|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-557 |
4.34e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 3 ERFRNLDEEVEKYRAVYNKLRYEHtfLKSEFEHQKEEYARILDEgKIKYESEIARLEEDKEELRNQLLNVDLTKD----- 77
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEELELELEeaqae 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 78 ----SKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEK 153
Cdd:COG1196 290 eyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 154 ELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHsNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAV 233
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 234 EHHKVLLVEKDRELIRKVQAAKE--EGYQKLVVLQDEKLELENRLADLEKMKVEH-----DVWRQSEKDQYEEKLRASQM 306
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEaaLLEAALAELLEELAEAAARLLLLLEAEADYegfleGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 307 A---EEITRKELQSVRLKLQQQIVTiENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRN 383
Cdd:COG1196 529 LigvEAAYEAALEAALAAALQNIVV-EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 384 FRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHER--ITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEA 461
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVtlAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 462 KKEELETENQVLNRQNvpfEDYTRLQKRLKDIQRRHNEFRSLILVPNMPPTASINPVSFQSSAMVPSMELPFPPHMQEEQ 541
Cdd:COG1196 688 LAEEELELEEALLAEE---EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570
....*....|....*.
gi 1034579839 542 HQRELSLLRKRLEELE 557
Cdd:COG1196 765 LERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-471 |
3.24e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 100 AEVAELKAEKENSEAQVENAQRIQVR---QLAEMQATVRSLEAEKQSAN----LRAERLEKELQSSSEQNTFLINKLHKA 172
Cdd:TIGR02168 165 AGISKYKERRKETERKLERTRENLDRledILNELERQLKSLERQAEKAErykeLKAELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 173 EREINTLSSKVKELkhSNKLEITDIKLETAR-AKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRkV 251
Cdd:TIGR02168 245 QEELKEAEEELEEL--TAELQELEEKLEELRlEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-L 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 252 QAAKEEGYQKLVVLQDEKLELENRLADLEKMKvehdvwrQSEKDQYEEKLRASQMAEEItRKELQsvrlklqqqivtiEN 331
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESR-LEELE-------------EQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 332 AEKEKNENSDLKQQISSLQIQVTSLAQSENDLlnsnqmlKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKH 411
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 412 KLHERITDREEKYNQAKEKLQRAAIAQKkrkslheNKLKRLQEKVEVLEAKKEELETENQ 471
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE-------RELAQLQARLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-376 |
1.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 99 EAEVAE----LKAEKENSEAQV---------------ENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSS 159
Cdd:COG1196 208 QAEKAEryreLKEELKELEAELlllklreleaeleelEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 160 EQNTFLINKLHKAEREINTLSSKVKELKhSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVL 239
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 240 LVEKDRELIRKVQAAKEEgYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRKELQSVR 319
Cdd:COG1196 367 LLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579839 320 LKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVER 376
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-287 |
4.07e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 3 ERFRNLDEEVEKYRAVYNKLRYEhtFLKSEFEHQKEEYARILDEGKiKYESEIARLEEDKEELRNQLLNVDltkdsKRVE 82
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELE-----EEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 83 QLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQV---RQLAEMQATVRSLEAEKQSANLRAERLEKELQSSS 159
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 160 EQNTFLINKLHKAEREINTLSSKVKELKH---SNKLEITDIKLETARAKSELERERNKIQSELDGLQS-DNEILKAAVEH 235
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEE 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579839 236 HKVLLVEKDRELIRKVQAAK------EEGYQKLVVLQDEKLELENRLADLEKMKVEHD 287
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEelreelEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-494 |
3.02e-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: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 200 ETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKL-VVLQDEKLELENRLAD 278
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 279 LEKMKVEHDvwrQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQivtiENAEKEKNENSDLKQQISSLQIQVTSLAQ 358
Cdd:COG1196 290 EYELLAELA---RLEQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 359 SENDLLNSNQMLKEMVERLKQEcRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQ 438
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579839 439 KKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQ 494
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
245-556 |
4.52e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 245 RELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRkELQSVRLKLQQ 324
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE-RIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 325 QIVTIENAEKEKNENSDLKQQISSLQIQV-TSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEK-AQLEAEKTLEEK 402
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELeAQIEQLKEELKALREALDELRAELTLLNEEAANLRERlESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 403 QIQWLEEKhklHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFED 482
Cdd:TIGR02168 839 RLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034579839 483 -YTRLQKRLKDIQRRHNEFRSLILvpnmpPTASINPVSFQSSAMVPsMELPFPPHMQEEQHQRELSLLRKRLEEL 556
Cdd:TIGR02168 916 eLEELREKLAQLELRLEGLEVRID-----NLQERLSEEYSLTLEEA-EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-496 |
4.75e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 199 LETARAKSELERERNKIQSELDGLQSDNEILKAAVE--HHKVLLVEKDRELI----RKVQAAKEEGYQKLVVLQDEKLEL 272
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 273 ENRLADLEKmkvehdvwrqsEKDQYEEKLRASQMA-EEITRKELQSVRLKLQQQIVTIENAEKEKNEN-SDLKQQISSLQ 350
Cdd:TIGR02169 757 KSELKELEA-----------RIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 351 IQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTleEKQIQWLEEKHK-LHERITDREEKYNQAKE 429
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL--EAALRDLESRLGdLKKERDELEAQLRELER 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579839 430 KLQRAAIAQKKRKSLhenkLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRR 496
Cdd:TIGR02169 904 KIEELEAQIEKKRKR----LSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-504 |
9.13e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 1 MRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARIldegkikyESEIARLEEDKEELRNQLLNVDLTKDSKR 80
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--------EDRRERLQQEIEELLKKLEEAELKELQAE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 81 VEQLAREKVYLCQKLKGLEAEVAELKAEKEnseaQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSE 160
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELE----EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 161 QNTF------LINKLHKAEREINTLSSK----------------VKELKHSNKLEITDIKLETARAKSELERERNKIQSE 218
Cdd:TIGR02168 518 LSGIlgvlseLISVDEGYEAAIEAALGGrlqavvvenlnaakkaIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 219 LDGLQSDNEILKAAVEHHK--------VLLVEKDRELIRkvQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWR 290
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRKalsyllggVLVVDDLDNALE--LAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 291 QSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNEnsdLKQQISSLQIQVTSLAQSENDLLNSNQML 370
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQL 752
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 371 KEMVERLKQECRNFRSQAEKAQLEAE------KTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSL 444
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAeaeaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 445 HENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRSLI 504
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-501 |
9.59e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 3 ERFRNLDEEVEKYRAVYNKLRYEHTFLKSEfEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVDLTKDSKRVE 82
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAE-EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 83 QLAREKVYLCQKlKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQN 162
Cdd:PTZ00121 1325 EEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 163 TFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVE 242
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 243 KDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRKElqsvRLKL 322
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE----ELKK 1559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 323 QQQIVTIENAEKEKNEN------SDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQEcRNFRSQAEKAQLEAE 396
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKnmalrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQL 1638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 397 KTLEEKQIQWLEEKHKLHERITDREE----KYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKK---EELETE 469
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAeeakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaEEKKKA 1718
|
490 500 510
....*....|....*....|....*....|..
gi 1034579839 470 NQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFR 501
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-470 |
1.30e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 2 RERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYaRILDEGKIKYESEIARLEEDKEELRNQLLNVDLTKDSKRV 81
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 82 EQLAREkvylcQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQ 161
Cdd:COG1196 331 ELEELE-----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 162 NTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLV 241
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 242 EKDRELIRKVQAAKEEGYQKL---------------------VVLQDEKLE---LENRLADLEKMKVEHDVWRQSEKDQY 297
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYeaaLEAALAAALQNIVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 298 EEK----------------------------------LRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLK 343
Cdd:COG1196 566 LKAakagratflpldkiraraalaaalargaigaavdLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 344 QQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEK 423
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579839 424 YNQAKEKLQRAAIAQKKRKSLHEN-----------KLKRLQEKVEVLEAKKEELETEN 470
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEeealeelpeppDLEELERELERLEREIEALGPVN 783
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-501 |
3.82e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 3 ERFRNLDEEVEKYRAVYNKLRYEhTFLKSEFEHQKEEYARILDEGKIKYEsEIARLEEDK--EELRNqllnvdlTKDSKR 80
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIR-KFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKkaDEAKK-------AEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 81 VEQlAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEA--EKQSANLRAERLEKELQSS 158
Cdd:PTZ00121 1304 ADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 159 SEQNTFLINKLHKAEREINTLSSKVKELKhsnKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKV 238
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 239 LLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAE-EITRKELQS 317
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaEEAKKADEA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 318 VRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMlKEMVERLKQECRNFRSQAEKAQLEAEK 397
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 398 TLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQN 477
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
490 500
....*....|....*....|....
gi 1034579839 478 VPFEDYTRLQKRLKDIQRRHNEFR 501
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELK 1722
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-340 |
4.09e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 114 AQVENAQRIQvRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHsnklE 193
Cdd:COG4942 17 AQADAAAEAE-AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 194 ITDIKLETARAKSELER-----ERNKIQSELDGLQSDNEILKAAVEHHKV-LLVEKDRELIRKVQAAKEEGYQKLVVLQD 267
Cdd:COG4942 92 IAELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLkYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034579839 268 EKLELENRLADLEKMKVEHDVwRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENS 340
Cdd:COG4942 172 ERAELEALLAELEEERAALEA-LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
51-436 |
7.11e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 51 YESEIARLEEDKEELRNQLLNVDLTKDSKRvEQLARekvylcqklkgleaevaeLKAEKENSEAQVENAQRIQVRQLAEM 130
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKR-QQLER------------------LRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 131 QATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSnklEITDIKLETARAKSELER 210
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE---EQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 211 ERNKIQSELDGLQ-SDNEILKAAVEHHKVLL-VEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKmkvEHDV 288
Cdd:TIGR02169 306 LERSIAEKERELEdAEERLAKLEAEIDKLLAeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK---EFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 289 WRQsEKDQYEEKLraSQMAEEITRKELQSVRLKLQQQIVTIENAEKeKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQ 368
Cdd:TIGR02169 383 TRD-ELKDYREKL--EKLKREINELKRELDRLQEELQRLSEELADL-NAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579839 369 MLKEMVERLKQECrnFRSQAEKAQLEAEKTLEEKQIQWLEEKhklhERITDREEKYNQAKEKLQRAAI 436
Cdd:TIGR02169 459 QLAADLSKYEQEL--YDLKEEYDRVEKELSKLQRELAEAEAQ----ARASEERVRGGRAVEEVLKASI 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3-486 |
9.21e-06 |
|
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: 48.81 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 3 ERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKI-----KYESEIARLEEDKEELRNQLLNVDLTKD 77
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLrarieELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 78 SKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAER-----LE 152
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 153 KELQSSSEQNTFLINKLHKAEREINTLSSKV-KELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILK- 230
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEk 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 231 -AAVEHHKVLLVEKDRE-----LIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVW--RQSEKDQYEEKLR 302
Cdd:TIGR00618 459 iHLQESAQSLKEREQQLqtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpLTRRMQRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 303 ASQMAEEITRKELQSVRLKLQQqivTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECR 382
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRAS---LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 383 NFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAK 462
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
490 500
....*....|....*....|....
gi 1034579839 463 KEELETENQVLNRQNVPFEDYTRL 486
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDRE 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
9-346 |
9.49e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 9 DEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDegkIKYESEIARL---EEDK--EELRNQLLNVD--LTKDSKRV 81
Cdd:pfam15921 509 ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN---VQTECEALKLqmaEKDKviEILRQQIENMTqlVGQHGRTA 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 82 EQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVEnaqriqvrqlaEMQATVRSLEAEK-QSANLRAERLeKELQSSSE 160
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR-----------ELEARVSDLELEKvKLVNAGSERL-RAVKDIKQ 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 161 QNTFLINKLHKAEREINTLSSKVKELKH-----SNKLEIT--DIKLETARAKSELERERNKIQSeLDGlqSDNEILKAAV 233
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnkSEEMETTtnKLKMQLKSAQSELEQTRNTLKS-MEG--SDGHAMKVAM 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 234 EHHKVLLVEKDR-----ELIRKVQAAKEEGYQKLVVLQDEKLELENRLADL----EKMKVEHDVWRQSEKDQYEE----- 299
Cdd:pfam15921 731 GMQKQITAKRGQidalqSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatekNKMAGELEVLRSQERRLKEKvanme 810
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034579839 300 ------KLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQI 346
Cdd:pfam15921 811 valdkaSLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRL 863
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-503 |
1.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 31 SEFEHQKEEYARILDEGKIKYES------EIARLEEDKEELRNqllnvDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAE 104
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEheerreELETLEAEIEDLRE-----TIAETEREREELAEEVRDLRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 105 LKAEKENSEAQVE---------NAQRIQVRQ-LAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAER 174
Cdd:PRK02224 298 LLAEAGLDDADAEavearreelEDRDEELRDrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 175 EINTLSSKVKELKH-----SNKLEITDIKLETARAKSE-LERERNKIQSELDGLQSDNEILKAAVEHHKVLL-------- 240
Cdd:PRK02224 378 AVEDRREEIEELEEeieelRERFGDAPVDLGNAEDFLEeLREERDELREREAELEATLRTARERVEEAEALLeagkcpec 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 241 ------------VEKDRELIRKVQAAKEEgyqklvvLQDEKLELENRLADLEKM-KVEHDVWRQSEKDQYEEKLRASQmA 307
Cdd:PRK02224 458 gqpvegsphvetIEEDRERVEELEAELED-------LEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAER-R 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 308 EEITRKELQSVRLKLQQQIVTIENAEKEKnENSDLKQQISSLQIQVTSLaqsendllnsNQMLKEMVERLKQECRNFRSQ 387
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKRE-AAAEAEEEAEEAREEVAEL----------NSKLAELKERIESLERIRTLL 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 388 AEKAQLEAE-KTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQ-KKRKSLHENKLKRLQEKVEVLEAKKEE 465
Cdd:PRK02224 599 AAIADAEDEiERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEaREDKERAEEYLEQVEEKLDELREERDD 678
|
490 500 510
....*....|....*....|....*....|....*...
gi 1034579839 466 LETENQVLNRQnvpFEDYTRLQKRLKDIQRRHNEFRSL 503
Cdd:PRK02224 679 LQAEIGAVENE---LEELEELRERREALENRVEALEAL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
32-438 |
1.83e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 32 EFEHQKEEYARILDEgKIKYESEIARLEEDKEELRNQLlnvDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKEN 111
Cdd:COG4717 82 EAEEKEEEYAELQEE-LEELEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 112 SEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNK 191
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 192 LEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLE 271
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 272 LENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIV------------TIENAEKEKNEN 339
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeagvedeeELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 340 SDLKQQISSLQIQVTSLAQSENDLLNSNQ--MLKEMVERLKQECRnfRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERI 417
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELE--ELEEELEELREELAELEAELEQLEEDGELAELL 475
|
410 420
....*....|....*....|.
gi 1034579839 418 TDREEKYNQAKEKLQRAAIAQ 438
Cdd:COG4717 476 QELEELKAELRELAEEWAALK 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
29-224 |
1.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 29 LKSEFEHQKEEYARILDEG-KIKYESEIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKA 107
Cdd:COG4913 230 LVEHFDDLERAHEALEDAReQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 108 EKENSEAQVENAQR-----------IQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREI 176
Cdd:COG4913 310 ELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034579839 177 NTLSSKVKELKHSNKLEITDIKletaRAKSELERERNKIQSELDGLQS 224
Cdd:COG4913 390 AALLEALEEELEALEEALAEAE----AALRDLRRELRELEAEIASLER 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
13-504 |
6.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 13 EKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKiKYESEIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVylc 92
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--- 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 93 QKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSAnlRAERLEKELQSSSEQNTFLINKLHKA 172
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA--EEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 173 E--REINTLSSKVKELKHSN----KLEITDIKLETARAKSELERERNKIQSELDGLQSDN----------EILKAAVEHH 236
Cdd:PTZ00121 1467 EeaKKADEAKKKAEEAKKADeakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkaeeakkaDEAKKAEEKK 1546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 237 KVLLVEKDREL-----IRKVQAAKEEGYQKLVVL---QDEKLELENRLADLEKMKVEHDVWRQSE-KDQYEEKLRASQM- 306
Cdd:PTZ00121 1547 KADELKKAEELkkaeeKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEELk 1626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 307 AEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSlqiqvtslaQSENDllnsnqmlKEMVERLKQECRNFRS 386
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK---------KAEED--------KKKAEEAKKAEEDEKK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 387 QAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAK-EKLQRAAIAQKKRKS---LHENKLKRLQEKVEVLEAK 462
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaEEAKKEAEEDKKKAEeakKDEEEKKKIAHLKKEEEKK 1769
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1034579839 463 KEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRSLI 504
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
93-256 |
7.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 93 QKLKGLEAEVAELKAEkeNSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLIN----- 167
Cdd:COG3206 189 KELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspviq 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 168 ----KLHKAEREINTLSSK-------VKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHH 236
Cdd:COG3206 267 qlraQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
170 180
....*....|....*....|
gi 1034579839 237 KVLLVEkDRELIRKVQAAKE 256
Cdd:COG3206 347 PELEAE-LRRLEREVEVARE 365
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
78-476 |
1.18e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 78 SKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQL-AEMQATVRSLEAEKQSANLRAERLEKELQ 156
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 157 SSSEQ----NTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELER---ERNKIQSELDGLqsDNEIL 229
Cdd:pfam15921 303 IIQEQarnqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEartERDQFSQESGNL--DDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 230 KAAVEHHK-----VLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMK------VEHDVWRQSEKDQYE 298
Cdd:pfam15921 381 KLLADLHKrekelSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsecqgqMERQMAAIQGKNESL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 299 EKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNE---------------NSDLKQQISSLQIQVTSL------- 356
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDltaslqekeraieatNAEITKLRSRVDLKLQELqhlkneg 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 357 -----AQSENDLLNSNQMLKE-MVERLKQECRNFRS------------QAEKAQLEAE---KTLEEKQIQWLEEK----- 410
Cdd:pfam15921 541 dhlrnVQTECEALKLQMAEKDkVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKEindRRLELQEFKILKDKkdaki 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 411 HKLHERITDRE----EKYNQAKEKLQRAA-IAQKKRKSLHE-----NKLKRLQEKVEVLEA----KKEELETENQVLNRQ 476
Cdd:pfam15921 621 RELEARVSDLElekvKLVNAGSERLRAVKdIKQERDQLLNEvktsrNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQ 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-502 |
2.12e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 210 RERNKIQSELDGL-QSDNEILKAAVEhhkvllVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELEnRLADLEKMKVEHDV 288
Cdd:TIGR02169 153 VERRKIIDEIAGVaEFDRKKEKALEE------LEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 289 W-RQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKE------------KNENSDLKQQISSLQIQVTS 355
Cdd:TIGR02169 226 YeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLleelnkkikdlgEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 356 LAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKaqleaektLEEKQIQWLEEKHKLHERITDREEKYNqakEKLQRAA 435
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE--------LEREIEEERKRRDKLTEEYAELKEELE---DLRAELE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579839 436 IAQKKRKSLHEnKLKRLQEKVEVLEAKKEELETE-NQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRS 502
Cdd:TIGR02169 375 EVDKEFAETRD-ELKDYREKLEKLKREINELKRElDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
183-493 |
2.25e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 183 VKELKHSNKLEITDIKLETARAK-SELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQK 261
Cdd:PRK05771 22 LEALHELGVVHIEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 262 LVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDqyEEKLRasqmaeeitRKELQSVRLKLqqqiVTIENAEKEKNENSD 341
Cdd:PRK05771 102 IKELEEEISELENEIKELEQEIERLEPWGNFDLD--LSLLL---------GFKYVSVFVGT----VPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 342 LKQQ-ISSLQIQVTSLAQSENDLLNsnqmlkemverlkqecrNFRSQAEKAQLEAEKTLEEKQIQwlEEKHKLHERITDR 420
Cdd:PRK05771 167 ENVEyISTDKGYVYVVVVVLKELSD-----------------EVEEELKKLGFERLELEEEGTPS--ELIREIKEELEEI 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579839 421 EEKYNQAKEKLqraaiaqKKRKSLHENKLKRLQEK----VEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDI 493
Cdd:PRK05771 228 EKERESLLEEL-------KELAKKYLEELLALYEYleieLERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELIDKA 297
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-224 |
2.86e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 2 RERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFE------HQKEEYARILDEGKIKYESEIARLEEDKEELRNQL--LNVD 73
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLArleaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 74 LTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAE-------KENSEAQVENAQRIQVR---QLAEMQATVRSLEAEKQS 143
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDleeQIEELSEDIESLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 144 ANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHsNKLEITDIKLETARAKSELERERNKIQSELDGLQ 223
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
.
gi 1034579839 224 S 224
Cdd:TIGR02168 943 E 943
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
52-179 |
3.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 52 ESEIARLEEDKEELRNQllNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiQVRQLAEMQ 131
Cdd:COG4913 667 EREIAELEAELERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLA 743
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034579839 132 ATVRSLEAEKQSANLRAERLEKELQSS-SEQNTFLINKLHKAEREINTL 179
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-503 |
4.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 42 RILDEGKIKYESEIARLEEDKEELRNQllNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVenaqr 121
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEK--EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE----- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 122 iqvRQLAEMQATVRSLEAEKQSANLRAERLEKElqssseqntflINKLHKAEREINTLSSKVKELKHSNKL--EITDIKL 199
Cdd:PRK03918 245 ---KELESLEGSKRKLEEKIRELEERIEELKKE-----------IEELEEKVKELKELKEKAEEYIKLSEFyeEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 200 ETARAKSELERERNKIQSELDGLQSDNEILKAavehhkvlLVEKDRELIRKVQAAKE--EGYQKLVVLQDEKLELENRLA 277
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEE--------LKKKLKELEKRLEELEErhELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 278 DLEKMKVEHDVWR-QSEKDQYEEKL-----RASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQ----QIS 347
Cdd:PRK03918 383 GLTPEKLEKELEElEKAKEEIEEEIskitaRIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEeytaELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 348 SLQIQVTSLAQSENDLLNSnqmLKEMVERLKQECRNFRSQAEKAQL-EAEKTLEEKQIQWLEEKHKLHERItdrEEKYNQ 426
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKE---LRELEKVLKKESELIKLKELAEQLkELEEKLKKYNLEELEKKAEEYEKL---KEKLIK 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579839 427 AKEKLQRAAIAQKKRKSLhENKLKRLQEKVEVLEAKKEELETENQVLNrqnvpFEDYTRLQKRLKDIQRRHNEFRSL 503
Cdd:PRK03918 537 LKGEIKSLKKELEKLEEL-KKKLAELEKKLDELEEELAELLKELEELG-----FESVEELEERLKELEPFYNEYLEL 607
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-469 |
4.72e-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: 42.83 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 252 QAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEhdvwRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIEN 331
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 332 AEKEKNENSD-LKQQISSLQ-------IQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRsqAEKAQLEAEKTLEEKQ 403
Cdd:COG4942 95 LRAELEAQKEeLAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR--ADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579839 404 IQWLEEkhkLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETE 469
Cdd:COG4942 173 RAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-497 |
5.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 1 MRERFRNLDEEVEKYRAVYNKLRYehtfLKSEFEHQKEEYARILDEGKiKYESEIARLEEDKEELRNQLLNV-DLTKDSK 79
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELeEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 80 RVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQsss 159
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-RIKELEEKEERLEELKKKLKELEKRLEELEERHE--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 160 eqntflinKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAV------ 233
Cdd:PRK03918 363 --------LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkka 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 234 ------------EHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEkdQYEEKL 301
Cdd:PRK03918 435 kgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK--ELEEKL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 302 RaSQMAEEITRKElqsvrlklqqqivtiENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQEC 381
Cdd:PRK03918 513 K-KYNLEELEKKA---------------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 382 RNFRSQAEKAQLEAEKTLEEkqiqwLEEKHKLHERITDreekynqAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEA 461
Cdd:PRK03918 577 KELEELGFESVEELEERLKE-----LEPFYNEYLELKD-------AEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034579839 462 KKEELETENQVLNRqnvpfEDYTRLQKRLKDIQRRH 497
Cdd:PRK03918 645 LRKELEELEKKYSE-----EEYEELREEYLELSREL 675
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
54-499 |
6.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 54 EIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQR----IQVRQLAE 129
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 130 MQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKletaRAKSELE 209
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE----AALRDLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 210 RERNKIQSELDGLQS-------DNEILKAAVEHHkvLLVEKDR-----ELIrKVQAAKE------EGY---QKLVVLQDE 268
Cdd:COG4913 419 RELRELEAEIASLERrksnipaRLLALRDALAEA--LGLDEAElpfvgELI-EVRPEEErwrgaiERVlggFALTLLVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 269 KLELE-NRLADLEKMKVEHDVWR--QSEKDQYEEKLRASQMAEEITRKE---LQSVRLKLQQQ--IVTIENAE------- 333
Cdd:COG4913 496 EHYAAaLRWVNRLHLRGRLVYERvrTGLPDPERPRLDPDSLAGKLDFKPhpfRAWLEAELGRRfdYVCVDSPEelrrhpr 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 334 --------------KEKNENSDL----------KQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAE 389
Cdd:COG4913 576 aitragqvkgngtrHEKDDRRRIrsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 390 KAQLE-----AEKTLE--EKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAK 462
Cdd:COG4913 656 YSWDEidvasAEREIAelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
490 500 510
....*....|....*....|....*....|....*..
gi 1034579839 463 KEELETENQVlnrqnvpfEDYTRLQKRLKDIQRRHNE 499
Cdd:COG4913 736 LEAAEDLARL--------ELRALLEERFAAALGDAVE 764
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
94-471 |
6.34e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 94 KLKGLEAEVAELKAEKENSEAQVENAqriqVRQLAEMQATVRSLEAEKQsanlRAERLEKELQSSSEqntflinKLHKAE 173
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQA----RETRDEADEVLEEHEERRE----ELETLEAEIEDLRE-------TIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 174 REINTLSSKVKELKhsNKLEITDIKLETARAKSELER-ERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQ 252
Cdd:PRK02224 272 REREELAEEVRDLR--ERLEELEEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 253 AAKEegyqklvvLQDEKLELENRLADLEkmkvehdvwrqSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENA 332
Cdd:PRK02224 350 DADD--------LEERAEELREEAAELE-----------SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 333 EKEK----NENSDLKQQISSLQiqvTSLAQSENDLLNSNQMLKE--------MVERLKQECRNFRSQAEKAQLEAEKTLE 400
Cdd:PRK02224 411 EDFLeelrEERDELREREAELE---ATLRTARERVEEAEALLEAgkcpecgqPVEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579839 401 EKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAiaqkKRKSLHENKLKRLQEKVEVLEAKKEELETENQ 471
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLE----ELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
29-481 |
7.17e-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: 42.42 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 29 LKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVD-LTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKA 107
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRlLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 108 EKENSEAQVENAQRIQVRQLAEMQAtvrsleaEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELK 187
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRR-------QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 188 HSNK----LEI-----TDIKLETARAKSELEReRNKIQSELDGLQSDNEILKAAVEhHKVLLVEKDRELIRKVQaaKEEG 258
Cdd:pfam05557 167 EAEQrikeLEFeiqsqEQDSEIVKNSKSELAR-IPELEKELERLREHNKHLNENIE-NKLLLKEEVEDLKRKLE--REEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 259 YQ-KLVVLQDEKLELENRLADLEKMKVEH--------DVWRQSEKDQYEEK-LRASQMAEEITRKELQSVRLKLQQQI-V 327
Cdd:pfam05557 243 YReEAATLELEKEKLEQELQSWVKLAQDTglnlrspeDLSRRIEQLQQREIvLKEENSSLTSSARQLEKARRELEQELaQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 328 TIENAEKEKNENSDLKQQISSLQIQVtSLAQSENDLLnsNQMLKEMVERLKQEcrNFRSQAEKAQLEAEKTLEEKQIQWL 407
Cdd:pfam05557 323 YLKKIEDLNKKLKRHKALVRRLQRRV-LLLTKERDGY--RAILESYDKELTMS--NYSPQLLERIEEAEDMTQKMQAHNE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034579839 408 EEKHKLhERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRlqEKVEVLEAKKEELETENQVLNRQNVPFE 481
Cdd:pfam05557 398 EMEAQL-SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNELE 468
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
59-194 |
8.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 59 EEDKEELRNQLLNVDLTKDSKRVEQLARekvylcqKLKGLEAEVAELKAEkenseaqvenaqriqvrqLAEMQATVRSLE 138
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAE------------------LEEKDERIERLE 447
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 139 AE----KQSANLRAERlEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEI 194
Cdd:COG2433 448 RElseaRSEERREIRK-DREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
73-503 |
1.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 73 DLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQvrQLAEMQATVRSLEAEKQSANLRAERLE 152
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 153 KELQSSSEqntfLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAA 232
Cdd:COG4717 153 ERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 233 VEHHKV-LLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVE----HDVWRQSEKDQYEEKLRASQMA 307
Cdd:COG4717 229 LEQLENeLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 308 EEITRKELQSVRLKLQQQIVTIENaEKEKNENSDLKQQISSLQIQVTSLAQSENDLlnsnqmlkemveRLKQECRNFRSQ 387
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEEL------------QLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 388 AEKAQLEAEKTLEEKQIQWlEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKslHENKLKRLQEKVEVLEAKKEELE 467
Cdd:COG4717 376 LAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....*.
gi 1034579839 468 TENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRSL 503
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-467 |
1.39e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 161 QNTFLINKLHKAEREiNTLSSKVKELKHSnKLEITDIKLETARAKSELERERNKIQSElDGLQSDNEILKAAVEHHKVLL 240
Cdd:pfam17380 267 ENEFLNQLLHIVQHQ-KAVSERQQQEKFE-KMEQERLRQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 241 VEKDRELIRKVQaakEEGYQKLVVLQDEKLELE-NRLADLEKMKVEHDvwRQSEKDQYE-EKLRASQMAEEITRKELQSV 318
Cdd:pfam17380 344 MERERELERIRQ---EERKRELERIRQEEIAMEiSRMRELERLQMERQ--QKNERVRQElEAARKVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 319 RLKLQQQIVTIENA---------EKEKNENSDLKQQISSLQIQVTSLAQSENDLlnsnqmlKEMVERLKQECRNFRSQAE 389
Cdd:pfam17380 419 KVEMEQIRAEQEEArqrevrrleEERAREMERVRLEEQERQQQVERLRQQEEER-------KRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579839 390 KAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELE 467
Cdd:pfam17380 492 QRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
69-281 |
1.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 69 LLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiqvrQLAEMQATVRSLEAEKQSANLRA 148
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 149 ERLEKELQSSSEQNTFLINKLHKAEREINTLS--SKVKELKHSNKLEITDIKLETARAKSELERER-NKIQSELDGLQSD 225
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579839 226 NEILKAAVEHHKVLLVEKDRELiRKVQAAKEEGYQKLVVLQDEKLELENRLADLEK 281
Cdd:COG4942 166 RAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
385-499 |
1.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 385 RSQAEKAQLEAEKTLEE--------KQIQWLEEKHKLHERITDREEKYNQAKEKLQRaaiaQKKRKSLHENKLKRlqeKV 456
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEakkeaeaiKKEALLEAKEEIHKLRNEFEKELRERRNELQK----LEKRLLQKEENLDR---KL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1034579839 457 EVLEAKKEELETENQVLNRQNvpfEDYTRLQKRLKDIQRRHNE 499
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQ---QELEKKEEELEELIEEQLQ 142
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-467 |
1.99e-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: 41.21 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 111 NSEAQVENAQRIQVRqLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKhsN 190
Cdd:TIGR02169 668 FSRSEPAELQRLRER-LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE--E 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 191 KLEITDIKLETARAK-SELERERNKIQSELDGLQSDNEILKAAVEHHKV----LLVEKDRELIRKVQAAKEEGYQKLVVL 265
Cdd:TIGR02169 745 DLSSLEQEIENVKSElKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 266 QDEKLELENRLADLEKMKVEHDVWRQSEKDQYEE-KLRASQMAEEITRKELQSVRLklqqqivtIENAEKEKNENSDLKQ 344
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlNGKKEELEEELEELEAALRDL--------ESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 345 QISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQwlEEKHKLHERITDREEKY 424
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ--AELQRVEEEIRALEPVN 974
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034579839 425 NQAKEKLQRAaiaqkkrkslhENKLKRLQEKVEVLEAKKEELE 467
Cdd:TIGR02169 975 MLAIQEYEEV-----------LKRLDELKEKRAKLEEERKAIL 1006
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
128-498 |
2.27e-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: 41.19 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 128 AEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIkletARAKSE 207
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI----QRLKND 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 208 LERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHD 287
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 288 VWRQSEKDQYEEKLRASQMAEEITRKELQsVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSN 367
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQ-IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 368 QML---------------KEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERiTDREEKYNQAKEKLQ 432
Cdd:TIGR00606 926 EELissketsnkkaqdkvNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC-EKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579839 433 RAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPF-EDYTRLQKRLKDIQRRHN 498
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMkQEHQKLEENIDLIKRNHV 1071
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
62-387 |
3.61e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 62 KEELRNQLLNV----DLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQriqvRQLAEMQATVRSl 137
Cdd:PRK11281 38 EADVQAQLDALnkqkLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQ----AELEALKDDNDE- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 138 EAEKQSANLRAERLEKELQSSSEQntflinkLHKAEREINTLSSKVkelkhsnkleitdIKLETArakseLERERNKIQS 217
Cdd:PRK11281 113 ETRETLSTLSLRQLESRLAQTLDQ-------LQNAQNDLAEYNSQL-------------VSLQTQ-----PERAQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 218 ELDGLQSDNEILKAavehhkvllVEKDRELIRKVQAAKEEGYQKLVVLQDE--KLELEN--RLADLEKMKVEHDVWRQse 293
Cdd:PRK11281 168 NSQRLQQIRNLLKG---------GKVGGKALRPSQRVLLQAEQALLNAQNDlqRKSLEGntQLQDLLQKQRDYLTARI-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 294 kDQYEEKLRASQmaEEITRKelqsvRLKLQQQIVT-IENAEK--EKNENSDLKQQIS-SLQIQVTSLAQSE--NDLLNSN 367
Cdd:PRK11281 237 -QRLEHQLQLLQ--EAINSK-----RLTLSEKTVQeAQSQDEaaRIQANPLVAQELEiNLQLSQRLLKATEklNTLTQQN 308
|
330 340
....*....|....*....|
gi 1034579839 368 QMLKEMVERLKQECRNFRSQ 387
Cdd:PRK11281 309 LRVKNWLDRLTQSERNIKEQ 328
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1-159 |
3.70e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.74 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 1 MRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVDLTKdskr 80
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 81 vEQLAREKVYLCQKLKGLEAEVAELKAEKEN------SEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKE 154
Cdd:pfam09787 128 -EELRRSKATLQSRIKDREAEIEKLRNQLTSksqsssSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQ 206
|
....*
gi 1034579839 155 LQSSS 159
Cdd:pfam09787 207 IKELQ 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-231 |
4.18e-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: 40.05 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 37 KEEYARILDEGKIKYESEIARLEEDKEELRnqllnvdltkdsKRVEQLAREKVYLCQKLKGLEAEVAELKAEKEnseaQV 116
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELE------------REIEEERKRRDKLTEEYAELKEELEDLRAELE----EV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 117 ENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKEL-----KHSNK 191
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleikKQEWK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034579839 192 LEITDIKLETARAK-SELERERNKIQSELDGLQSDNEILKA 231
Cdd:TIGR02169 457 LEQLAADLSKYEQElYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
93-279 |
5.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 93 QKLKGLEAEVAELKAEKENSEAQVENAQRI-----QVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNtfliN 167
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAEldalqERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS----D 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 168 KLHKAEREINTLSSKVKELKHsnklEITDIKLETARAKSELERernkIQSELDGLQSDNEILKAAVEHHKVLLVEK--DR 245
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE----ELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLELRALLEErfAA 757
|
170 180 190
....*....|....*....|....*....|....*
gi 1034579839 246 ELIRKVQAAKEEGYQK-LVVLQDEKLELENRLADL 279
Cdd:COG4913 758 ALGDAVERELRENLEErIDALRARLNRAEEELERA 792
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
260-467 |
6.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 260 QKLVVLQDEKLELENRLADLekmkvehdvwrQSEKDQYEEKLRASQMAEEITRKELQsvrlKLQQQIVTIENAEKEKNEn 339
Cdd:COG3883 23 KELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEID----KLQAEIAEAEAEIEERRE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 340 sDLKQQISSLQIQVTSL--------AQSENDLLNSNQMLKEMVERLKQECRNFrsQAEKAQLEAEKTLEEKQIQWLEEKh 411
Cdd:COG3883 87 -ELGERARALYRSGGSVsyldvllgSESFSDFLDRLSALSKIADADADLLEEL--KADKAELEAKKAELEAKLAELEAL- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579839 412 klheritdrEEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELE 467
Cdd:COG3883 163 ---------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
329-476 |
6.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 329 IENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLE 408
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579839 409 EKHK-LHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQ 476
Cdd:COG4717 153 ERLEeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
29-394 |
7.40e-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: 39.33 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 29 LKSEFEHQKEEYARIL---DEGKIKYESEIARLEEDKEELRNQLlnVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAEL 105
Cdd:pfam15921 438 MKSECQGQMERQMAAIqgkNESLEKVSSLTAQLESTKEMLRKVV--EELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 106 KAEKENSEAQVEnAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKE 185
Cdd:pfam15921 516 NAEITKLRSRVD-LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 186 LKHsnklEITDIKLETARAKSELERERNKIQsELDGLQSDNEIlkaavehHKVLLVEKDRELIRKVQAAKEEGYQKLVVL 265
Cdd:pfam15921 595 LEK----EINDRRLELQEFKILKDKKDAKIR-ELEARVSDLEL-------EKVKLVNAGSERLRAVKDIKQERDQLLNEV 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 266 QDEKLELENRLADLEKMKveHDVWRQSEK-----DQYEEKLRASQMAEEITRKELQS----------VRLKLQQQIVT-- 328
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLK--RNFRNKSEEmetttNKLKMQLKSAQSELEQTRNTLKSmegsdghamkVAMGMQKQITAkr 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 329 ----------------IENAEKEKNEnsdLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQ 392
Cdd:pfam15921 741 gqidalqskiqfleeaMTNANKEKHF---LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
..
gi 1034579839 393 LE 394
Cdd:pfam15921 818 LQ 819
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
114-362 |
7.87e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 114 AQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKhsNKLE 193
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR--EELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 194 itdiklETARAKSELERERNKIQSELDGlQSDNEILK--AAVEHhkvlLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLE 271
Cdd:COG3883 90 ------ERARALYRSGGSVSYLDVLLGS-ESFSDFLDrlSALSK----IADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 272 LENRLADLEKMKVEHDVwRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQI 351
Cdd:COG3883 159 LEALKAELEAAKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|.
gi 1034579839 352 QVTSLAQSEND 362
Cdd:COG3883 238 AAAAAAASAAG 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
52-225 |
9.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 52 ESEIARLEEDKEELRNQL--LNVDLTKDSKRVEQLAR--EKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQvRQL 127
Cdd:COG4913 616 EAELAELEEELAEAEERLeaLEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE-EQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579839 128 AEMQATVRSLEAEKQSANLRAERLEKELQSSSEQntflINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSE 207
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170
....*....|....*...
gi 1034579839 208 LERERNKIQSELDGLQSD 225
Cdd:COG4913 771 LEERIDALRARLNRAEEE 788
|
|
| |
