-----------KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 352 QKLQ--QTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnkrLSDTVDR 429
Cdd:COG4717 123 KLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ----------LSLATEE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958671317 430 LLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
283-464 |
4.17e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQtmrkAE 362
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN----VR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 363 TLPEVEAeLSQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:COG1579 87 NNKEYEA-LQKEIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 1958671317 443 KERMAALEE-KGRLSEEIEKLRQ 464
Cdd:COG1579 163 AEREELAAKiPPELLALYERIRK 185
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
37-470 |
5.22e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 37 REKLLESLRESQETLVATQSRLQDALHERDQLQRHLNsalpQEFATLTRELSmcrEQLLEREEEISELKAERNNTRlllE 116
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELN----QLLRTLDDQWK---EKRDELNGELSAADAAVAKDR---S 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 117 HLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVLKalkslfEHHKALDEKVRERLRAALERVTTLEEQLAgahqqv 193
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLE------ERLKALTGKHQDVTAKYNRRRSKIKEQNN------ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 194 salQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVtLSATVTELEEDLGTARRDLIKS 273
Cdd:pfam12128 390 ---RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK-SRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 274 EELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQELLEVAEQ 352
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAlDELELQLFPQAGTLLHFLRKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 353 KLQQTMRK---------AETLPEV-----------------------------EAELSQRIAALTKA----EERHGNIEE 390
Cdd:pfam12128 546 DWEQSIGKvispellhrTDLDPEVwdgsvggelnlygvkldlkridvpewaasEEELRERLDKAEEAlqsaREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 391 HLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsesnERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKNARLDLRRLFD----------EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-470 |
5.67e-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: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 361 AETLpevEAELSQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958671317 423 LSDTVDRlLSESNERLQLHLKERMAALEekgRLSEEIEKLRQEVDQLK 470
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLLA---RLEKELAELAAELAELQ 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
207-470 |
5.86e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 207 AEEEETVDLGPKRLwKDDTGRVEELQGLLE--KQNYELSQARERLVTLSATVTELEEDLGTARR--------DLIKSEEL 276
Cdd:PTZ00121 1479 AEEAKKADEAKKKA-EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL 1557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 277 sgKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqq 356
Cdd:PTZ00121 1558 --KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--- 1632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 357 tmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNE 436
Cdd:PTZ00121 1633 --KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKK 1703
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958671317 437 RLQLHLKErmaalEEKGRLSEEIEKLRQE----VDQLK 470
Cdd:PTZ00121 1704 AEELKKKE-----AEEKKKAEELKKAEEEnkikAEEAK 1736
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-470 |
6.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 35 DEREKLLESLRESQETLVATQSRLQDALHERDQLqrhlNSALPQefatLTRELSMcreqLLEREEEISELKAERNNTRLL 114
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI----SSELPE----LREELEK----LEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 115 LEHLECLVSRHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 190 HQQVSALQQG-----------AGIRDGVAEEEETVdlgpkRLWKDDTGRVEELQGLLEK-QNYELSQARERLVTLSATVT 257
Cdd:PRK03918 327 EERIKELEEKeerleelkkklKELEKRLEELEERH-----ELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 258 ELEEDLG--TARRDLIKSE-----------------------ELSGKHQRDL-REALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:PRK03918 402 EIEEEISkiTARIGELKKEikelkkaieelkkakgkcpvcgrELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 312 ATsihdlndKLENELANKESLHRQCE--EKARHLQELLE-VAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNI 388
Cdd:PRK03918 482 LR-------ELEKVLKKESELIKLKElaEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 389 EEHLRQLEGQLEEKNQELARVRQR----------------EKMNEDHNK--RLSDTVDRLLSESnERLQLHLKERMAALE 450
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesveeleerlKELEPFYNEylELKDAEKELEREE-KELKKLEEELDKAFE 633
|
490 500
....*....|....*....|
gi 1958671317 451 EKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 634 ELAETEKRLEELRKELEELE 653
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-380 |
1.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 34 LDEREKLLESLRESQETLVATQSRLQDALherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 180 TTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQAR------------- 246
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeel 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 247 ERLVTLSATVTELEEDLGTARRDL--IKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958671317 325 --ELANKESLHRQCEEKARHLQE---LLEVAEQKLQQTMRKA--ETLPEVEAELSQRIAALTK 380
Cdd:COG4717 468 dgELAELLQELEELKAELRELAEewaALKLALELLEEAREEYreERLPPVLERASEYFSRLTD 530
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
31-468 |
1.83e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 31 VNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRH-------------LNSALPQEFATLTRELSMCREQLLER 97
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYemdynsylksiesLKKKIEEYSKNIERMSAFISEILKIQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 98 EEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspSGVSSEVEVLKALKSLFEHHKAL-------DEKVRE 170
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQDISSKVSSLNQRIR-----------ALRENLDELSRNMEMLNGQSVCPvcgttlgEEKSNH 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 171 RLRAALERVTTLEEQLAGAHQQVSALqqgagirdgvaeEEETVDLGPK--RLWKDDTGRVEELQGLLEKQNYELSQARER 248
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDI------------DEKIVDLKKRkeYLESEEINKSINEYNKIESARADLEDIKIK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 249 LVTLSATVTELE-----------EDLGTARRDLIKSeeLSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:PRK01156 538 INELKDKHDKYEeiknrykslklEDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKS 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 318 LND----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:PRK01156 616 YIDksirEIENEANNLNNKYNEIQENKILIEKLRG-----------KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 394 QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERLQlHLKERMAALEEKGRLSEEIEK------LRQEVD 467
Cdd:PRK01156 685 KSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE-SMKKIKKAIGDLKRLREAFDKsgvpamIRKSAS 759
|
.
gi 1958671317 468 Q 468
Cdd:PRK01156 760 Q 760
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
227-426 |
2.40e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEelsgkHQRDLREALAQKEDMEERITTLEKRYl 306
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALEAELAELPERL- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 307 aaqreatsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTmrKAETLPEVEaELSQRIAALtkaEERHG 386
Cdd:COG4717 149 -------------EELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQ-DLAEELEEL---QQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958671317 387 NIEEHLRQLEGQLEEKNQELARVrQREKMNEDHNKRLSDT 426
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEA 248
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
38-468 |
3.17e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 38 EKLLESLRESQETLVATQ---SRLQDALHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNTRLL 114
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 115 LEHLeclvsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618 293 APLA-------AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 195 ALQ-QGAGIRDGVAEEEETvdlgpkrLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKS 273
Cdd:TIGR00618 347 LQTlHSQEIHIRDAHEVAT-------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 274 EELSGKHQRDLREALAQKEDMEERITTLEKRY---LAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEV 349
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAqceKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 350 AEQklQQTMRKAETLPEVEAELSQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD 425
Cdd:TIGR00618 500 QEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958671317 426 TVDRLLSESNERLQL-----HLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR00618 578 CDNRSKEDIPNLQNItvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-371 |
3.24e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSG--KHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671317 305 YLAAQREATSIHDLNDKLENELANKEslhRQCEEKARHLQELLEVAEQKLQQTMRKAETL-PEVEAEL 371
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAEREELaAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-468 |
3.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 361 AETLPEVEA--------ELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958671317 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-459 |
6.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 30 MVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERN 109
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 110 NTRLLLEHLECLVSRHERSLRMT-VVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERVttleEQLAG 188
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK-LRKELREL----EKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 189 AHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARr 268
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE- 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 269 dliksEELSGKHQRDLREALAQKEDMEERITTLEKRY------LAAQREATSIHDLNDKLENELANKESLHRQCEEKARH 342
Cdd:PRK03918 570 -----EELAELLKELEELGFESVEELEERLKELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 343 LQELLEVAEQKLQQT--MRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN 420
Cdd:PRK03918 645 LRKELEELEKKYSEEeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958671317 421 KrlsdtvdrlLSESNERLQLHLKERmaALEEKGRLSEEI 459
Cdd:PRK03918 725 E---------LREKVKKYKALLKER--ALSKVGEIASEI 752
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
65-476 |
7.14e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 65 RDQLQRHLNSALpqefaTLTRELSMCREQLLEREEEISELKAErnntrlllehLECLVSRhERSLRMTVvkrQAQSPSgV 144
Cdd:PRK04863 278 ANERRVHLEEAL-----ELRRELYTSRRQLAAEQYRLVEMARE----------LAELNEA-ESDLEQDY---QAASDH-L 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 145 SSEVEVLKALKSLFEHHKALDEKVrERLRAALERVTTLEEQLAGAHQQVSALQQGA-GIRDGVAEEEETVDLGPKRL--W 221
Cdd:PRK04863 338 NLVQTALRQQEKIERYQADLEELE-ERLEEQNEVVEEADEQQEENEARAEAAEEEVdELKSQLADYQQALDVQQTRAiqY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 222 KDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLR---------EALAQKE 292
Cdd:PRK04863 417 QQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 293 DMEERITTLEK-RYLAAQREAtsihdlndkLENELANKESLHRQceekARHLQELLEVAEQKLQQTMRKAETLPEVEAEL 371
Cdd:PRK04863 497 VARELLRRLREqRHLAEQLQQ---------LRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 372 SQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESN---ERLQLHLKERMAA 448
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQdvtEYMQQLLEREREL 643
|
410 420
....*....|....*....|....*...
gi 1958671317 449 LEEKGRLSEEIEKLRQEVDQLKGRGGPF 476
Cdd:PRK04863 644 TVERDELAARKQALDEEIERLSQPGGSE 671
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-470 |
7.58e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDlgpkrlwkDDTGRVEELQGLLEKQNYELSQ 244
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD--------TVVSKIELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 325 ELankESLHRQCEEKARHLQELlevaEQKLQQTmrKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEgqleeknQ 404
Cdd:TIGR00606 942 KV---NDIKEKVKNIHGYMKDI----ENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR-------Q 1005
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671317 405 ELARVRQREKMNEDHNKRLsdTVDRLLSESNERLQLHLKE--RMAALEEKgrlsEEIEKLRQEVDQLK 470
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLR--KRENELKEVEEELKQHLKEmgQMQVLQMK----QEHQKLEENIDLIK 1067
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
22-484 |
7.98e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 22 ADANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:pfam12128 454 NQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 102 SELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDE---KVRER 171
Cdd:pfam12128 534 GTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRErldKAEEA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGIrdgVAEEEETVDLGPKRLwkddTGRVEELQGLLEKQ-NYELSQARERLV 250
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRRL----FDEKQSEKDKKNKAlAERKDSANERLN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 251 TLSATVTELEEDLGTARRDLIK-SEELSGKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDkleNELAN 328
Cdd:pfam12128 686 SLEAQLKQLDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK---RDLAS 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 329 K--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEAELsqriaaltkaeerhgniee 390
Cdd:pfam12128 763 LgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAI------------------- 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 391 hlRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSE---------------SNERLQLHLKERMAALEE-KGR 454
Cdd:pfam12128 824 --SELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGlrcemsklatlkedaNSEQAQGSIGERLAQLEDlKLK 901
|
490 500 510
....*....|....*....|....*....|
gi 1958671317 455 LSEEIEKLRQEVDQLKGrggpfVDGIHSRS 484
Cdd:pfam12128 902 RDYLSESVKKYVEHFKN-----VIADHSGS 926
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
235-470 |
9.51e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 235 LEKQNYELSQARERLVTLSATVTELEEDLgtarrdliKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS 314
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQE--------LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 315 IHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIaaLTKAE 382
Cdd:pfam02463 243 QELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK--LKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKL 462
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
....*...
gi 1958671317 463 RQEVDQLK 470
Cdd:pfam02463 401 SEEEKEAQ 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-412 |
1.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSgKHQRDLREALAQKEDM----------EERITTLEKRY--------- 305
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYswdeidvasaEREIAELEAELerldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 306 -LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEER 384
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*....
gi 1958671317 385 HG-NIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913 767 LReNLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
2.34e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI-----AALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958671317 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-470 |
2.37e-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: 44.63 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 230 ELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERIttlekrylaaQ 309
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN----------Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 310 REATSIHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHG 386
Cdd:TIGR04523 381 SYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 387 NIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALE----- 450
Cdd:TIGR04523 461 NTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekke 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958671317 451 --------------------------EKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 536 keskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQKSLK 581
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
308-472 |
2.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 308 AQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGN 387
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 388 IEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAAleekGRLSEEIEKLRQEVD 467
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA----QAHNEEAESLREDAD 352
|
....*
gi 1958671317 468 QLKGR 472
Cdd:PRK02224 353 DLEER 357
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
47-469 |
2.50e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 47 SQETLVATQSRLQDALHERDQLQRHLnsalpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVsrhE 126
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHL-----QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL---C 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 127 RSLRMTVVKRQAQSPSGVSSEVevLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQ-----GAG 201
Cdd:TIGR00618 508 GSCIHPNPARQDIDNPGPLTRR--MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQcdnrsKED 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 202 IRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQ----NYELS----QARERLVTLSATVTELEEDLG------TAR 267
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRlhlqQCSQELALKLTALHALQLTLTqervreHAL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 268 RDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLENELANKESLHRQceekarHLQELL 347
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASSSLGS------DLAARE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 348 EVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEG----QLEEKNQELARVRQREKMNEDHNKRL 423
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQffnrLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958671317 424 SDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-452 |
2.98e-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: 44.33 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 31 VNMLDEREKLL-ESLRESQETLVATQSRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLE 96
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 172 LRAALERVTTLEEQLAGAHQQVSALQQgagirdgvAEEEETVDL-----GPKRLWKDDTGRVEELQGLLEKQ-------- 238
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQ--------AREKEIHDLeiqltAIKTSEEHYLKEVEDLKTELEKEklknielt 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 239 ---------NYELSQ---------------------ARERLV----TLSATVTELEEDLGTARRDLI-----------KS 273
Cdd:pfam05483 492 ahcdkllleNKELTQeasdmtlelkkhqediinckkQEERMLkqieNLEEKEMNLRDELESVREEFIqkgdevkckldKS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 274 EELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLN---------------------DKLENELANKESL 332
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASAKQK 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI--AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYK 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1958671317 411 QREKMNEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALEEK 452
Cdd:pfam05483 732 NKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILKDK 786
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-478 |
3.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 272 KSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 352 QKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL- 430
Cdd:COG4372 101 EELESLQEEAEEL---QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALs 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958671317 431 LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVD 478
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
227-469 |
3.12e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVtlsatvtELEEDLGTAR-----RDLIKSEELSGKHQRDLREA----LAQKEDMEER 297
Cdd:COG5185 276 SSKRLNENANNLIKQFENTKEKIA-------EYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 298 ITTLEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveael 371
Cdd:COG5185 349 QESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD--------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 372 sqriaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSE-------SNERLQlHL 442
Cdd:COG5185 420 -------RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSvrskkedLNEELT-QI 490
|
250 260 270
....*....|....*....|....*....|..
gi 1958671317 443 KERMAAL-----EEKGRLSEEIEKLRQEVDQL 469
Cdd:COG5185 491 ESRVSTLkatleKLRAKLERQLEGVRSKLDQV 522
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
227-465 |
3.66e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLgtarRDLIKSEELSgkhQRDLREALAQKEdmeERITTLEKRYL 306
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL----LELTRVNELL---KAKFSEDGTQKK---MSSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 307 AAQREAtsihdlndKLENELANKESLHRQCEEKARHLQEL-LEVA--EQKLQQTMR-KAETLPEVEaELSQRIAALTKAE 382
Cdd:pfam15905 165 RNKLEA--------KMKEVMAKQEGMEGKLQVTQKNLEHSkGKVAqlEEKLVSTEKeKIEEKSETE-KLLEYITELSCVS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN-----------KRLSDTVDRLLSESNERLQLHLKErMAALEE 451
Cdd:pfam15905 236 EQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELskqikdlnekcKLLESEKEELLREYEEKEQTLNAE-LEELKE 314
|
250
....*....|....*
gi 1958671317 452 KGRL-SEEIEKLRQE 465
Cdd:pfam15905 315 KLTLeEQEHQKLQQK 329
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-324 |
3.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 81 ATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVE----VLKALKS 156
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 157 LFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRV----EELQ 232
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVErelrENLE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 233 GLLEKQNYELSQARERLVTL--------SATVTELEEDLGT-----ARRDLIKSEELSgKHQRDLREALaqKEDMEERIT 299
Cdd:COG4913 773 ERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESlpeylALLDRLEEDGLP-EYEERFKELL--NENSIEFVA 849
|
250 260
....*....|....*....|....*.
gi 1958671317 300 TLEKRYLAAQREATS-IHDLNDKLEN 324
Cdd:COG4913 850 DLLSKLRRAIREIKErIDPLNDSLKR 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-472 |
5.84e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 24 ANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-DRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 104 LKAERNNTRLLLEHLE-------CLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRA 174
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 175 ALERVTTLEEQLAGAHQQ-VSALQQGAGIR--------DGVAEEE----ETVDLGPKRLWKDDTGRVEELQGLLEKQN-- 239
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERyATAIEVAAGNRlnnvvvedDAVAKEAiellKRRKAGRATFLPLNKMRDERRDLSILSEDgv 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 240 -------YELSQARERLVTLSATVTELEEDLGTARRDLI-------------KSEELSGKHQR------DLREALAQKED 293
Cdd:TIGR02169 599 igfavdlVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGkyrmvtlegelfeKSGAMTGGSRAprggilFSRSEPAELQR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR-------QCEEKARHLQELLEVAEQKLQQTMRKAET--- 363
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 364 -LPEVEAELSQRIAALTKAEERHGNIEEHL-----RQLEGQLEEKNQELARVRQR-----EKMNEDHNKR--LSDTVDRL 430
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARlreieQKLNRLTLEKeyLEKEIQEL 838
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958671317 431 LSESNErLQLHLKERMAALEE----KGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 839 QEQRID-LKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESR 883
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-411 |
6.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958671317 366 EVEA-ELSQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRQ 411
Cdd:PRK11281 108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQN 142
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
38-340 |
6.44e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 38 EKLLESLRESQE-TLVATQSRLQ------DALHERDQLQRHLNsalpqefaTLTRELSmcreqllEREEEISELKAERNN 110
Cdd:PLN02939 131 EDLVGMIQNAEKnILLLNQARLQaledleKILTEKEALQGKIN--------ILEMRLS-------ETDARIKLAAQEKIH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 111 TRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKslfEHHKALDEKVrERLRAALERVTTLEEQLAGAH 190
Cdd:PLN02939 196 VEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDDI-QFLKAELIEVAETEERVFKLE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 191 QQVSALQqgAGIRD----GVAEEEETVDLGPKR---LWKddtgRVEELQGLLEKQNYELSQArerlvtlsATVTELEEDL 263
Cdd:PLN02939 264 KERSLLD--ASLREleskFIVAQEDVSKLSPLQydcWWE----KVENLQDLLDRATNQVEKA--------ALVLDQNQDL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 264 gtarRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQRE--------ATSIHDLNDKLENelANKESLHRQ 335
Cdd:PLN02939 330 ----RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEihsyiqlyQESIKEFQDTLSK--LKEESKKRS 403
|
....*
gi 1958671317 336 CEEKA 340
Cdd:PLN02939 404 LEHPA 408
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-472 |
7.94e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 235 LEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREAts 314
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 315 ihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGnIEEHLRQ 394
Cdd:COG4372 118 -----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-LDELLKE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671317 395 LEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-472 |
8.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKvRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETv 213
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 214 dlgpKRLWKDDTGRVEELqgllEKQNYELSQARERLVTLSATVTELEEDLGTARRDLikseelSGKHQRDLREALAQKED 293
Cdd:COG4717 138 ----EAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 294 MEERITTLEKRYLAAQREATSIHDLNDKLENE------------------------------------------------ 325
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 326 ---------LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVE-AELSQRIAALTKAEERHGNIEEHLRQL 395
Cdd:COG4717 284 gllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 396 E-GQLEEKNQEL-------------ARVRQREKMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEK-GRLSEEIE 460
Cdd:COG4717 364 QlEELEQEIAALlaeagvedeeelrAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410
....*....|..
gi 1958671317 461 KLRQEVDQLKGR 472
Cdd:COG4717 443 ELEEELEELREE 454
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
281-470 |
9.65e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 281 QRDLREALAQKEDMEERITTLekRYLAAQREATSIHDLND-KLENE---LANKESLHRQCEEKARHLQELLEVAEQKLQQ 356
Cdd:COG0497 171 KKELEELRADEAERARELDLL--RFQLEELEAAALQPGEEeELEEErrrLSNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 357 TMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekMNEDHN--KRLSDTVDRLLSes 434
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER--LALLRRlaRKYGVTVEELLA-- 324
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958671317 435 nerLQLHLKERMAALEEkgrLSEEIEKLRQEVDQLK 470
Cdd:COG0497 325 ---YAEELRAELAELEN---SDERLEELEAELAEAE 354
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-486 |
9.76e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 269 DLIKSE-ELSGKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQCEEKARHLQEL- 346
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLn 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 347 -------LEVAE-QKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:PHA02562 262 taaakikSKIEQfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958671317 419 HNKRLSdTVDRLLS---ESNERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGIHSRSHV 486
Cdd:PHA02562 342 LKNKIS-TNKQSLItlvDKAKKVKAAIEE---LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIV 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-472 |
9.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELSQRIAALT 379
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEI 459
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170
....*....|...
gi 1958671317 460 EKLRQEVDQLKGR 472
Cdd:COG4717 202 EELQQRLAELEEE 214
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
258-604 |
9.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 258 ELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESL--HRQ 335
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 336 CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnIEEHLRQL----EGQLEEKNQELARVRQ 411
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLslatEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 412 REKMNEDHNKRLSDTVDRLlsesnerlqlhlKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFV---DGIHSRSHVGS 488
Cdd:COG4717 207 RLAELEEELEEAQEELEEL------------EEELEQLENELEAAALEERLKEARLLLLIAAALLAllgLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 489 TADVRFSLSTAAHVPPGLHRRYTALREESAKDWKPAPLPGVLAATTTPAFDSDpeiSDVDEDEPGGLVGTQVDVISpggh 568
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA---LGLPPDLSPEELLELLDRIE---- 347
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958671317 569 sDAQTLammlQEQLDAINQEIRMIQEEKESTELRAE 604
Cdd:COG4717 348 -ELQEL----LREAEELEEELQLEELEQEIAALLAE 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-476 |
1.03e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG-IRDGVA--EEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYEL 242
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIqYQQAVQalEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEV 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 243 SQARERLVTLSATVTELEEDLGTARRdlIKSE-ELSGKHQRdLREALAQKEdmeerittlEKRYLAAQREAtsihdlndk 321
Cdd:COG3096 458 LELEQKLSVADAARRQFEKAYELVCK--IAGEvERSQAWQT-ARELLRRYR---------SQQALAQRLQQ--------- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 322 LENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEE 401
Cdd:COG3096 517 LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671317 402 KNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE----RLQLHLKERMAALEEKgRLSEEIEKLRQEVDQLKGRGGPF 476
Cdd:COG3096 593 RIKELAARAPAWLAAQDALERLREQSGEALADSQEvtaaMQQLLEREREATVERD-ELAARKQALESQIERLSQPGGAE 670
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
367-470 |
1.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 367 VEAELSQRIAALTKAEERHGNIEEHlrQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLHLKERM 446
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEAR 454
|
90 100
....*....|....*....|....
gi 1958671317 447 AALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLE 478
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
273-410 |
1.07e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 273 SEELSGKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039 45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671317 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-470 |
1.28e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELSQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK---LRQE 465
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASavdLDAK 195
|
....*
gi 1958671317 466 VDQLK 470
Cdd:pfam04012 196 LEQAG 200
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-360 |
1.57e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.27 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 172 LRAALERVTTLEEQLAGAHQQVSALQqgagirdgvaeeEETVDLgpKRLWKDDT-------GRVEELQGLLEKQNYELSQ 244
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKLEELR------------KENRLL--KRLQKRQEkalgkyeGTESELPQLIARHNEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 245 ARERLVTLSATVTELEEDLGTARRDLIKSEElSGKHQRDLREA--LAQKEDMEERITTLEKRYLAAQREatsIHDLNDKL 322
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRD-QLKRLEKLSEDknLAEREELQKKLEQLEAKLEDKDEK---IQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958671317 323 EN-------ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:pfam15619 148 ELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
257-472 |
1.64e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 257 TELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERIT--TLEKRYLAAQREATSIHDLNDKLENELANKESLHR 334
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 335 QCEEKARHLQELLEVAEQKLQQTmrkaetLPEVEAELSQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQ------EIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671317 414 KMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam02463 310 VDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-412 |
2.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDlgpkrlwkddtgRVEELQGllekqnyELSQ 244
Cdd:COG3206 170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELES-------QLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 245 ARERLVTLSATVTELEEDLGTARRDLikSEELSGKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 325 ELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:COG3206 299 QIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
....*...
gi 1958671317 405 ELARVRQR 412
Cdd:COG3206 366 LYESLLQR 373
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
227-411 |
2.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEdmeerittlekrYL 306
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS------------YL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 307 AAQREATSIHDLNDKLEN----ELANKESLHRQCEEKAR--HLQELLEVAEQKLQQTMRKAET-LPEVEAELSQRIAALT 379
Cdd:COG3883 106 DVLLGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEAQQAEQEALLA 185
|
170 180 190
....*....|....*....|....*....|..
gi 1958671317 380 KAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
228-470 |
3.01e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 228 VEELQGLLEKqnYELSQARERLVTLSATVTELEEDLGTARRDLiksEELSGKHQRDlREALaqkEDMEERITTLEKRYLA 307
Cdd:pfam06160 69 LFEAEELNDK--YRFKKAKKALDEIEELLDDIEEDIKQILEEL---DELLESEEKN-REEV---EELKDKYRELRKTLLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 308 aQREA--TSIhdlnDKLENELANKESLHRQCEE--------KARHLQELLEVAEQKLQQTMRK--------AETLPEVEA 369
Cdd:pfam06160 140 -NRFSygPAI----DELEKQLAEIEEEFSQFEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelKTELPDQLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 370 ELSQRIAALTKAEER--HGNIEEHLRQLEGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQLHl 442
Cdd:pfam06160 215 ELKEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVE- 290
|
250 260
....*....|....*....|....*...
gi 1958671317 443 kermaalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam06160 291 -------KNLPEIEDYLEHAEEQNKELK 311
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
261-470 |
3.43e-03 |
|
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: 40.77 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 261 EDLGTARRDLIKS-EELsgkhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKES----L 332
Cdd:TIGR04523 155 EKLNNKYNDLKKQkEEL----ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKqnnqL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 333 HRQCEEKARHLQEL---LEVAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLE----EKNQE 405
Cdd:TIGR04523 231 KDNIEKKQQEINEKtteISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQKEQD 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 406 LAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 308 WNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
241-412 |
3.52e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 241 ELSQARERLVTLSATVTELEEDLG--TARRDLIKS---------------EELSGKHQR-----DLREALAQ-KEDMEER 297
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAerARELDLLRFqleeleaaalqpgeeEELEEERRRlsnaeKLREALQEaLEALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ----------ELLEVAEQKLQ---QTMRK---- 360
Cdd:COG0497 239 EGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvt 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958671317 361 AETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-465 |
3.74e-03 |
|
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: 40.77 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 235 LEKQNYELSQARERLvtlSATVTELEEDLgtarRDLIKSE---ELSGKHQRDLREALaqkedmEERITTLEKRYLAAQRE 311
Cdd:TIGR04523 417 LQQEKELLEKEIERL---KETIIKNNSEI----KDLTNQDsvkELIIKNLDNTRESL------ETQLKVLSRSINKIKQN 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 312 AtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEH 391
Cdd:TIGR04523 484 L-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671317 392 LR--QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK-GRLSEEIEKLRQE 465
Cdd:TIGR04523 554 LKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKKiSSLEKELEKAKKE 625
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
272-474 |
4.28e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 272 KSEELSGKHQRDLREALAQKEdMEERITTLEKRylAAQREATSIHDLNDKLenelanKESLHRQCEEKARHLQELLEVAE 351
Cdd:PLN03229 555 KAEKLKAEINKKFKEVMDRPE-IKEKMEALKAE--VASSGASSGDELDDDL------KEKVEKMKKEIELELAGVLKSMG 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 352 QKLQQTMRKAETLPEVEA--ELSQRIAALTkaEERHGNIEEHLR--QLEGQLEEKNQELARVrqrekmnedhnkrlSDTV 427
Cdd:PLN03229 626 LEVIGVTKKNKDTAEQTPppNLQEKIESLN--EEINKKIERVIRssDLKSKIELLKLEVAKA--------------SKTP 689
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958671317 428 DRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:PLN03229 690 DVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAA 736
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
166-383 |
4.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagirdgvaeeeetvdlgpkrlwkddtgRVEELQGLLEKQNYELSQA 245
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNE----------------------------EYNELQAELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 246 RERLVTLSATVTELEEDLGTARRDLIKSEELSGkhqrdLREALAQKEDMEE---RITTLEKRYLAAQREATSIHDLNDKL 322
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARALYRSGGSVS-----YLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAEL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958671317 323 ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEE 383
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
135-470 |
5.35e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRdgvaEEEETV 213
Cdd:pfam09731 88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ----AVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 214 DLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSeelsGKHQRDLREALAQKED 293
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 294 MEERITTLEKRYLAA-----QREATSIHD---LNDKLENELANKE------SLHRQCEEKARHLQELLEVAEQKLQQTMR 359
Cdd:pfam09731 240 SLAKLVDQYKELVASerivfQQELVSIFPdiiPVLKEDNLLSNDDlnsliaHAHREIDQLSKKLAELKKREEKHIERALE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 360 KA-ETLPEVEAELSQRIaaltkaeerhgniEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTV 427
Cdd:pfam09731 320 KQkEELDKLAEELSARL-------------EEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVL 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958671317 428 DRLLSESNERLQLHLKERMAalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam09731 386 VEQEIELQREFLQDIKEKVE--EERAGRLLKLNELLANLKGLE 426
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-470 |
5.35e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.06 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 360 -------KAETLPEVEAELSQRIAALTKAEE------------RHGNieEHLRQLEGQLE---EKNQELARVRQREKMNE 417
Cdd:pfam05622 81 arddyriKCEELEKEVLELQHRNEELTSLAEeaqalkdemdilRESS--DKVKKLEATVEtykKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 418 DHN----------------------------KRLSDTVDRLLSESN--ERLQL---HLKERMAALE-EKGRLSEEIEKLR 463
Cdd:pfam05622 159 ERNaeymqrtlqleeelkkanalrgqletykRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkEKERLIIERDTLR 238
|
....*..
gi 1958671317 464 QEVDQLK 470
Cdd:pfam05622 239 ETNEELR 245
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
229-353 |
5.95e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.04 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 229 EELQGL-LEKQNYE--LSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKhqrdlreALAQKEDMEERITTLEKRY 305
Cdd:pfam05911 688 EEFEQLkSEKENLEveLASCTENLESTKSQLQESEQLIAELRSELASLKESNSL-------AETQLKCMAESYEDLETRL 760
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958671317 306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK 353
Cdd:pfam05911 761 TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
106-411 |
6.90e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 106 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPsgvssevEVLKALKSLFehhKALDEKVRERLRAALERVTTLEEQ 185
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-------ETSAELNQLL---RTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 186 LAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEE-LQGLLEKQNyELSQARERLVtlSATVTELEEDLG 264
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErLKALTGKHQ-DVTAKYNRRR--SKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 265 TARRDLIKSEELSGKHQRDLREALAQ-----KEDMEERITTLEKrylAAQREATSIHDLNDKLENELANKESLHRQceek 339
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQAleselREQLEAGKLEFNE---EEYRLKSRLGELKLRLNQATATPELLLQL---- 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671317 340 aRHLQELLEVAEQKLQQTMRKAETLPEveaelsqriaALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:pfam12128 467 -ENFDERIERAREEQEAANAEVERLQS----------ELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
258-470 |
7.42e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 258 ELEEDLGTARRDLI-KSEELSGKHQRDLREALAQkeDMEERITTLE-------KRYLAAQREATSIHDLNDK-------- 321
Cdd:cd16269 94 KLMEQLEEKKEEFCkQNEEASSKRCQALLQELSA--PLEEKISQGSysvpggyQLYLEDREKLVEKYRQVPRkgvkaeev 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 322 LENELANKESlhrqcEEKArHLQ--ELLEVAEQKLQQTMRKAETLpEVEAELSQRIAALT--KAEERHGNIEEHLRQLEG 397
Cdd:cd16269 172 LQEFLQSKEA-----EAEA-ILQadQALTEKEKEIEAERAKAEAA-EQERKLLEEQQRELeqKLEDQERSYEEHLRQLKE 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958671317 398 QLEEKNQelarvrqrekmnedhnkrlsdtvdRLLSESNERLQLHLKErMAALEEKGrLSEEIEKLRQEVDQLK 470
Cdd:cd16269 245 KMEEERE------------------------NLLKEQERALESKLKE-QEALLEEG-FKEQAELLQEEIRSLK 291
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-470 |
7.57e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671317 343 LQELLEVAEQKLQQTMRKAETLPEVE-AELSQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQR---EKMNED 418
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERElTEEEEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERElseARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958671317 419 HNKRLSDTVDRLLSEsNERLQLHLKErmaaleekgrLSEEIEKLRQEVDQLK 470
Cdd:COG2433 459 REIRKDREISRLDRE-IERLERELEE----------ERERIEELKRKLERLK 499
|
|
| |
