|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-740 |
2.09e-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: 74.32 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 372 GSSPNNASELS----LASLTEKIQKMEENqhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAE 447
Cdd:TIGR02168 664 GSAKTNSSILErrreIEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 448 QLSQENEKLINLLQERvkneepSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKE 527
Cdd:TIGR02168 737 RLEAEVEQLEERIAQL------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 528 ENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLE------ADKQKAIEASST--VGQTAENFEVQEMLK 599
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESelEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 600 VARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLS-RTSLKLQ---EKASESDAEIKDM 675
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366637 676 KETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWR-RFQA 740
Cdd:TIGR02168 971 RRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
389-730 |
3.90e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 389 KIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlinlLQERVKNEE 468
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 469 PSAQGGKVLELEQKCTDI-------------LEKSRFEREKLL-----------------------NIQQQLTCSLRKVE 512
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIeeeiskitarigeLKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 513 EENQGAIDMIKHLKEENEKLNGFLEHER--CNNSVMAKTLEECRVTLEGLKMENGSLKA-LLEADKQKAIEASSTVGQTA 589
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLK 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 590 ENFEVQEMLKVARAE----KDQLQLSCTELRQELLKANGE-IKHVSSLLAKMEKDYSYLKEVCD--HQAEQLSRTSLKLQ 662
Cdd:PRK03918 546 KELEKLEELKKKLAElekkLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDaeKELEREEKELKKLE 625
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366637 663 EKASESDAEIKDMKETIFELEDQVEQHRavKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKE 730
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
377-734 |
3.90e-09 |
|
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: 60.03 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 377 NASELSLASLTEKIQKMEEnqhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSQENEK 455
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 456 LINLLQErvKNEEPSAQGGKVLELEQKCTDI-LEKSRFEREKLLNIQQQLTCSLRKVEEENQGA-------IDMIKHLKE 527
Cdd:TIGR04523 265 IKKQLSE--KQKELEQNNKKIKELEKQLNQLkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIqnqisqnNKIISQLNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 528 ENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTV-GQTAENFEVQEMLKVARAEKD 606
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 607 QLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTS------------------------LKLQ 662
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLN 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 663 EKASESDAEIKDMKETIFELEDQVEQHRA------------------------------VKLHNNQLISELEGSVIKLEE 712
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQKSLKK 582
|
410 420
....*....|....*....|..
gi 1720366637 713 QKSDLERQLKTLTKQIKEETEE 734
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKE 604
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
475-781 |
4.88e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 475 KVLELEQKCTDILEKSRFEREKLLNIQQQLTcSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECR 554
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 555 VTLEGLKMENGSLKALLEADKQkaieasstvgqtaenfEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLA 634
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIE----------------ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 635 KMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQK 714
Cdd:TIGR02168 828 SLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366637 715 SDLERQLKTLTKQIKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEEKNARLQKEL 781
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
377-785 |
5.40e-09 |
|
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: 59.65 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 377 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSF-----------HQHRER 445
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniqknidkikNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 446 AEQLS------QENEKL---INLLQERV---------KNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCS 507
Cdd:TIGR04523 200 ELLLSnlkkkiQKNKSLesqISELKKQNnqlkdniekKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 508 LRKVEE---------------ENQGAIDMIKHLKEE------------------NEKLNGF----------LEHERCNNS 544
Cdd:TIGR04523 280 NKKIKElekqlnqlkseisdlNNQKEQDWNKELKSElknqekkleeiqnqisqnNKIISQLneqisqlkkeLTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 545 VMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTV-GQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKAN 623
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 624 GEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTS------------------------LKLQEKASESDAEIKDMKETI 679
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLNEEKKELEEKVKDLTKKI 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 680 FELEDQVEQHRAVKLHNNQLISELEGsviKLEEQKSDLER-QLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQ 758
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLED---ELNKDDFELKKeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
490 500
....*....|....*....|....*..
gi 1720366637 759 ELRTVKRRLLEEEEKNARLQKELGDIQ 785
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
567-781 |
1.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 567 LKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEv 646
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 647 cdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTK 726
Cdd:COG1196 310 ---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366637 727 QIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKRRLLEEEEKNARLQKEL 781
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALL-ERLERLEEELEELEEALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-652 |
1.47e-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: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 383 LASLTEKIQKMEENQHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 455
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 456 ----LINLLQERVKNEEPSAQGGKVLELEQKCTDILEKsrfEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEK 531
Cdd:TIGR02168 321 leaqLEELESKLDELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 532 LNGFLEhercnnsVMAKTLEECRVTLEGLKMENGSL-KALLEADKQKAIEASSTVGQTAENFE-----VQEMLKVARAEK 605
Cdd:TIGR02168 398 LNNEIE-------RLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQeelerLEEALEELREEL 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720366637 606 DQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAE 652
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
487-786 |
3.25e-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: 57.37 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 487 LEKSRFEREKLLN-IQQQLTCSLR----KVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKT---LEECRVTLE 558
Cdd:TIGR02168 191 LEDILNELERQLKsLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 559 GLKMENGSLKALLEaDKQKAIEAsstvgQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEK 638
Cdd:TIGR02168 271 ELRLEVSELEEEIE-ELQKELYA-----LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 639 DYSYLKEVCDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKS 715
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366637 716 DLERQLKTLTKQ--------IKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQG 786
Cdd:TIGR02168 425 ELLKKLEEAELKelqaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-781 |
5.31e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 377 NASELSLASLTEKIQKMEENQH---STAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQEN 453
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 454 EKLINLLQERVKNEEPSAQGGKVLELEQkctDILEKSRFEREKLLniqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLn 533
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARR---EELEDRDEELRDRL---EECRVAAQAHNEEAESLREDADDLEERAEEL- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 534 gfleheRCNNSVMAKTLEECRVTLEGLKMENGSLKALLEadkqkaiEASSTVGQTAENFE-VQEMLKVARAEKDQLQLSC 612
Cdd:PRK02224 362 ------REEAAELESELEEAREAVEDRREEIEELEEEIE-------ELRERFGDAPVDLGnAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 613 TELRQELLKANGEIKHVSSLLAKmEKDYSYLKEVCDhqAEQLSRTSLKlQEKASESDAEIKDMKETIFELEDQVEqhRAV 692
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEA-GKCPECGQPVEG--SPHVETIEED-RERVEELEAELEDLEEEVEEVEERLE--RAE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 693 KLhnnqliSELEGSVIKLEEQKSDLERQLKTLTKQIKEETE---EWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLE 769
Cdd:PRK02224 503 DL------VEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410
....*....|..
gi 1720366637 770 EEEKNARLQKEL 781
Cdd:PRK02224 577 LNSKLAELKERI 588
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
376-780 |
7.25e-08 |
|
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: 56.27 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 376 NNASELSLasLTEKIQKmeenQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTiletsfhQHRERAEQLSQENEK 455
Cdd:pfam05483 374 KNEDQLKI--ITMELQK----KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK-------QFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 456 LINLLQERVKN-EEPSAQGGKVLELEQKCTDILE--KSRFEREKLLNIQQQLTCSLRKVEEEN--QGAIDMIKHLKEENE 530
Cdd:pfam05483 441 LIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEdlKTELEKEKLKNIELTAHCDKLLLENKEltQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 531 KLNGFLEHErcnnSVMAKTLEECRVTLEGLKMEngsLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQ-LQ 609
Cdd:pfam05483 521 DIINCKKQE----ERMLKQIENLEEKEMNLRDE---LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKiLE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 610 LSCTELR----------QELLKANGEIKHVSSLLAKMEKDYsylkEVCDHQAE-QLSRTSLKLQEKASESDAEIKDMKET 678
Cdd:pfam05483 594 NKCNNLKkqienknkniEELHQENKALKKKGSAENKQLNAY----EIKVNKLElELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 679 IFELEDQVEQHRAVKLHNNQLISELEGSVI-KLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCE-- 755
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIEls 749
|
410 420
....*....|....*....|....*.
gi 1720366637 756 -AQQELRTVKRRLLEEEEKNARLQKE 780
Cdd:pfam05483 750 nIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
379-789 |
1.39e-07 |
|
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: 55.18 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 379 SELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 456
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 457 -INLLQERVKNEEPSAQGgkvLELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGaiDMIKHLKEENEKLNGf 535
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQK---LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS--EFTSNLAEEEEKAKS- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 536 LEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEAdkqkaiEASSTVGQTAENFEVQEMLKVARAEK-DQLQLSCTE 614
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEG------ESTDLQEQIAELQAQIAELRAQLAKKeEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 615 LRQELLKANGEIKHVSSL---LAKMEKDYSyLKEVCDHQAEQLSRtslKLQEKASESDAEIKDMKETIF---ELEDQVEQ 688
Cdd:pfam01576 252 LEEETAQKNNALKKIRELeaqISELQEDLE-SERAARNKAEKQRR---DLGEELEALKTELEDTLDTTAaqqELRSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 689 HRAvklhnnQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLL 768
Cdd:pfam01576 328 EVT------ELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420
....*....|....*....|.
gi 1720366637 769 EEEEKNARLQKELGDIQGHSS 789
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLS 422
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
387-782 |
1.54e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 387 TEKIQKMEENQHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---INLLQER 463
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 464 VKN------------EEPSAQGGKVLELEQKCTDILEKSRFeREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEK 531
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 532 LNGFLEHErcnnsvmaKTLEECRVTLEGLKMENGSLKALL-EADKQKAIEASSTVGqtaenfEVQEMLKVARAEKdqlql 610
Cdd:PRK03918 340 LEELKKKL--------KELEKRLEELEERHELYEEAKAKKeELERLKKRLTGLTPE------KLEKELEELEKAK----- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 611 scTELRQELLKANGEIKHVSSLLAKMEKDYSYLKE------VCDHQAEQLSRTSLKlqekaSESDAEIKDMKETIFELED 684
Cdd:PRK03918 401 --EEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 685 QVEQHRAVKLHNNQLISElEGSVIKLE---EQKSDLERQLKTLT-KQIKEETEEWRRFQADLQT----AVVVANDIK--C 754
Cdd:PRK03918 474 KERKLRKELRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklE 552
|
410 420
....*....|....*....|....*...
gi 1720366637 755 EAQQELRTVKRRLLEEEEKNARLQKELG 782
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELE 580
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
377-781 |
2.98e-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: 54.20 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 377 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQE----LTAENEKLvDEKTILETSFHQHRERAEQLSQE 452
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQshayLTQKREAQ-EEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 453 nEKLINLLQERV----KNEEPSAQGGKVLELEQKCTDI---LEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIK-- 523
Cdd:TIGR00618 276 -EAVLEETQERInrarKAAPLAAHIKAVTQIEQQAQRIhteLQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqe 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 524 -HLKEENEKLNGFLEHeRCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQkaiEASSTVGQTAENFEVQEMLKVAR 602
Cdd:TIGR00618 355 iHIRDAHEVATSIREI-SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR---EQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 603 AEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFEL 682
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ----QLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 683 EDQvEQHRAVKLH-------NNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCE 755
Cdd:TIGR00618 507 CGS-CIHPNPARQdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
410 420
....*....|....*....|....*.
gi 1720366637 756 AQQeLRTVKRRLLEEEEKNARLQKEL 781
Cdd:TIGR00618 586 IPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
402-752 |
3.61e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 402 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLINLLQERVKNEEpsaqggKVLELEQ 481
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQ------EIKNLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 482 KCTDIleKSRFEREKLLNiqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVT----- 556
Cdd:TIGR04523 392 QINDL--ESKIQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTresle 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 557 --LEGLKMENGSLKALLEADKQKAIEASSTVGQ-TAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLL 633
Cdd:TIGR04523 468 tqLKVLSRSINKIKQNLEQKQKELKSKEKELKKlNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 634 AKM--EKDYSYLKEVCDHQAEQLSR-----TSLK-----LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLIS 701
Cdd:TIGR04523 548 NKDdfELKKENLEKEIDEKNKEIEElkqtqKSLKkkqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720366637 702 ELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 752
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-785 |
3.64e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 369 SPTGSSPNNASEL-SLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAE 447
Cdd:TIGR02169 661 APRGGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 448 Q----LSQENEKLINLLQERVKNE-EPSAQGGKVLELEQKCTDIleKSRFEREKLLNIQQQltcsLRKVEEENQgaiDMI 522
Cdd:TIGR02169 741 EleedLSSLEQEIENVKSELKELEaRIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAE----LSKLEEEVS---RIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 523 KHLKEENEKLNgflehercnnsvmaktleecRVTLEglkmengslKALLEADKQKAIEasstvgqtaENFEVQEMLKVAR 602
Cdd:TIGR02169 812 ARLREIEQKLN--------------------RLTLE---------KEYLEKEIQELQE---------QRIDLKEQIKSIE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 603 AEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSylkevcdhqaeqlsrtslKLQEKASESDAEIKDMKETIFEL 682
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD------------------ELEAQLRELERKIEELEAQIEKK 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 683 EDQVEQHRAVKLHNNQLISELEGSVIKLEEQkSDLERQLKTLTKQIKEETEEWRRFQadlqtavvvanDIKCEAQQELRT 762
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQEYEE 983
|
410 420
....*....|....*....|...
gi 1720366637 763 VKRRLLEEEEKNARLQKELGDIQ 785
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAIL 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
590-791 |
3.91e-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: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 590 ENF----EVQEMLKVARAEKDQLQLSCtELRQELLKANGEIKHVSSLLAKM-----EKDYSYLKEVCDHQAEQLSRtslk 660
Cdd:COG4913 232 EHFddleRAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR---- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 661 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQ 739
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720366637 740 ADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGHSSSM 791
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-641 |
5.37e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 377 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL 456
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 457 INLLQERVKNEEpsAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLtcsLRKVEEENQGAIDMIKHLKEENEKLNGFL 536
Cdd:COG1196 329 EEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 537 EHERcNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENfevQEMLKVARAEKDQLQLSCTELR 616
Cdd:COG1196 404 ELEE-AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE---EEALLELLAELLEEAALLEAAL 479
|
250 260
....*....|....*....|....*
gi 1720366637 617 QELLKANGEIKHVSSLLAKMEKDYS 641
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
485-772 |
5.91e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 485 DILEKS-------RFEREKLLNiQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTL 557
Cdd:TIGR02169 647 ELFEKSgamtggsRAPRGGILF-SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 558 EGLKMENGSLKALLE--ADKQKAIEASSTvgqtaenfEVQEMLKVARAEKDQLQLSCTELRQELLK-----ANGEIKHVS 630
Cdd:TIGR02169 726 EQLEQEEEKLKERLEelEEDLSSLEQEIE--------NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 631 SLLAKMEKDYSYLKEVCDHQAEQLSRTSLK---LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSV 707
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366637 708 IKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKC---EAQQELRTVKRRLLEEEE 772
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAkleALEEELSEIEDPKGEDEE 945
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
377-770 |
6.56e-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: 53.20 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 377 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAEneklvdektiletsfHQHRERAEQLSQENekl 456
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS---------------LQEKERAIEATNAE--- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 457 INLLQERVKneepsaqggkvLELEQkctdiLEKSRFEREKLLNIQQQLTcSLRKVEEENQGAIDMIKHLKEENEKLNGfl 536
Cdd:pfam15921 519 ITKLRSRVD-----------LKLQE-----LQHLKNEGDHLRNVQTECE-ALKLQMAEKDKVIEILRQQIENMTQLVG-- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 537 EHERCNNSVMAKTlEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVgqtaENFEVqEMLKVARAEKDQLQlSCTELR 616
Cdd:pfam15921 580 QHGRTAGAMQVEK-AQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLEL-EKVKLVNAGSERLR-AVKDIK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 617 QELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 696
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366637 697 NQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEE 770
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-785 |
1.52e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 383 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTA--ENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLL 460
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 461 QERVKNEEpsaqggKVLELEQKCTDILEKSRFEREKLLniqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGflEHER 540
Cdd:COG4717 163 EELEELEA------ELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 541 CNNSVMAKTLEECRVTLEGLKMENGSLkALLEADKQKAIEASSTVGQTAenFEVQEMLKVARAEKDQLQLSCTELRQELL 620
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVL--FLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 621 KANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKEtifeleDQVEQHRAVKLHNNQLI 700
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL------EELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 701 SELE-GSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAvvvandikcEAQQELRTVKRRLLEEEEKNARLQK 779
Cdd:COG4717 383 DEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELRE 453
|
....*.
gi 1720366637 780 ELGDIQ 785
Cdd:COG4717 454 ELAELE 459
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
380-780 |
2.52e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 380 ELSLASLTEKIQKMEENQHSTA----EELQATLQE---LSDQQQmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQE 452
Cdd:PRK10246 175 ELTGTEIYGQISAMVFEQHKSArtelEKLQAQASGvalLTPEQV--QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 453 NEklinLLQERVKNEEPSAQGGKVLELEQKCTDILE---KSRFEREKLLNIQQQ---LTCSLRKVEEEN----------- 515
Cdd:PRK10246 253 DE----LQQEASRRQQALQQALAAEEKAQPQLAALSlaqPARQLRPHWERIQEQsaaLAHTRQQIEEVNtrlqstmalra 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 516 ---QGAIDMIKHLKEENEKLNGFL-EHERCNnsVMAKTLEECRVTLEGLKMENGSLKAL---LEADKQK-AIEASSTVGQ 587
Cdd:PRK10246 329 rirHHAAKQSAELQAQQQSLNTWLaEHDRFR--QWNNELAGWRAQFSQQTSDREQLRQWqqqLTHAEQKlNALPAITLTL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 588 TAENfevqemLKVARAEKDQLQlsctELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKAS- 666
Cdd:PRK10246 407 TADE------VAAALAQHAEQR----PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQq 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 667 --------ESDAEIKDMKETIFELED-------------QVEQHRAVKLHNNQL-ISELEGSVIKLEEQKSDLERQLKTL 724
Cdd:PRK10246 477 ladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVNQSrLDALEKEVKKLGEEGAALRGQLDAL 556
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366637 725 TKQIKEE--------------TEEWRRFQADLQTAVVVANDI------KCEAQQELRTVKRRLLEEEEKNARLQKE 780
Cdd:PRK10246 557 TKQLQRDeseaqslrqeeqalTQQWQAVCASLNITLQPQDDIqpwldaQEEHERQLRLLSQRHELQGQIAAHNQQI 632
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-785 |
5.88e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 593 EVQEMLKVARAE-----KDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASE 667
Cdd:COG1196 217 ELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 668 SDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVV 747
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720366637 748 VANdikcEAQQELRTVKRRLLEEEEKNARLQKELGDIQ 785
Cdd:COG1196 373 ELA----EAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
548-753 |
6.56e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 548 KTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEM-LKVARAEKDQLQLSCTELRQEL------L 620
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAELEAQKEELaellraL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 621 KANGEIKHVSSLL-----AKMEKDYSYLKEVCDH---QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAV 692
Cdd:COG4942 114 YRLGRQPPLALLLspedfLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366637 693 KLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIK 753
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-778 |
6.57e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 383 LASLTEKIQKMEENQHSTAEELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLL 460
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 461 QERVKNEEpsaqggkvlELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHER 540
Cdd:COG4717 170 AELAELQE---------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 541 CNNSV------------------MAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVAR 602
Cdd:COG4717 241 LEERLkearlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 603 --AEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYS--YLKEVCDHQAEQLSR---TSLKLQEKASESDAEIKDM 675
Cdd:COG4717 321 leELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 676 KETIFELEDQVEQHRAVKLHNNQLISELEgsvikLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAvvVANDIKCE 755
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQL--EEDGELAE 473
|
410 420
....*....|....*....|...
gi 1720366637 756 AQQELRTVKRRLLEEEEKNARLQ 778
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALK 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
522-785 |
9.47e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 522 IKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEV-QEMLKV 600
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARlEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 601 ARAEKDQLQLSCTELRQELLKANGEIkhvssllakmekdysylkevcdhqaEQLSRTSLKLQEKASESDAEIKDMKETIF 680
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEEL-------------------------EELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 681 ELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANdikcEAQQEL 760
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----EEEEAL 444
|
250 260
....*....|....*....|....*
gi 1720366637 761 RTVKRRLLEEEEKNARLQKELGDIQ 785
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELL 469
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
36-151 |
1.75e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.63 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 36 DATASPARAGARCGTAATRSEAGGRRPSGSAEHGQPLSEAGGARDRSVGCGSRPLTAAPFPHRGPPRRGSRQGTIPTTKR 115
Cdd:PHA03307 198 PPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG 277
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720366637 116 TGIPAPRELSVTISRERSVPRGPSSSKKLGSSPTSS 151
Cdd:PHA03307 278 PSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPR 313
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-784 |
3.44e-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: 47.76 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 402 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLINL--LQERVKNEEPSAQGGKVLEL 479
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 480 EQkctdilEKSRFEREkLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNnsvMAKTLEECRVTLEG 559
Cdd:TIGR02169 236 ER------QKEAIERQ-LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---VKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 560 LKmenGSLKAL------LEADKQKAIEASSTVGQTAENFEvqEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLL 633
Cdd:TIGR02169 306 LE---RSIAEKereledAEERLAKLEAEIDKLLAEIEELE--REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 634 AKMEKDYSYLKEVCD---HQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKL 710
Cdd:TIGR02169 381 AETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366637 711 EEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRRLLEEEEKNARLQKELGDI 784
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
36-376 |
5.15e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.09 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 36 DATASPARAGArcgTAATRSEAGGRRPSGsaehgqPLSEAGGARDRSVGCGS-RPLTAAPFPHRGPPRRGSRQG--TIPT 112
Cdd:PHA03307 49 ELAAVTVVAGA---AACDRFEPPTGPPPG------PGTEAPANESRSTPTWSlSTLAPASPAREGSPTPPGPSSpdPPPP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 113 TKRTGIPAPRELSVTISRERSV----PRGPSSSKKLGSSPTSSCNPTPTKHLRTTPAKPKQEHEGAEKAVLESQVRELLA 188
Cdd:PHA03307 120 TPPPASPPPSPAPDLSEMLRPVgspgPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 189 EAKTKDSeinRLRSelkkckerwalSTEDANASDPSAegtASPESDAQPLIRTLEEKNKTFQKELADLEEENRALKEKLT 268
Cdd:PHA03307 200 AAASPRP---PRRS-----------SPISASASSPAP---APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 269 YLEQSPNSEGAASHTGDSSCPTSITHESSFGSPVGNELSSETDEYRRTTHGSALRTSGSSSSDVTKASLSPDASDfehIT 348
Cdd:PHA03307 263 ITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR---GA 339
|
330 340 350
....*....|....*....|....*....|.
gi 1720366637 349 ADTPSRPLS---ATSNPFKSSKGSPTGSSPN 376
Cdd:PHA03307 340 AVSPGPSPSrspSPSRPPPPADPSSPRKRPR 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
593-785 |
5.87e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 593 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEI 672
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 673 KDM------------------KETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEE 734
Cdd:COG4942 107 AELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720366637 735 wrrfQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQ 785
Cdd:COG4942 187 ----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
590-768 |
6.81e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 590 ENFEVQEMLKVARAEKDQL-----QLSCTELRQELLKANGEIKHVSSLlakMEKDYSYLKEVcDHQAEQLSRTSLKLQEK 664
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENlalleELDLDEAEEKNEEIQERIDQLYDI---LEREVKARKYV-EKNSDTLPDFLEHAKEQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 665 ASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQLISELEGSVIKLEEQK---SDLERQLKTLTKQIKEETEEWRRFQA 740
Cdd:PRK04778 326 NKELKEEIDRVKQS-YTLnESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQLEEIEKEQEKLSE 404
|
170 180 190
....*....|....*....|....*....|.
gi 1720366637 741 DLQT---AVVVANDIKCEAQQELRTVKRRLL 768
Cdd:PRK04778 405 MLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-730 |
1.51e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 378 ASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL- 456
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAa 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 457 --INLLQERVKNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCSL-----RKVEEENQGAIDMIKHLKEEN 529
Cdd:COG1196 491 arLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAAK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 530 EKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQ 609
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 610 LSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQH 689
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1720366637 690 RAVKLHNNQLISELEGSVIKLEEQK-------SDLERQLKTLTKQIKE 730
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEElpeppdlEELERELERLEREIEA 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
593-782 |
1.78e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 593 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEK-ASESDAE 671
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSgGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 672 IKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEwrrfQADLQTAVVVAND 751
Cdd:COG3883 107 VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|.
gi 1720366637 752 IKCEAQQELRTVKRRLLEEEEKNARLQKELG 782
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
388-781 |
1.89e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 388 EKIQKMEENQHSTAEELQATLQE----LSDQQQMVQELTAENEKLvdektiletsfhqhRERAEQLSQENEKLInllqer 463
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKV--------------SLKLEEEIQENKDLI------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 464 vknEEPSAQGGKVLELEQKCTDILEK-SRFEREKllniqqqltcslrkvEEENQGAIDMIKHLKEeneklngflehercn 542
Cdd:pfam05483 148 ---KENNATRHLCNLLKETCARSAEKtKKYEYER---------------EETRQVYMDLNNNIEK--------------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 543 nsvMAKTLEECRVTLEGLKMEngsLKALLEADKQKAIEASSTVGQTAENFEVQ-EMLKVARAEKDQLQLSCTELRQELLK 621
Cdd:pfam05483 195 ---MILAFEELRVQAENARLE---MHFKLKEDHEKIQHLEEEYKKEINDKEKQvSLLLIQITEKENKMKDLTFLLEESRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 622 ANGEIKHVSSLlakMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMK---ETIFEL----EDQVEQHRAVKL 694
Cdd:pfam05483 269 KANQLEEKTKL---QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLteekEAQMEELNKAKA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 695 HNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAqQELRTV---KRRLLEEE 771
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDEKLLDEK 424
|
410
....*....|
gi 1720366637 772 EKNARLQKEL 781
Cdd:pfam05483 425 KQFEKIAEEL 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
614-783 |
2.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 614 ELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRtslklQEKASESDAEIKDMKETIFELEDQVEQHRAvk 693
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQE----RREALQR-----LAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 694 lhNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTV---KRRLLEE 770
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleeRFAAALG 760
|
170
....*....|...
gi 1720366637 771 EEKNARLQKELGD 783
Cdd:COG4913 761 DAVERELRENLEE 773
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
388-727 |
3.36e-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: 44.35 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 388 EKIQKMEENQhstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETS-------------FHQHRERAEQLSqENE 454
Cdd:pfam05557 146 AKASEAEQLR----QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSkselaripelekeLERLREHNKHLN-ENI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 455 KLINLLQERV--------KNEEPSAQGGKV-LELEQKCTDILEKSRFEREKLLNIQQQLTCSlRKVEEENQGAIDmikhL 525
Cdd:pfam05557 221 ENKLLLKEEVedlkrkleREEKYREEAATLeLEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQQREIV----L 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 526 KEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEAsstvgqTAENFEVQEMLKVARAEk 605
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLL------TKERDGYRAILESYDKE- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 606 dqlqLSCTELRQELLKANGEikhvsslLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETifelEDQ 685
Cdd:pfam05557 369 ----LTMSNYSPQLLERIEE-------AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ----ESL 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720366637 686 VEQHRAVKLHNN--QLISELEGSVIKLEEQKSDLERQLKTLTKQ 727
Cdd:pfam05557 434 ADPSYSKEEVDSlrRKLETLELERQRLREQKNELEMELERRCLQ 477
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
546-791 |
3.98e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 546 MAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAEnfEVQEMLKVARAEKDQLQLSCTELRQELLKANGE 625
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELE--QLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 626 IKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEG 705
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQE----ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 706 SVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQ 785
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
....*.
gi 1720366637 786 GHSSSM 791
Cdd:COG4372 238 LLDALE 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
380-787 |
5.41e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 380 ELSLASLTEKIQK--MEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRERAEQLSQENE- 454
Cdd:TIGR00618 425 QLAHAKKQQELQQryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqETRKKAVVLARLLELQEEPc 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 455 ----KLINLLQERVKNEEPS-------------AQGGKVLE-LEQKCTDILEKSRFEREKLLNIQQ----------QLTC 506
Cdd:TIGR00618 505 plcgSCIHPNPARQDIDNPGpltrrmqrgeqtyAQLETSEEdVYHQLTSERKQRASLKEQMQEIQQsfsiltqcdnRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 507 SLRKVEEENQGAIDMIKHLKEENEKLNGFLE------HERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIE 580
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHallrklQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 581 ASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLlakmekdysylkevcDHQAEQLSRTSLK 660
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY---------------DREFNEIENASSS 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 661 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNqliSELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQA 740
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN---NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1720366637 741 DLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGH 787
Cdd:TIGR00618 807 EIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
383-717 |
5.53e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 383 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLvdEKTILETSfHQHRERAEQLsqeNEKLINLLQE 462
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL--RKSLLANR-FSFGPALDEL---EKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 463 RVKNEEPSAQGGKVleleqKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKH----LKEENEKLNGF--- 535
Cdd:PRK04778 181 FSQFVELTESGDYV-----EAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHLDHLdie 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 536 -----LEHERCNNSVMAKTLE--ECRVTLEGLKMENGSLKALLEadkqKAIEASSTVGQTAEnfEVQEMLKVARAEKDQL 608
Cdd:PRK04778 256 keiqdLKEQIDENLALLEELDldEAEEKNEEIQERIDQLYDILE----REVKARKYVEKNSD--TLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 609 QLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLkLQEKASESDAEIKDMKETIFELEDQVEQ 688
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSE-LQEELEEILKQLEEIEKEQEKLSEMLQG 408
|
330 340 350
....*....|....*....|....*....|.
gi 1720366637 689 HRAVKLHNNQLISELEG--SVIKLEEQKSDL 717
Cdd:PRK04778 409 LRKDELEAREKLERYRNklHEIKRYLEKSNL 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-607 |
7.59e-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: 42.44 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 383 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQE 462
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 463 RVKNEEPSAQGGKVLELeqkctdileksrFEREKLLNIQQQLTcSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCN 542
Cdd:COG4942 109 LLRALYRLGRQPPLALL------------LSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366637 543 NSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEvQEMLKVARAEKDQ 607
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
595-785 |
8.14e-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: 42.44 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 595 QEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKdysylkevcdhQAEQLSRTSLKLQEKASESDAEIKD 674
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------RIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 675 MKETIFELEDQVEQHRA------VKLHNNQLISELE--------GSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQA 740
Cdd:COG4942 88 LEKEIAELRAELEAQKEelaellRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366637 741 DLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQ 785
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
372-780 |
8.20e-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: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 372 GSSPNNASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhqhRERAEQLSQ 451
Cdd:pfam02463 129 GISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEE-----LKLQELKLK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 452 ENEKLINLLQERVKNEEPSAQGGKVLELEQkctdILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEK 531
Cdd:pfam02463 204 EQAKKALEYYQLKEKLELEEEYLLYLDYLK----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 532 LNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLS 611
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 612 CTELRQELLKangeikhvssllakmekdysylkevcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIF---ELEDQVEQ 688
Cdd:pfam02463 360 ELEKLQEKLE----------------------------QLEEELLAKKKLESERLSSAAKLKEEELELKseeEKEAQLLL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 689 HRAVKLHNNQLISELEGSVIKLEEQKSdLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLL 768
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEES-IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
410
....*....|..
gi 1720366637 769 EEEEKNARLQKE 780
Cdd:pfam02463 491 SRQKLEERSQKE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-786 |
1.01e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 385 SLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTilETSFHQHRERAEQLSQENEKLINLLqERV 464
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEEL-ERL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 465 KNEEPSAQGgkvlELEQKCTDILEKSRFEREKllniqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFL-------- 536
Cdd:TIGR02168 460 EEALEELRE----ELEEAEQALDAAERELAQL-----QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselis 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 537 ---EHERC--------NNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFE-VQEMLKVARAE 604
Cdd:TIGR02168 531 vdeGYEAAieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgFLGVAKDLVKF 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 605 KDQLQLSCTELRQELLKANgEIKHVSSLLAKMEKDYS------YLKEVCDHQAEQLSRTSLKLQEKASESD---AEIKDM 675
Cdd:TIGR02168 611 DPKLRKALSYLLGGVLVVD-DLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKTNSSILERRREIEeleEKIEEL 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 676 KETIFELEDQVEQHRavklhnnQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEE---WRRFQADLQTAVVVANDI 752
Cdd:TIGR02168 690 EEKIAELEKALAELR-------KELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAE 762
|
410 420 430
....*....|....*....|....*....|....
gi 1720366637 753 KCEAQQELRTVKRRLLEEEEKNARLQKELGDIQG 786
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
617-786 |
1.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 617 QELLKANGEIKhvsSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLqEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 696
Cdd:PRK03918 182 EKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 697 NQLISELEGSVIKLEEQKSDLERQLKTLtKQIKEETEEWRRFQADLQTAVVVANDIKCEA---QQELRTVKRRLLEEEEK 773
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLsrlEEEINGIEERIKELEEK 336
|
170 180
....*....|....*....|...
gi 1720366637 774 NAR----------LQKELGDIQG 786
Cdd:PRK03918 337 EERleelkkklkeLEKRLEELEE 359
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
376-706 |
1.19e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 376 NNASELSLASLTEKIQKMEENQHST--AEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQEN 453
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRlkKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 454 EKLInlLQERVKNEEPSAQGGKVLELEQKCTDILEKsrFEREKLLNIQQQLTCSLRKVEEENQgaidmikhLKEENEKLN 533
Cdd:pfam02463 812 EEAE--LLEEEQLLIEQEEKIKEEELEELALELKEE--QKLEKLAEEELERLEEEITKEELLQ--------ELLLKEEEL 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 534 GFLEHERcnnsvmAKTLEECRVTLEGLKMENGSLKALLEADKQKAIE---ASSTVGQTAENFEVQEMLKVARAEKDQLQL 610
Cdd:pfam02463 880 EEQKLKD------ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEeriKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 611 SCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHR 690
Cdd:pfam02463 954 NKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE----RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
330
....*....|....*.
gi 1720366637 691 AVKLHNNQLISELEGS 706
Cdd:pfam02463 1030 NKGWNKVFFYLELGGS 1045
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
382-734 |
1.23e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 382 SLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQ 461
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 462 ERVKNEEPSAQGGKVLELEQkctdiLEKSRFEREKLLNIQQQLTCSLRKVEEENqgaidmiKHLKEENEKLNGFLEHERC 541
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELA-----LKLTALHALQLTLTQERVREHALSIRVLP-------KELLASRQLALQKMQSEKE 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 542 NNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQtaENFEVQEMLKVARAEKDqlqlsctelrqELLK 621
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA--REDALNQSLKELMHQAR-----------TVLK 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 622 ANGEIKHVSSLLAKME----KDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLHNN 697
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLSR 836
|
330 340 350
....*....|....*....|....*....|....*...
gi 1720366637 698 -QLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEE 734
Cdd:TIGR00618 837 lEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-785 |
1.56e-03 |
|
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: 42.34 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 384 ASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQER 463
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 464 VKneepsaQGGKVLELEQKCTDILEKsrfereklLNIQQQLTCSLRKVEEEnqgaidmIKHLKEENEKLNGFLEHERCNN 543
Cdd:TIGR00606 771 ET------LLGTIMPEEESAKVCLTD--------VTIMERFQMELKDVERK-------IAQQAAKLQGSDLDRTVQQVNQ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 544 SVMAKTLEECRVTLEGLKMEngslKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELrQELLKAN 623
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIELNR----KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREI 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 624 GEIKHVSSLLAKMEKDYSYLKEVCDHQAEqlsrtslklqEKASESDAEIKDMKETIfeleDQVEQHRAVKLHNNQlisel 703
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKE----------TSNKKAQDKVNDIKEKV----KNIHGYMKDIENKIQ----- 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 704 EGSviklEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRRLLEEEEKNA 775
Cdd:TIGR00606 966 DGK----DDYLKQKETELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELK 1038
|
410
....*....|
gi 1720366637 776 RLQKELGDIQ 785
Cdd:TIGR00606 1039 QHLKEMGQMQ 1048
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
391-780 |
1.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 391 QKMEENQhsTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLINLLQERVKNEEP- 469
Cdd:PTZ00121 1385 KKAEEKK--KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAk 1457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 470 SAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCS------LRKVEEENQGAIDMIKhlKEENEKLNGFLEHERCNN 543
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkadeAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKK 1535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 544 SVMAKTLEECRVTLEGLKMEngSLKALLEA----DKQKAIEASSTVGQTAEnfEVQEMLKVARAEKDQLQLSCTELRQEL 619
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAE--ELKKAEEKkkaeEAKKAEEDKNMALRKAE--EAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 620 LKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSlklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQl 699
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE- 1687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 700 iSELEGSVIKLEEQKsdleRQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKN--ARL 777
Cdd:PTZ00121 1688 -KKAAEALKKEAEEA----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHL 1762
|
...
gi 1720366637 778 QKE 780
Cdd:PTZ00121 1763 KKE 1765
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
376-561 |
1.67e-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: 41.76 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 376 NNASELsLASLTEKIQKM------EENQHSTAEELQATLQElsdqqqMVQELTAENEKLVDEKTILETSFH-QHRE--RA 446
Cdd:pfam06160 259 DEAEEA-LEEIEERIDQLydllekEVDAKKYVEKNLPEIED------YLEHAEEQNKELKEELERVQQSYTlNENEleRV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 447 EQLSQENEKLI---NLLQERVKNEEP--SAQGGKVLELEQKCTDI-------------LEKSRFE-REKLLNIQQQLTCS 507
Cdd:pfam06160 332 RGLEKQLEELEkryDEIVERLEEKEVaySELQEELEEILEQLEEIeeeqeefkeslqsLRKDELEaREKLDEFKLELREI 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366637 508 LRKVEEEN-----QGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLK 561
Cdd:pfam06160 412 KRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLY 470
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
168-782 |
1.75e-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: 42.13 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 168 KQEHEGAEKAVLESQVRELLAEAKTKdseINRLRSELKKCKERWALSTE--DANASDPSAEGTASPESDAQPLirtleEK 245
Cdd:pfam12128 277 RQEERQETSAELNQLLRTLDDQWKEK---RDELNGELSAADAAVAKDRSelEALEDQHGAFLDADIETAAADQ-----EQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 246 NKTFQKELADLEEENRALKEKLTYLEQSPNSEGAAShtgDSSCPTSIThessfGSPVGNELSSETDEYRRT---THGSAL 322
Cdd:pfam12128 349 LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI---KEQNNRDIA-----GIKDKLAKIREARDRQLAvaeDDLQAL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 323 RTSGSSSSDVTKASLSPDASDFEHITADTPSRPLSATSNPfksskgsptgsspnnASELSLASLTEKIQKMEENQ-HSTA 401
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATP---------------ELLLQLENFDERIERAREEQeAANA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 402 EELQATLQE-----LSDQQqmvqeltaeNEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQERVKNEEPSAqgGKV 476
Cdd:pfam12128 486 EVERLQSELrqarkRRDQA---------SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI--GKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 477 LELEQKC-TDI-------------------LEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFL 536
Cdd:pfam12128 555 ISPELLHrTDLdpevwdgsvggelnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 537 EHERCNNSVMAKTLEECRVTLEGLKMENGSLK----ALLEADKQKAIEASSTVG--QTAENFEVQEMLKvarAEKDQLQL 610
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRLFDEKQSEKdkknKALAERKDSANERLNSLEaqLKQLDKKHQAWLE---EQKEQKRE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 611 SCTELRQELLKANGEIK-HVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKL---QEKASESDAEIKDMKETIFELE-DQ 685
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIERIAvRR 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 686 VEQHRAVKLHNNQLISELEgsviKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKR 765
Cdd:pfam12128 792 QEVLRYFDWYQETWLQRRP----RLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC 867
|
650 660
....*....|....*....|..
gi 1720366637 766 RL-----LEEEEKNARLQKELG 782
Cdd:pfam12128 868 EMsklatLKEDANSEQAQGSIG 889
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
3-169 |
1.80e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 3 MRGRGSPAGARSGSLAAGNWKALGSffDWSGPVDATASPARAGARCGTAATRSEAGGRRP-SGSAEHGQPLSEAGGARDR 81
Cdd:PHA03307 223 APGRSAADDAGASSSDSSSSESSGC--GWGPENECPLPRPAPITLPTRIWEASGWNGPSSrPGPASSSSSPRERSPSPSP 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 82 SV-GCGSRPLTAAPFPHRGPPRRGSrqgtipttkrtgIPAPRELSVTiSRERSVPRGPSSSKKLGSSPTSSCNPTPTKHL 160
Cdd:PHA03307 301 SSpGSGPAPSSPRASSSSSSSRESS------------SSSTSSSSES-SRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367
|
....*....
gi 1720366637 161 RTTPAKPKQ 169
Cdd:PHA03307 368 RPRPSRAPS 376
|
|
| PHA03309 |
PHA03309 |
transcriptional regulator ICP4; Provisional |
51-385 |
2.19e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 165564 [Multi-domain] Cd Length: 2033 Bit Score: 41.76 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 51 AATR-SEAGGRRP-SGSAEHGQPLS-EAGGARDRSVGCGSRPLTAAPFPHRG----PPRRGS----RQGT-IPTTKRTGI 118
Cdd:PHA03309 1633 AASRfDEADGEDPlPPAACGGKPIApETLVALCEQRGRGPTSLPRAPTPRSGealaAPRRSGakdpRQGQyCPSARRSEA 1712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 119 P---APRELSVTI-SRERSVPRGPSSSKKLGSsptssCNPTPTKHLRTTPAKP----KQEHEGAE-KAVLESQVRELLAE 189
Cdd:PHA03309 1713 PhspSPRDVALRLlERQQELNRQLLLELRRGS-----CEISPSPRRRDAEGRRfgcrQDDDDGYDyEGGRESPERVLGRR 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 190 AKTKDSEINRLRSELKKCKERWALSTEDANASDPSAEGTASPESDAQP---LIRTLEEKNKTFQKELADLEEENRAL--- 263
Cdd:PHA03309 1788 QSRRDSVPVRRRSGAANCGGRWMISAGRSSSSSSSSSSSSSSSPSSRPsrsATPSLSPSPSPPRRAPVDRSRSGRRRerd 1867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 264 KEKLTYLEQSPNSEGAASHTGDSS----CPTSITHESSFGSPVGNELSSETDEYRRTTHGSALRTSGSSSSDVTKASLSP 339
Cdd:PHA03309 1868 RPSANPFRWAPRQRSRADHSPDGTapgdAPLNLEDGPGRGRPIWTPSSATTLPSRSGPEDSVDETETEDSAPPARLAPSP 1947
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366637 340 -------DASDFEHITADTP----SRPLSATSNPFKSSKGSP--TGSSPNNASELSLAS 385
Cdd:PHA03309 1948 letsraeDSEDSEYPEYSNPrlgkSPPALKSREARRPSSKQPrrPSSGKNGHTDVSAAS 2006
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
593-780 |
2.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 593 EVQEMLKVARAEKDQLQlsctELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVcdHQAEQLSRTSLKLQEKASESDAEI 672
Cdd:COG4717 75 ELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 673 KDMKETIFELEDQVEQhravklhnnqlISELEGSVIKLEEQKSDLERQLKTLT-KQIKEETEEWRRFQADLQTAvvvaND 751
Cdd:COG4717 149 EELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAEL----EE 213
|
170 180
....*....|....*....|....*....
gi 1720366637 752 IKCEAQQELRTVKRRLLEEEEKNARLQKE 780
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
612-780 |
3.10e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 612 CTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRtslkLQEKASESDAEIKDMKETIFELEDQVEQHRA 691
Cdd:PRK04863 899 IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQS----DPEQFEQ----LKQDYQQAQQTQRDAKQQAFALTEVVQRRAH 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 692 VKLHNNQ-LISELEGSVIKLEEQKSDLE---RQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRL 767
Cdd:PRK04863 971 FSYEDAAeMLAKNSDLNEKLRQRLEQAEqerTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
170
....*....|...
gi 1720366637 768 LEEEEKNARLQKE 780
Cdd:PRK04863 1051 DSGAEERARARRD 1063
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
593-742 |
4.13e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 593 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDysyLKEVCDH-QAEQLSR--TSLKLqekasesd 669
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNkEYEALQKeiESLKR-------- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366637 670 aEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGsviKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADL 742
Cdd:COG1579 104 -RISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
376-712 |
4.20e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 376 NNASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQqqmVQELTAENEKLVdektilETSFHQHRERAEQLSQENEK 455
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQ---LEALKSESQNKI------ELLLQQHQDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 456 LINLLQERVKNEEPSAQggkvlELEQKCTDILEKSRFER-------EKLLNIQQQLTCSLR--------KVEEENQGAID 520
Cdd:pfam15921 279 EITGLTEKASSARSQAN-----SIQSQLEIIQEQARNQNsmymrqlSDLESTVSQLRSELReakrmyedKIEELEKQLVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 521 MIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAE-NFEVQEMLK 599
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 600 VARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVcdhqAEQLSRTSLKLQekasESDAEIKDMKETI 679
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV----VEELTAKKMTLE----SSERTVSDLTASL 505
|
330 340 350
....*....|....*....|....*....|....
gi 1720366637 680 FELEDQVEQhravklhNNQLISELEGSV-IKLEE 712
Cdd:pfam15921 506 QEKERAIEA-------TNAEITKLRSRVdLKLQE 532
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
663-781 |
4.84e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 663 EKASESDAEIKDMKETIFELEDQVEQHRavklhnnQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADL 742
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEE-------EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720366637 743 QTAVVVANDIKcEAQQELRTVKRRLLEEEEKNARLQKEL 781
Cdd:COG2433 458 RREIRKDREIS-RLDREIERLERELEEERERIEELKRKL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
654-744 |
5.32e-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: 39.75 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 654 LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETE 733
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|.
gi 1720366637 734 EWRRFQADLQT 744
Cdd:COG4942 91 EIAELRAELEA 101
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
182-791 |
5.88e-03 |
|
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: 40.42 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 182 QVRELLAEAKTKDSEINRLRS-ELKKCKERWALSTEDANASDPSAEGTASPESDAQPLIRTLEEKNKTFQKELADLEEEN 260
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 261 RALKEKLTYLEqspNSEGAASHTGDSSCPTSITHESSFGSpvgNELSSETDEYRrttHGSALRTSGSSSSDVTKASLSPD 340
Cdd:TIGR00606 336 RLLNQEKTELL---VEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFE---RGPFSERQIKNFHTLVIERQEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 341 ASDFEHITADTPSRPLSATSNPFK-SSKGSPTGSSPNNASELSLASLTEKIQKMEENQHSTA---------EELQATLQE 410
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQEQADEiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdrileldQELRKAERE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 411 LS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQERVKNEEPSAQGGKV-----LELEQKC 483
Cdd:TIGR00606 487 LSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIksrhsDELTSLL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 484 TDILEKSRFER--EKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLngflehERCNNSVMAKTLEECRVTLEGLK 561
Cdd:TIGR00606 567 GYFPNKKQLEDwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK------EEQLSSYEDKLFDVCGSQDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 562 MENGSlKALLEADKQKAIEASST-------VGQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLA 634
Cdd:TIGR00606 641 LERLK-EEIEKSSKQRAMLAGATavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELK 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 635 KMEKDYSYLKEVCDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAvKLHNNQLISELEGSVIKLE 711
Cdd:TIGR00606 720 KKEKRRDEMLGLAPGRQSIIDLKEKEIPElrnKLQKVNRDIQRLKNDIEEQETLLGTIMP-EEESAKVCLTDVTIMERFQ 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 712 EQKSDLERQLKTLTKQIKeeteewrrfQADLQTAVVVANDIKCEAQQELRTV------KRRLLEEEEKNAR-LQKELGDI 784
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVvskielNRKLIQDQQEQIQhLKSKTNEL 869
|
....*..
gi 1720366637 785 QGHSSSM 791
Cdd:TIGR00606 870 KSEKLQI 876
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
386-594 |
6.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 386 LTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRE---RAEQLSQENEKLINLLQE 462
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 463 RVKNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQltcsLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCN 542
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366637 543 NSVMAKTLEECRVTLEGLKMENGSL--KALLEADKQKAIEASSTVGQTAENFEV 594
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
358-750 |
7.73e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.56 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 358 ATSNPFKSSKGSPTGSSPNNASE--LSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTIL 435
Cdd:COG5185 190 KGISELKKAEPSGTVNSIKESETgnLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 436 ETS-FHQHRERAEQLSQENEKLINL---LQERVKNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKV 511
Cdd:COG5185 266 RLEkLGENAESSKRLNENANNLIKQfenTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 512 EEENQGAIDMIKHLKEENEKLNGFLEHERcnnsvMAKTLEECRVTLEGLKMENGSLKAlleADKQKAIEASSTVGQTAEN 591
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSK-----SSEELDSFKDTIESTKESLDEIPQ---NQRGYAQEILATLEDTLKA 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 592 FEVQEmlkvaraekdqlqlscTELRQELLKANGEIKHVSSLLAKMEKDYSylKEVCDHQAEQLSRTSLKLQEKASESDAE 671
Cdd:COG5185 418 ADRQI----------------EELQRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSK 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366637 672 IKDMKETIFELEDQVEQHRAvklhnnqliselegsviKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVAN 750
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKA-----------------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-786 |
8.03e-03 |
|
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: 39.67 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 383 LASLTEKIQKMEENQH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 456
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 457 -------INLLQERV--KNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCS-------------------- 507
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 508 ---------------------LRKVEEENQGAIDM--------------------IKHLKEENE---------------- 530
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAgratflplnkmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 531 -----KLNGFL-------EHER---------CNNSVMAKTLEECR--------VTLEGL------KMENGSLKALLEADK 575
Cdd:TIGR02169 589 dlsilSEDGVIgfavdlvEFDPkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGElfeksgAMTGGSRAPRGGILF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 576 QKAIEASSTVGQtAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLS 655
Cdd:TIGR02169 669 SRSEPAELQRLR-ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366637 656 RTSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEET 732
Cdd:TIGR02169 748 SLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366637 733 EEWRRFQADLQTAVVVANDIK------CEAQQELRTVKRRLLEEEEKNA----RLQKELGDIQG 786
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| |
