|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
269-531 |
4.85e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 349 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG 428
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 429 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESnERLQLHLKERMAALEEKNVLIQESETFRKNL 508
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260
....*....|....*....|...
gi 1370463116 509 EESLHDKERLAEEIEKLRSELDQ 531
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-534 |
9.78e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 347 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 426
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 427 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 502
Cdd:TIGR02168 871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
|
250 260 270
....*....|....*....|....*....|..
gi 1370463116 503 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-472 |
1.17e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 83 QDIESLTGGLAGSKGADPPEFAAL--TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ 160
Cdd:TIGR02168 650 LDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 161 AQSPSGVSSEVEVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESE 240
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 241 HLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT 320
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 321 KYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQT 399
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEA 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 400 MRKAETLPEVEAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNK 463
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARE 1032
|
....*....
gi 1370463116 464 RLSDTVDRL 472
Cdd:TIGR02168 1033 RFKDTFDQV 1041
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-535 |
1.85e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 263 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 342
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 343 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 422
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 423 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 501
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....
gi 1370463116 502 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-541 |
2.12e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 288 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 367
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 368 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 440
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 441 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 510
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|.
gi 1370463116 511 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-527 |
8.28e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 174 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 253
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 254 KRlsngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 333
Cdd:TIGR02168 780 AE------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 334 EDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAEL 413
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 414 AQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEE 493
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
|
330 340 350
....*....|....*....|....*....|....*
gi 1370463116 494 KNVL-IQESETFRKNLEESLHDKERLAEEIEKLRS 527
Cdd:TIGR02168 987 VNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-529 |
1.61e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLAGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSL 199
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 200 ERVSALEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEGMEPGQK--VHEKRLSNG---------SIDSTDET- 267
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGilgvlseliSVDEGYEAa 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 -----------------SQIVELQELLEKQNYEMAQMKE----RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR-- 324
Cdd:TIGR02168 539 ieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKal 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 325 -----------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQ 386
Cdd:TIGR02168 619 syllggvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 387 ERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN 462
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463116 463 KRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:TIGR02168 778 AEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
102-589 |
4.02e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 181
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI 261
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 262 DSTDETSQIVELqellekqnyemaqmKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 341
Cdd:PRK02224 336 AAQAHNEEAESL--------------REDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 342 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAA 419
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 420 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNV 496
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 497 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTTKVIR 576
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDER 625
|
490
....*....|...
gi 1370463116 577 RPRRGRMGVRRDE 589
Cdd:PRK02224 626 RERLAEKRERKRE 638
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
290-533 |
5.62e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 290 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 369
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 370 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 445
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 446 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 523
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
|
250
....*....|
gi 1370463116 524 KLRSELDQLK 533
Cdd:TIGR02168 465 ELREELEEAE 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
268-497 |
6.49e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 347
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 348 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERh 427
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE- 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 428 gnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVL 497
Cdd:COG1196 426 --LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
269-539 |
7.13e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 349 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 428
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 429 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 507
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 1370463116 508 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-494 |
1.31e-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: 68.56 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 114 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKALKslfehhkaldEKVRE 193
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQEE----------EKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 194 RLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMAssegstesehlegmepgqKVHEKRLSNGSIDSTDETSQIVEL 273
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEAR---IEELEE------------------DLHKLEEALNDLEARLSHSRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 274 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYLSAQRE 353
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 354 STSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEER 433
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463116 434 MRHLEgQLEEKNQELQRARQR-EKMN-------EEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEK 494
Cdd:TIGR02169 950 ELSLE-DVQAELQRVEEEIRAlEPVNmlaiqeyEEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
253-532 |
4.20e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 253 EKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 332
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 333 KEDMEERIttlekrylsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 412
Cdd:TIGR02169 781 LNDLEARL---------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 413 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARqrekmnEEHNKRLSDTVDRL--LTESNERLQLHLKERMAA 490
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSELKAK 925
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370463116 491 LEEKNVLIQESETFRKNLEES---LHDKERLAEEIEKLRSELDQL 532
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-531 |
7.82e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 320 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHdmnDKLENELANKEAILRQMEEknRQLQERLE 390
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERY---RELKEELKELEAELLLLKL--RELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 391 LAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 470
Cdd:COG1196 243 ELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463116 471 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 531
Cdd:COG1196 320 ELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-535 |
1.98e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGglagskgadppEFAALTKELNACREQLLE 119
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEE-----------ELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTV------VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRE 193
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 194 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVEL 273
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 274 QELLEKQNYEMAQMKERLAALSSRVGE---VEQEAETARKDLIKTEEMNTKYQRDIREAMA---QKEDMEERITTLEKRy 347
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVligVEAAYEAALEAALAAALQNIVVEDDEVAAAAieyLKAAKAGRATFLPLD- 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 348 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 427
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 428 GNIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRK 506
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
490 500 510
....*....|....*....|....*....|....*
gi 1370463116 507 NLEESLHDKERLAEE------IEKLRSELDQLKMR 535
Cdd:COG1196 741 LLEEEELLEEEALEElpeppdLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-541 |
3.16e-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: 64.31 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 265 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 338 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 417
Cdd:TIGR02168 337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 495
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370463116 496 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-539 |
5.04e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 255 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 334
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 335 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 414
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 415 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 494
Cdd:TIGR02169 800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370463116 495 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 539
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-460 |
6.07e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 189 EKVRERLRVSLERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKRLSNGSIDSTD 265
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEK 345
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL---KREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 346 RYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaetlpeveaelaqrIAALTKAEE 425
Cdd:TIGR02169 411 LQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL-----------------AADLSKYEQ 469
|
250 260 270
....*....|....*....|....*....|....*
gi 1370463116 426 RHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 460
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
192-539 |
7.68e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 192 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 268
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 346
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 347 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 425
Cdd:PRK04863 415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 426 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 503
Cdd:PRK04863 494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565
|
330 340 350
....*....|....*....|....*....|....*.
gi 1370463116 504 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:PRK04863 566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
102-457 |
1.34e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGVSS 169
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 170 EVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEgmepgQ 249
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----E 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 250 KVHEKRLS-------------NGSIDSTDETSQ---------IVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAET 307
Cdd:COG4717 244 RLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 308 ARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQE 387
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKE 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 388 RLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQREKM 457
Cdd:COG4717 403 ELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEE 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-427 |
1.81e-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: 58.53 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 43 DRLLDTLRETQESL-SLAQQRLQDVIYDRdsLQRQLNSA----LPQDIESLTGGLAGSKGadppEFAALTKELNACREQL 117
Cdd:TIGR02168 189 DRLEDILNELERQLkSLERQAEKAERYKE--LKAELRELelalLVLRLEELREELEELQE----ELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 118 LEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKaldekvrERLRV 197
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQK-------QILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 198 SLERvsaLEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdetSQIVELQELL 277
Cdd:TIGR02168 310 RLAN---LERQLEELEAQLEELESKLDELAEELAELE---------------------------------EKLEELKEEL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 278 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyLSAQRESTSI 357
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEE 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 358 HDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 427
Cdd:TIGR02168 433 AEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
323-538 |
1.90e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 323 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 402
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 403 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 464
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463116 465 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGS 538
Cdd:COG4942 176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-471 |
2.33e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKgadppEFAALTKELNACREQLL 118
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-----ALEEAAEEEAELEEEEE 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 119 EKEEEISELKAERNNTRLLLEHLecLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfehhKALDEKVRERLRVS 198
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAEL--LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL----RGLAGAVAVLIGVE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 199 LERVSALEEELAAANQEIVALREQNVHIQR-----------------KMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI 261
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIeylkaakagratflpldKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 262 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERIT 341
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 342 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT 421
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463116 422 KAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 471
Cdd:COG1196 774 REIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
265-530 |
2.73e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 57.00 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 344
Cdd:pfam19220 45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 424
Cdd:pfam19220 125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 425 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNerlqlhlkeRMAALEeknVLIQESET 503
Cdd:pfam19220 205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASLRMKLEALTA---------RAAATE---QLLAEARN 269
|
250 260
....*....|....*....|....*..
gi 1370463116 504 FRKNLEESLHDKERLAEEIEKLRSELD 530
Cdd:pfam19220 270 QLRDRDEAIRAAERRLKEASIERDTLE 296
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
109-514 |
3.10e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 109 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 188
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 189 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRLSNgSIDSTDE 266
Cdd:PTZ00121 1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 347 ylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRI 417
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKA 1704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEK 494
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
410 420
....*....|....*....|
gi 1370463116 495 nvLIQESETFRKNLEESLHD 514
Cdd:PTZ00121 1785 --LDEEDEKRRMEVDKKIKD 1802
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
268-460 |
4.28e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 347
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 348 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 408
Cdd:COG3883 93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1370463116 409 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 460
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-535 |
5.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 324 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 397
Cdd:COG4913 238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 398 QTMRKAETLPEVEAELAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrLLTESN 477
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP-ASAEEF 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 478 ERLQLHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG4913 383 AALRAEAAALLEALEE------ELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-540 |
1.09e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSLFEHHKALDEKVRER 194
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 195 LRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNGSIDSTDETSQIVELQ 274
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSEF---YEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 275 ELLEKqnyemaqmkerLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdIREAMAQKEDMEERIT-----TLEKRYLS 349
Cdd:PRK03918 328 ERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTgltpeKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 350 AQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEVEAELAQRIAALTKA 423
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 424 EERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKnvliqeset 503
Cdd:PRK03918 472 EEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGE--------- 540
|
410 420 430
....*....|....*....|....*....|....*..
gi 1370463116 504 fRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLI 540
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-535 |
1.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLSNGS 260
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 261 IDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-----------AETARKDLIK--TEEMNtKY 322
Cdd:PRK03918 386 PEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAELK-RI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 323 QRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQKLQQ 398
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 399 TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLlt 474
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-- 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 475 esnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE---------RLAEEIEKLRSELDQLKMR 535
Cdd:PRK03918 622 ---KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELAGLRAELEELEKR 688
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
39-532 |
1.63e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIE--SLTGGLAGSKGADPPEFAALTKELNACREQ 116
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 117 LLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRM-TVVKRQAQSPSGVSSEVEvlKALKSLFEHHKALDEK--VRE 193
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPgpLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 194 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTDET 267
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 SQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRY 347
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 348 LSAQRESTSIHDMNDKLEnELANKEAILR---QMEEKNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTK 422
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKE-MLAQCQTLLReleTHIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKA 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 423 AEERHGNIEER----------MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 492
Cdd:TIGR00618 759 RTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1370463116 493 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-479 |
2.29e-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: 54.00 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 347
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 348 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 415
Cdd:COG4942 107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463116 416 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 479
Cdd:COG4942 186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
185-516 |
2.62e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 185 KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDST 264
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 265 DETSQIVE---LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--------DLIKTEEMntKYQRDIREAMAQK 333
Cdd:PTZ00121 1493 EEAKKKADeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 334 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAE 404
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 405 TLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHL 484
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAE 1725
|
330 340 350
....*....|....*....|....*....|..
gi 1370463116 485 KERMAALEEknvLIQESETFRKNLEESLHDKE 516
Cdd:PTZ00121 1726 EENKIKAEE---AKKEAEEDKKKAEEAKKDEE 1754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-556 |
3.08e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 275 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 349
Cdd:TIGR02168 203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 350 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 429
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 430 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 509
Cdd:TIGR02168 350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370463116 510 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 556
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
214-530 |
3.26e-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: 54.57 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 214 QEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKVHEKRLSNGSI-DSTDETSQIVELQELLEKQNYEMAQMKER 290
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQqlRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 291 LAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD----------M 360
Cdd:COG3096 916 GKALA----QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgllgensdL 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 361 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEERhgnIEERMR 435
Cdd:COG3096 986 NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEER---ARIRRD 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 436 HLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEeknvLIQESetfrkNLEE 510
Cdd:COG3096 1063 ELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR----LARDN-----DVER 1131
|
330 340
....*....|....*....|
gi 1370463116 511 SLHDKERLAEEIEKLRSELD 530
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSD 1151
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-528 |
4.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 362 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 438
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 439 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 511
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
170
....*....|....*..
gi 1370463116 512 LHDKERLAEEIEKLRSE 528
Cdd:COG4913 779 RARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
284-695 |
4.67e-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: 53.97 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 284 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 363
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 364 LENELANKEAI----LRQMEEKNRQLQERLELAEQKLQqtmrkaETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEG 439
Cdd:pfam15921 304 IQEQARNQNSMymrqLSDLESTVSQLRSELREAKRMYE------DKIEELEKQLVLANSELTEARTERDQFSQESGNLDD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 440 QLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEEKN 495
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKN 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 496 VLIQESETFRKNLEESlhdKERLAEEIEKLRSELDQLKmrtgsliepTIPRTHLDTSAELRYSVGSLVDSQSDyrTTKVi 575
Cdd:pfam15921 458 ESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLE---------SSERTVSDLTASLQEKERAIEATNAE--ITKL- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 576 rrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLAMM 652
Cdd:pfam15921 523 ----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEKAQ 594
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1370463116 653 LQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 695
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-451 |
5.33e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 102 EFAALTKELNACREQLLEKEEEISELKAERnntRLLLEHLEclvsRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLF 181
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEE---YELLAELA----RLEQDIARLEERRRELE----ERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 182 EHHKALDEKVRERlrvsLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRlsngsi 261
Cdd:COG1196 330 EELEELEEELEEL----EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA------ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 262 dstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 341
Cdd:COG1196 400 ------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE-------EEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 342 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAELAQRIAALT 421
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAALEAAL 544
|
330 340 350
....*....|....*....|....*....|
gi 1370463116 422 KAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
265-685 |
8.60e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 344
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 345 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 424
Cdd:TIGR02169 232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 425 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 503
Cdd:TIGR02169 298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 504 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 583
Cdd:TIGR02169 345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 584 GVRRDEPKVKS--LGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 661
Cdd:TIGR02169 409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482
|
410 420
....*....|....*....|....
gi 1370463116 662 KEIRLIQEEKESTELRAEEIENRV 685
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERV 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-533 |
8.73e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR- 192
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHEl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 193 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEpgQKVHEKRLSNGSIDSTDETSQIV 271
Cdd:PRK03918 364 yEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKAIEELKKAKGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 272 -------ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----------------RDIR 327
Cdd:PRK03918 442 grelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlkeleeklkkynlEELE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 328 EAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTM 400
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFY 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 401 RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERL 480
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRE 674
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1370463116 481 QLHLKERMAALEEknvLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:PRK03918 675 LAGLRAELEELEK---RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-539 |
1.16e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 291 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 368
Cdd:PRK03918 127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 369 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 445
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 446 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 517
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362
|
250 260
....*....|....*....|..
gi 1370463116 518 LAEEIEKLRSELDQLKMRTGSL 539
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGL 384
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
33-539 |
1.30e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 33 QLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQrQLNSALPQDIESLTGGLAGSKgadppefaaltKELNA 112
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKRE-----------KELSL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 113 CREQ---LLEKEE----EISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:pfam15921 396 EKEQnkrLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 186 ALDEKVRERL---RVSLER----VSAL-------EEELAAANQEIVALREQnvhIQRKMASSEG-STESEHLEGMEPGQK 250
Cdd:pfam15921 475 EMLRKVVEELtakKMTLESsertVSDLtaslqekERAIEATNAEITKLRSR---VDLKLQELQHlKNEGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 251 VHEKRLSngsidstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA 329
Cdd:pfam15921 552 ALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 330 MAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPE 408
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 409 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERM 488
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKH 765
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1370463116 489 AALEEKNVLIQESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:pfam15921 766 FLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
192-527 |
1.89e-06 |
|
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: 51.88 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 192 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE---------SEHLEGMEPGQKVHEKrlsngsID 262
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESdleqdyqaaSDHLNLVQTALRQQEK------IE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 263 STDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 342
Cdd:COG3096 351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 343 LEKrylsaQRESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 416
Cdd:COG3096 422 LEK-----ARALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 417 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 496
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568
|
330 340 350
....*....|....*....|....*....|.
gi 1370463116 497 LIQESETFRKNLEESLHDKERLAEEIEKLRS 527
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
269-426 |
2.28e-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: 49.92 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR-- 346
Cdd:COG1579 8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 347 -------YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAA 419
Cdd:COG1579 84 nvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEE 160
|
....*..
gi 1370463116 420 LTKAEER 426
Cdd:COG1579 161 LEAEREE 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
269-454 |
2.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:COG4913 250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 349 SAQRE-STSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAELAQRIAALTKAEER 426
Cdd:COG4913 327 ELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 1370463116 427 HGNIEERMRHLEGQLEEKNQELQRARQR 454
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-533 |
3.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 324 RDIREAMAQKED----MEERITTLEKRYLSAQRestsIHDMNDKLENelANKEAILRQMEEKNRQLqERLELAEQKLQQT 399
Cdd:TIGR02168 182 ERTRENLDRLEDilneLERQLKSLERQAEKAER----YKELKAELRE--LELALLVLRLEELREEL-EELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 400 MRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------ 472
Cdd:TIGR02168 255 LEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELesklde 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463116 473 ----LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 533
Cdd:TIGR02168 335 laeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
350-537 |
4.29e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 350 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 429
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 430 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 493
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370463116 494 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 537
Cdd:PRK02224 357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
205-435 |
5.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 205 LEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgQKVHEKRLSNGSIDSTDET----SQIVELQELLEKQ 280
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAE--------------AALEEFRQKNGLVDLSEEAklllQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 281 NYEMAQMKERLAALSSRVGEVEQEAETARKDlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDM 360
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463116 361 NDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 435
Cdd:COG3206 304 RAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
343-535 |
5.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 343 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpevEAELAQRIAALTK 422
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE-------LEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 423 AEERHGNIEERmRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESE 502
Cdd:COG4717 124 LLQLLPLYQEL-EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190
....*....|....*....|....*....|...
gi 1370463116 503 TFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
367-524 |
6.16e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 367 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 446
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 447 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 523
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 1370463116 524 K 524
Cdd:PRK12704 180 E 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-390 |
6.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQspsgvssevevlkalkslfeh 183
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA--------------------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 184 hkALDEKvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDS 263
Cdd:COG4913 672 --ELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-----KELEQAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 264 TDETSQivELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQRDIREAMAQKEDMEE---R 339
Cdd:COG4913 744 RLELRA--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEylaL 820
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370463116 340 ITTLEKRYLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 390
Cdd:COG4913 821 LDRLEEDGLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
35-481 |
8.01e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 35 MVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA-------------LPQDIESLTGGLAGSKGADPP 101
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkYKNDIENKKQILSNIDAEINK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 102 EFAALTK--ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKS 179
Cdd:PRK01156 324 YHAIIKKlsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKI 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 180 LFEHHKALdEKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNG 259
Cdd:PRK01156 400 QEIDPDAI-KKELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHY 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMA 331
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIK 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 332 QK------EDMEER---------------ITTLEKRYLSAQRESTSIHDMNDKLENELANKEA----ILRQMEEKNRQLQ 386
Cdd:PRK01156 553 NRykslklEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLN 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 387 ERLELAEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 463
Cdd:PRK01156 633 NKYNEIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
490
....*....|....*...
gi 1370463116 464 RLSDTVdrllTESNERLQ 481
Cdd:PRK01156 713 ELSDRI----NDINETLE 726
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-556 |
9.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 SQIVELQELLEKQNYEMAQMKERLAALSSRvGEVEQEAETARKDLIKTEEmntkYQRDIREAMAQKED----------ME 337
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERldassddlaaLE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 338 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQri 417
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE-- 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 418 aaltkaeerhgNIEERMRHLEGQLEEKNQELQRARQrekmneEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAAL 491
Cdd:COG4913 770 -----------NLEERIDALRARLNRAEEELERAMR------AFNREWPAETADLDAdlESLPEYLALLDrleeDGLPEY 832
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 492 EEK--NVLIQESETFRKNLEESLHDKERLAEE-IEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 556
Cdd:COG4913 833 EERfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
284-456 |
9.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 284 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND- 362
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 363 --------KLENELANKEAILRQMEEKN---RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRiaALTKAEERHGNIE 431
Cdd:COG4717 128 lplyqeleALEAELAELPERLEELEERLeelRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*
gi 1370463116 432 ERMRHLEGQLEEKNQELQRARQREK 456
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELE 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
378-533 |
9.86e-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: 48.00 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 378 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARq 453
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 454 rEKMNEEHNKRLSDTVDR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL-HDKERLAEEIEKLRSEL 529
Cdd:COG1579 80 -EQLGNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAEL 158
|
....
gi 1370463116 530 DQLK 533
Cdd:COG1579 159 EELE 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
309-532 |
1.09e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 309 RKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ 384
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 385 LQERLELAEQK------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQRE 455
Cdd:TIGR00618 245 LTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 456 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQ 531
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDI 404
|
.
gi 1370463116 532 L 532
Cdd:TIGR00618 405 L 405
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
30-451 |
1.63e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN---------SALPQDIESLTGG- 91
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrnmevqrlEALLKAMKSECQGq 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 92 ----LAGSKGADPP--EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPS 165
Cdd:pfam15921 446 merqMAAIQGKNESleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRS 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 166 GVSSEVEVLKALKSLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGM 245
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 246 EPGQKVHEKR--LSNGSIDSTDETSQIVELQELLEKQNYEMAQM----KERLAALSSRVGEVEQ---EAETARKDLIKTE 316
Cdd:pfam15921 594 QLEKEINDRRleLQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 317 EMNTKYQRDIREamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERL 389
Cdd:pfam15921 674 EDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKI 750
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463116 390 ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA 812
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
102-533 |
2.00e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 102 EFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSE 170
Cdd:pfam12128 280 ERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 171 VEVLKalkslfEHHKALDEKVRERLRVSLERVSALEEELAAanqeIVALREQNVHIQRKMASSEGSTESEHLEGME-PGQ 249
Cdd:pfam12128 356 LENLE------ERLKALTGKHQDVTAKYNRRRSKIKEQNNR----DIAGIKDKLAKIREARDRQLAVAEDDLQALEsELR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 250 KVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREA 329
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSELRQA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 330 MAQKEDMEERITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKA 403
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGGE 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 404 ETL-------------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 464
Cdd:pfam12128 578 LNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 465 LSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam12128 658 LFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK 735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-532 |
2.53e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYDR------------------DSLQRQLNS--ALPQDIESLTGGLAGSKG 97
Cdd:pfam15921 122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHELeaakclkedmledsntqiEQLRKMMLSheGVLQEIRSILVDFEEASG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 98 ADPPE-------------------FAALTKELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRHErsLR 153
Cdd:pfam15921 202 KKIYEhdsmstmhfrslgsaiskiLRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHE--VE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 154 MTVVKRQAQS----PSGVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIV 217
Cdd:pfam15921 280 ITGLTEKASSarsqANSIQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 218 ALReqnvhIQRKMASSEGSTESEHLEGMEPGQKVHEKRLS-----NGSIDSTDETSQIV--ELQELLEKQNYEMAQMKER 290
Cdd:pfam15921 360 EAR-----TERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEVQRLEAL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 291 LAALSSRV-GEVEQEAETARKdliKTEEMNtKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEnela 369
Cdd:pfam15921 435 LKAMKSECqGQMERQMAAIQG---KNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 370 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE---LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 446
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 447 ELQRAR-QREKmnEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:pfam15921 587 AMQVEKaQLEK--EINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
....*...
gi 1370463116 525 LRSELDQL 532
Cdd:pfam15921 665 SRNELNSL 672
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
169-533 |
3.09e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 169 SEVEVLKALKSLFEHHKALDEKVRERL--RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGME 246
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 247 PGQKV-----HEKRLSNGSIDSTDETSQIVELQELlEKQNYEMAQMKERlaalssrvgeVEQEAETARKDLIKTEEMntk 321
Cdd:pfam17380 346 RERELerirqEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVKILEEER--- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 322 yQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMr 401
Cdd:pfam17380 412 -QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 402 kaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERL 480
Cdd:pfam17380 463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLL 518
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370463116 481 QLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLE 569
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
115-503 |
3.16e-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: 48.12 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 115 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 189
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 190 KVrERLRVSLERVSAL------EEELAAANQEIVA----LREQNVHIQRKMASSEGSTESEHLEG--MEPGQKVHEKRLS 257
Cdd:TIGR00606 759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 258 NGSIdstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:TIGR00606 838 LDTV-----VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 338 ERITTLEKRYLSAQRESTSIHDMNDKLENElankeaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 417
Cdd:TIGR00606 913 PLETFLEKDQQEKEELISSKETSNKKAQDK-------VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 418 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 494
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
|
....*....
gi 1370463116 495 NVLIQESET 503
Cdd:TIGR00606 1063 IDLIKRNHV 1071
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-422 |
4.57e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 38 MLDERDRLLDTLRETQESLSLAQQRLQDviydrdsLQRQLnSALPQDIESLTGglagskgadppEFAALTKELNACREQL 117
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSD-------ASRKI-GEIEKEIEQLEQ-----------EEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 118 LEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEHHKAldEKVRERLRV 197
Cdd:TIGR02169 747 SSLEQEIENVKSE-------LKELEARIEELEEDL---------------HKLEEALNDLEARLSHSRI--PEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 198 SLERVSALEEELAAANQEIvalreQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIdstdetsQIVELQELL 277
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 278 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQRES 354
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 355 TSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 422
Cdd:TIGR02169 948 EEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-541 |
5.33e-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: 47.27 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 193 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 272
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 273 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 352
Cdd:TIGR00618 279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 353 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 426
Cdd:TIGR00618 353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 427 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 487
Cdd:TIGR00618 430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1370463116 488 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
325-502 |
5.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 325 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 403
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 404 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 472
Cdd:COG3883 97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|
gi 1370463116 473 LTESNERLQLHLKERMAALEEKNVLIQESE 502
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-524 |
5.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 240 EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMN 319
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 320 TKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQT 399
Cdd:PTZ00121 1111 AEEARKAEEAKKKAEDA---------RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEA 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 400 MRKAETLPEVE----AELAQRIAALTKAEERHgNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTE 475
Cdd:PTZ00121 1181 ARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370463116 476 SNERLQLHLKERMAAL--EEKnvliQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIkaEEA----RKADELKKAEEKKKADEAKKAEEKKK 1303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-383 |
7.10e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGG------LAGSKGADPPEFAALTKELNACR 114
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRER 194
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 195 LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKV--HEKRLSNGSIDSTDETSQIVE 272
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330 340 350
....*....|....*....|....*....|.
gi 1370463116 353 EstsihdmndkleneLANKEAILRQMEEKNR 383
Cdd:TIGR02169 491 E--------------LAEAEAQARASEERVR 507
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
355-465 |
7.72e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 355 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 429
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 1370463116 430 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 465
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-571 |
8.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 192 RERLRVSLERVSALEEELAAANQEIVALR-EQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE------KRLSNGSIDST 264
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIDVASAEREIAeleaelERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 265 DETSQIVELQEllekqnyEMAQMKERLAALSSRVGEVEQEAETArkdlikteemntkyQRDIREAMAQKEDMEERITTLE 344
Cdd:COG4913 689 ALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 345 KRYLSAQRESTSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKA 423
Cdd:COG4913 748 RALLEERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEY 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 424 EERHGNIEERmrhlegQLEEKNQELQRARQR----------EKMNEEHN--KRLSDTVDRLLTESN----ERLQLHLKER 487
Cdd:COG4913 818 LALLDRLEED------GLPEYEERFKELLNEnsiefvadllSKLRRAIReiKERIDPLNDSLKRIPfgpgRYLRLEARPR 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 488 M-AALEEKNVLIQE--SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIepTIPRTHLDTSAELRYSV-GSLV 563
Cdd:COG4913 892 PdPEVREFRQELRAvtSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARV--LDVRNHLEFDAEEIDREdGEEV 969
|
....*...
gi 1370463116 564 DSQSDYRT 571
Cdd:COG4913 970 ETYSSSGG 977
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
253-524 |
1.12e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 253 EKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQ 332
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 333 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMR-------KAET 405
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKelkskekELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 406 LPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL 484
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQ 577
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1370463116 485 KERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
333-532 |
1.17e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 333 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 411
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 412 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 489
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370463116 490 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 532
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-540 |
1.22e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 185
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 186 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMA--SSEGSTESEHLEGMEPGQKVHEKRLSNgsIDS 263
Cdd:TIGR04523 233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISD--LNN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerittl 343
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK------ 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 344 ekrylsaqRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 423
Cdd:TIGR04523 377 --------KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 424 ----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLK 485
Cdd:TIGR04523 449 dsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LK 523
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463116 486 ERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 540
Cdd:TIGR04523 524 EKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
39-222 |
1.38e-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: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 39 LDERDRLLDTLRETQESLSLAQQRLQDVIyDRDSLQRQLnSALPQDIESLTgglagskgADPPEFAALTKELNACREQLL 118
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEI-DVASAEREI-AELEAELERLD--------ASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 119 EKEEEISELKAERNNTRlllehleclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEhhKALDEKVRERLRVS 198
Cdd:COG4913 703 ELEEELDELKGEIGRLE----------KELEQAEEELDELQDRLEAAEDLARLELRALLEERFA--AALGDAVERELREN 770
|
170 180
....*....|....*....|....*
gi 1370463116 199 LE-RVSALEEELAAANQEIVALREQ 222
Cdd:COG4913 771 LEeRIDALRARLNRAEEELERAMRA 795
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
205-538 |
1.44e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 205 LEEELAAANQEIVALREQNvhiqrkmaSSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEM 284
Cdd:pfam10174 441 LEEALSEKERIIERLKEQR--------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSG 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 285 AQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKL 364
Cdd:pfam10174 513 LKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESG-------KA 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 365 ENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTkaEERHGNIEERMR-HLEG 439
Cdd:pfam10174 578 QAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQL 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 440 QLEEKNQELQRARQREkmnEEHNKRLSDTvDRLLTESNERLQLHLKERMAALEEKNVL--------IQESETFRKNLEES 511
Cdd:pfam10174 656 QLEELMGALEKTRQEL---DATKARLSST-QQSLAEKDGHLTNLRAERRKQLEEILEMkqeallaaISEKDANIALLELS 731
|
330 340 350
....*....|....*....|....*....|.
gi 1370463116 512 LHDKERLAEEIEKLRSELD----QLKMRTGS 538
Cdd:pfam10174 732 SSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
326-493 |
1.71e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 326 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqqtmRKAET 405
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--------RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 406 LPEVEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 485
Cdd:COG1579 91 YEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1370463116 486 ERMAALEE 493
Cdd:COG1579 164 EREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
365-533 |
2.53e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 365 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 444
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 445 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesetfRKNLEESLHDKER 517
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
|
170
....*....|....*.
gi 1370463116 518 LAEEIEKLRSELDQLK 533
Cdd:COG3883 162 LKAELEAAKAELEAQQ 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
268-558 |
2.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 268 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 347
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 348 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 427
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 428 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 507
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370463116 508 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYS 558
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
383-580 |
2.90e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 383 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 462
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 463 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 535
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370463116 536 TGSLIEPTIPRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 580
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
220-529 |
3.41e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 220 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 297
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 298 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 377
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 378 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 447
Cdd:pfam01576 241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 448 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 498
Cdd:pfam01576 321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398
|
330 340 350
....*....|....*....|....*....|...
gi 1370463116 499 --QESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:pfam01576 399 akQDSEHKRKKLEGQLQELQARLSESERQRAEL 431
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
272-454 |
3.61e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 272 ELQELLEKQNyEMAQMKERL-------AALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 342
Cdd:COG0497 173 ELEELRADEA-ERARELDLLrfqleelEAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 343 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 412
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370463116 413 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 454
Cdd:COG0497 329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
418-541 |
3.71e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 418 AALTKAEERHGNIEErmrhlegqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvL 497
Cdd:COG2433 380 EALEELIEKELPEEE---------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---L 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370463116 498 IQESETFRKNLEESLH-DKE--RLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG2433 447 ERELSEARSEERREIRkDREisRLDREIERLERELEEERERIEELKR 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-407 |
4.85e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 174 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHE 253
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 254 KRLSNgSIDSTDETSQIVELQELLEKQNyeMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 333
Cdd:COG4942 104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463116 334 EDMEERITTLEKryLSAQRESTSihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 407
Cdd:COG4942 181 AELEEERAALEA--LKAERQKLL-----ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
260-415 |
5.36e-04 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 43.50 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDL-----IKTEEMNTKYQR---------- 324
Cdd:TIGR03007 196 PDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnseldGRIEALEKQLDAlrlrytdkhp 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 325 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAE 404
Cdd:TIGR03007 276 DVIATKREIAQLEEQKEEEGSAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLR 348
|
170
....*....|.
gi 1370463116 405 TLPEVEAELAQ 415
Cdd:TIGR03007 349 TIPEVEAELTQ 359
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
189-448 |
5.45e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 189 EKVRERLRVSLERVS-ALEEELAAANQEIVALREQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKRLSNGSIDSTD 265
Cdd:pfam10174 449 ERIIERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGLKKDSKLKSLEIAVEQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 266 ETSQIVELQELLEK-QNYEMAQMKErlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 344
Cdd:pfam10174 529 KKEECSKLENQLKKaHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 345 KRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA- 423
Cdd:pfam10174 607 SLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSl 685
|
250 260
....*....|....*....|....*....
gi 1370463116 424 EERHGNIE----ERMRHLEGQLEEKNQEL 448
Cdd:pfam10174 686 AEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
285-533 |
6.59e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 285 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 364
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 365 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 444
Cdd:pfam05557 64 ---EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQST 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 445 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 524
Cdd:pfam05557 131 NSELEELQER---LDLLKAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201
|
....*....
gi 1370463116 525 LRSELDQLK 533
Cdd:pfam05557 202 LEKELERLR 210
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
186-529 |
6.77e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 186 ALDEKVRERLRV-------SLERVSALEEELAAANqeiVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLS 257
Cdd:pfam12128 597 ASEEELRERLDKaeealqsAREKQAAAEEQLVQAN---GELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 258 NGSIDSTDETSQIVELQE--LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQ 332
Cdd:pfam12128 674 AERKDSANERLNSLEAQLkqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 333 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEA 411
Cdd:pfam12128 753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQ 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 412 ELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAA 490
Cdd:pfam12128 829 QLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQ 894
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1370463116 491 LEE-KNVLIQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 529
Cdd:pfam12128 895 LEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
244-533 |
7.72e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 244 GMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 323
Cdd:COG4372 1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 324 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 403
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 404 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 483
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1370463116 484 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
265-529 |
8.56e-04 |
|
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: 43.04 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 340
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 341 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 419
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 420 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 492
Cdd:pfam02463 319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370463116 493 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
326-533 |
9.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 326 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQERLELAEQklQQTMRKAET 405
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAARERLAE--LEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 406 LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQLH 483
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLERE 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 484 LKERMAALEEKNVLIQ--------ESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG4913 354 LEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
264-532 |
1.05e-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: 42.70 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 332
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 333 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPEVEA 411
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN----LKKKIQKNKSLEsQISELKKQNNQLK----DNIEKKQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 412 ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL 491
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSEL 316
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370463116 492 EEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 532
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
158-533 |
1.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 158 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKVRERLRVSlERVSALEEELAAANQEIVALREQnvhIQRKMASSEGS 236
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKL---LQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 237 TESEHLEGMEPGQKVHEKRLSngsidstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVG-EVEQEAETARKDLIKT 315
Cdd:COG4717 136 ALEAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 316 EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREST---------------SIHDMNDKLENELANKEAIL----- 375
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 376 ----------RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKN 445
Cdd:COG4717 285 llallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 446 QELQRARQREKMNE-------------EHNKRLSDTVDRLlTESNERLQLHLKERMAALE--EKNVLIQESETFRKNLEE 510
Cdd:COG4717 365 LEELEQEIAALLAEagvedeeelraalEQAEEYQELKEEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|...
gi 1370463116 511 SLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG4717 444 LEEELEELREELAELEAELEQLE 466
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
189-457 |
1.30e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 189 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvheKRLSNGSIDSTDETS 268
Cdd:pfam19220 107 EELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAE-------------------KALQRAEGELATARE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTE----EMNTKYQRDIREAMAQKEDMEERITTLE 344
Cdd:pfam19220 168 RLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ-------LQERLELAEQKLQQTMRKAETLPEVEAELAQRI 417
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQEMQRARAELEERA 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 418 -----------AALTKAEERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 457
Cdd:pfam19220 328 emltkalaakdAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-426 |
1.59e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 189 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGsidstdeTS 268
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----RRIRALEQELAALEAELAEL-------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNYEMAQMKeRLAALSSRVGEVEQ--EAETArKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:COG4942 91 EIAELRAELEAQKEELAELL-RALYRLGRQPPLALllSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 347 yLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 426
Cdd:COG4942 169 -LEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
179-465 |
1.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 179 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKV 251
Cdd:PRK04863 797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 252 HEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 331
Cdd:PRK04863 877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 332 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 403
Cdd:PRK04863 950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463116 404 ETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 465
Cdd:PRK04863 1030 DAKRQMLQELKQELQDLGvpadsgaeeRARARRDELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
105-534 |
1.84e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 105 ALTKELNACREQLLEKEEEISELKAERNNTRlllEHLECLVSR--HERSLRMTVVKRQAQSPSGVSSevevlkaLKSLFE 182
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARleEETAQKNNALKKIRELEAQISE-------LQEDLE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 183 HHKALDEKVRERLRVSLERVSALEEEL------AAANQEIVALREQNVHIQRKMASSEGstesehlegmepgqKVHEKRL 256
Cdd:pfam01576 282 SERAARNKAEKQRRDLGEELEALKTELedtldtTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 257 SNGSIDstdETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrdireamaQKEDM 336
Cdd:pfam01576 348 QEMRQK---HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEH--------------KRKKL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 337 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 416
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 417 IAALtkaeerhgniEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KN 495
Cdd:pfam01576 491 LRQL----------EDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALEEgKK 548
|
410 420 430
....*....|....*....|....*....|....*....
gi 1370463116 496 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
486-544 |
1.86e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 41.74 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 486 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 544
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
198-402 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 198 SLERVSALEEELAAANQEIVALREQNVHIQRKmassegstesehlegmepgQKVHEKRLSNgsIDSTDEtsqivELQELL 277
Cdd:pfam15619 9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 278 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREsts 356
Cdd:pfam15619 63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK--- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370463116 357 IHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 402
Cdd:pfam15619 140 IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
36-494 |
2.58e-03 |
|
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: 41.63 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 36 VNMLDERDRLLD-TLRETQESLSLAQQRLQDViydRDSLQRQLNS--ALPQDIESLTGGLAgskgadppefaALTKELNA 112
Cdd:pfam05483 270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTIC-----------QLTEEKEA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 113 CREQLLEKEEE----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEH 183
Cdd:pfam05483 336 QMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 184 HKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVH---------------IQRKMASSEGSTESEHLEGM 245
Cdd:pfam05483 411 KKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleiqltaiktseehYLKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 246 EPGQKVHEKRLSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI---------- 313
Cdd:pfam05483 489 ELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkckl 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 314 -KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELANK 371
Cdd:pfam05483 569 dKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 372 EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRHLe 438
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSEL- 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463116 439 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMAALEEK 494
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTAILKDK 786
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
280-510 |
2.58e-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: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 280 QNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 357
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 358 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 437
Cdd:COG3206 235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463116 438 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 510
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
372-537 |
2.64e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 372 EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 452 RQREKMNEEHNKRLSdtvdRLLTESNERLQlHLKERMAALEEknVLIQESETFRKNlEESLHDKERLAEEIEKLR----- 526
Cdd:COG3096 598 AARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQ--LLEREREATVER-DELAARKQALESQIERLSqpgga 669
|
170
....*....|...
gi 1370463116 527 --SELDQLKMRTG 537
Cdd:COG3096 670 edPRLLALAERLG 682
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-541 |
2.73e-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: 41.54 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 338
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 411
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 412 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 476
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463116 477 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
83-240 |
2.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 83 QDIESLTGGLAGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQ 162
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 163 SpsgVSSEVEVLKALKSLFEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESE 240
Cdd:COG1579 93 A---LQKEIESLKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-373 |
3.19e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 104 AALTKELNACREQLLEKEEEISELKAERNNTRlllehleclvsrherslrmtvvkrqaqspsgvSSEVEVLKALKSLfeh 183
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALK--------------------------------KEEKALLKQLAAL--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 184 hkaldekvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNGSIDS 263
Cdd:COG4942 61 --------ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-----AQKEELAELLRALYRLGRQPPLALLLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDM----EER 339
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKE 207
|
250 260 270
....*....|....*....|....*....|....
gi 1370463116 340 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 373
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
318-533 |
3.98e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 318 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 397
Cdd:COG0497 138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 398 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 472
Cdd:COG0497 205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 473 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 531
Cdd:COG0497 273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352
|
..
gi 1370463116 532 LK 533
Cdd:COG0497 353 AE 354
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-535 |
4.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 173 VLKALKSLFEhhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSteSEHLEGMEPGQKVH 252
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL--EEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 253 EKRLsngsidstDETSQIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAET---ARKDLIKTEEMNTKYQRDIREA 329
Cdd:COG4717 115 REEL--------EKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 330 MAQK-EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK-----------LQ 397
Cdd:COG4717 183 LEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 398 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESN 477
Cdd:COG4717 263 GLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463116 478 ERLQLHLKERMAALE--EKNVLIQESETFRKNL--------EESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG4717 343 LDRIEELQELLREAEelEEELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
189-431 |
4.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 189 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdetS 268
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 269 QIVELQELLEKQNyemAQMKERLAAL---SSRVGEVEQ--EAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERI 340
Cdd:COG3883 73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESFSDFLDRLSALSKIADADadlLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 341 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 420
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
250
....*....|.
gi 1370463116 421 TKAEERHGNIE 431
Cdd:COG3883 230 AAAAAAAAAAA 240
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
262-534 |
5.16e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 262 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQrdIREAMAQKEDMEERI 340
Cdd:pfam10174 158 ESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ--LQPDPAKTKALQTVI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 341 TTLEKRYLSAQRestSIHDMNDKLENELAN-------KEAILRQME----------EKNRQLQERLELAEQKLQQTMRKA 403
Cdd:pfam10174 236 EMKDTKISSLER---NIRDLEDEVQMLKTNgllhtedREEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 404 ETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEE---------HNKRLSDTV 469
Cdd:pfam10174 313 ETLTNQNSDCKQHIevlkESLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirDLKDMLDVK 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463116 470 DR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKN-------LEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:pfam10174 393 ERkinVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDRERL 467
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
273-535 |
5.57e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 353 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 431
Cdd:pfam07888 109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 432 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNER---LQLHLKERMAALEEKNVLIQESETFR 505
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKeaeNEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270
....*....|....*....|....*....|
gi 1370463116 506 KNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
375-488 |
5.92e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 375 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 453
Cdd:COG0542 413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463116 454 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 488
Cdd:COG0542 493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
309-532 |
5.99e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 309 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 388
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 389 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 460
Cdd:COG5022 877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463116 461 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:COG5022 956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
177-448 |
8.26e-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: 39.82 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 177 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEPGQKVHEKrl 256
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 257 sngsidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETaRKDLIKtEEMNTKYQRDIREAMAQKEDM 336
Cdd:pfam12128 337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIK-EQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 337 EERITTLEKRYlsAQRESTSIHDMN-DKLENELANKEAILRQMEEKNR---------------QLQERLELAEQKLQQTM 400
Cdd:pfam12128 407 DRQLAVAEDDL--QALESELREQLEaGKLEFNEEEYRLKSRLGELKLRlnqatatpelllqleNFDERIERAREEQEAAN 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370463116 401 RKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 448
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
259-442 |
8.58e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.28 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 259 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 329
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 330 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 407
Cdd:cd22656 152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
170 180 190
....*....|....*....|....*....|....*
gi 1370463116 408 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 442
Cdd:cd22656 229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
272-500 |
8.80e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 38.93 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 272 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 351
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 352 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 428
Cdd:pfam06008 105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 429 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 498
Cdd:pfam06008 174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252
|
..
gi 1370463116 499 QE 500
Cdd:pfam06008 253 QE 254
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
190-533 |
9.11e-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: 39.45 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 190 KVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrkmasSEGSTESEHLEGM--EPGQKVHEKRLSNG-SIDSTDE 266
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE---------EKNREEVEELKDKyrELRKTLLANRFSYGpAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 267 T-----SQIVELQELLEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 336
Cdd:pfam06160 154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 337 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 416
Cdd:pfam06160 224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 417 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQLHLKERMAA---- 490
Cdd:pfam06160 288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLeeLEKRYDEIVERLEEKEVAysel 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1370463116 491 LEEKNVLIQESETFRKNLEE------SLHDKERLA-EEIEKLRSELDQLK 533
Cdd:pfam06160 363 QEELEEILEQLEEIEEEQEEfkeslqSLRKDELEArEKLDEFKLELREIK 412
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
277-468 |
9.16e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153350 Cd Length: 243 Bit Score: 38.73 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 277 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 352
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 353 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 417
Cdd:cd07666 93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370463116 418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 468
Cdd:cd07666 170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
40-222 |
9.25e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 40 DERDRLLDTLRETQ----ESLS--LAQQRLQDVIYDRDSLQRQLNSaLPQDIESLTGGLAGSKGADPPEFAALTK----E 109
Cdd:PRK05771 16 SYKDEVLEALHELGvvhiEDLKeeLSNERLRKLRSLLTKLSEALDK-LRSYLPKLNPLREEKKKVSVKSLEELIKdveeE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 110 LNACREQLLEKEEEISELKAERNNTRLLLEHLECLVS-----RHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKS 179
Cdd:PRK05771 95 LEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNfdldlSLLLGFKYVSvfvgtVPEDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463116 180 LFEH-------HKALDEKVRERLR-------------VSLERVSALEEELAAANQEIVALREQ 222
Cdd:PRK05771 175 DKGYvyvvvvvLKELSDEVEEELKklgferleleeegTPSELIREIKEELEEIEKERESLLEE 237
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
193-620 |
9.45e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 39.72 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 193 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEK--RLSNGSID----STDE 266
Cdd:COG5192 363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 346
Cdd:COG5192 440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 347 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 425
Cdd:COG5192 516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 426 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 502
Cdd:COG5192 591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 503 TFRKN-LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPT------------IPRTHLDTS-AELRYSVGSLVDSQSD 568
Cdd:COG5192 664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYragryvrivlshVPLEFVDEFnSRYPIVLGGLLPAEKE 743
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1370463116 569 YRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 620
Cdd:COG5192 744 MGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
63-532 |
9.57e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 63 LQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKGADPPEFAALtKELNACREQLLEKEEEISELKAERNNT----RLLL 138
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAL-KKIRELEAQISELQEDLESERAARNKAekqrRDLG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 139 EHLECLVSRHERSLRMTVVKRQAQSPSgvSSEVEVLKalKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIV- 217
Cdd:pfam01576 299 EELEALKTELEDTLDTTAAQQELRSKR--EQEVTELK--KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAn 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 218 ------ALREQNVHIQRKMAS-SEGSTESEHlegmepGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmaqmker 290
Cdd:pfam01576 375 lekakqALESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE------- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 291 LAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQrestsihdmnDKLENELAN 370
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ----------EQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 371 KEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEEKNQ 446
Cdd:pfam01576 512 KRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQELDDLLV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463116 447 ELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLR 526
Cdd:pfam01576 588 DLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663
|
....*.
gi 1370463116 527 SELDQL 532
Cdd:pfam01576 664 AEMEDL 669
|
|
| |
