|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-628 |
1.60e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKK 487
Cdd:COG1196 231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 488 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915607 568 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVAQ 628
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-581 |
3.39e-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: 66.62 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 364 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 438
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 439 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 512
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915607 513 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDK 581
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-587 |
1.33e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 309 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 388
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 389 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 468
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 469 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 548
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270
....*....|....*....|....*....|....*....
gi 966915607 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEET 587
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
374-616 |
4.18e-10 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 61.75 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 374 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 446
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 447 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 519
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 520 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQReaefssaghslqdkqsvEETSGEGPEVEME 597
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE-----------------YEEKEQTLNAELE 310
|
250
....*....|....*....
gi 966915607 598 SWQKQYDSLQKIVEKQQQK 616
Cdd:pfam15905 311 ELKEKLTLEEQEHQKLQQK 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
352-625 |
1.20e-08 |
|
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: 58.11 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 352 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 426
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 427 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 507 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSV 584
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETII----KNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 966915607 585 EETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-627 |
1.68e-08 |
|
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: 57.77 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 481
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 482 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 547
Cdd:TIGR02169 274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 548 EETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVA 627
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-621 |
6.28e-08 |
|
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: 55.84 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 305 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 382
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 383 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 462
Cdd:TIGR02169 786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 463 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTE 542
Cdd:TIGR02169 841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL---------KKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 543 LE----------SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSV-----EETSGEGP-----EVEMESWQKQ 602
Cdd:TIGR02169 908 LEaqiekkrkrlSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAElqrveEEIRALEPvnmlaIQEYEEVLKR 987
|
330
....*....|....*....
gi 966915607 603 YDSLQKIVEKQQQKMDQLR 621
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-628 |
8.63e-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: 55.45 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 419 TFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE---EVKKQEERVKGRDKHINNLKKKCQKESEQ 495
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 496 NREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAG 575
Cdd:TIGR02168 742 VEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 576 HSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEK-------QQQKMDQLRSQVQVAQ 628
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALL 879
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-565 |
1.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 361 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 440
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 520
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966915607 521 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLR 565
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-625 |
1.88e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 304 REQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQL 381
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAevEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 382 EQKVRESElqVHSALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIrESLKVAL 461
Cdd:TIGR02168 774 EEELAEAE--AEIEELEA----------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-AATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 462 QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSElkstelqEKVT 541
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL--RSELEELSEELRELE-------SKRS 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 542 ELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQSVEEtsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQLR 621
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDN-------LQERLSEEY------SLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....
gi 966915607 622 SQVQ 625
Cdd:TIGR02168 979 NKIK 982
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
293-628 |
2.27e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 293 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELL- 370
Cdd:pfam10174 57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 371 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 422
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 423 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVkKQEERVKGRDKHINN----LK 486
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEI-KQMEVYKSHSKFMKNkidqLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 487 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915607 567 REAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVAQ 628
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
420-625 |
4.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 420 FLRAQFAqktEALSREKIDLEK----KLSASEVEVQLIRESLKVALQKHsEEVKKQEERVKGRDKHINNLKKkcqkeseQ 495
Cdd:COG4717 42 FIRAMLL---ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEA-------E 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 496 NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaiCRDRETQLESLRQREAEfSSAG 575
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE-LLEQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966915607 576 HSLQDKQSVEETSGegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:COG4717 186 LSLATEEELQDLAE-----ELEELQQRLAELEEELEEAQEELEELEEELE 230
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
411-628 |
5.32e-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: 52.72 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 411 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 489 CQKESEQNREKQQRIET-------LERYLADLPT-LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRE 558
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQnnkkikeLEKQLNQLKSeISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915607 559 TQLESLRQ----REAEFSSAGHSLQDKQS---VEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVAQ 628
Cdd:TIGR04523 342 EQISQLKKeltnSESENSEKQRELEEKQNeieKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
410-627 |
9.72e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRENTFLRAQFAQ---KTEALSREKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHIN 483
Cdd:COG4942 28 ELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 484 NLKKKCQKESEQNREK----QQRIETLERYLADLPTLEDHQKQsqQLKDSELKSTELQEKVTELESLLEETQAICRDRET 559
Cdd:COG4942 108 ELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARRE--QAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915607 560 QLESLRQREAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVA 627
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAA-------ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-567 |
1.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 361 EHLLKEKELLID-----KQRKHISQLEQKVRESELQVHsALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALS 433
Cdd:COG4913 215 EYMLEEPDTFEAadalvEHFDDLERAHEALEDAREQIE-LLEPIRELAERYaaARERLAELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 434 REKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKKCQKESEQNREKQQRIETLERYLAD 512
Cdd:COG4913 294 EAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915607 513 L--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG4913 371 LglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
427-622 |
1.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 427 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 507 ERYLADLPTLEDHQKQSQQLKdsELKStELQEKVTELESLLEetqaicrDRETQLESLRQREAEFSSaghslqDKQSVEE 586
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLS--EFYE-EYLDELREIEKRLS-------RLEEEINGIEERIKELEE------KEERLEE 342
|
170 180 190
....*....|....*....|....*....|....*....
gi 966915607 587 TSGEGPEVEmeswqKQYDSLQKIVEKQQ---QKMDQLRS 622
Cdd:PRK03918 343 LKKKLKELE-----KRLEELEERHELYEeakAKKEELER 376
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
410-623 |
1.77e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRE-NTFLRAQFAQKT-------------EALSREKIDLEKKlsaseveVQLIRESLKVALQKHSEEVKKQEERV 475
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANRqrekekerykrdrEQWERQRRELESR-------VAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 476 KGRDKhinnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvtel 543
Cdd:pfam07888 108 ASSEE----LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 544 eslLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQL 620
Cdd:pfam07888 180 ---LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGL 256
|
...
gi 966915607 621 RSQ 623
Cdd:pfam07888 257 GEE 259
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-582 |
4.50e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 361 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFA----------Q 427
Cdd:TIGR02169 684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQEEEKLKERLEeleedlssleQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 428 KTEALSREKIDLEKKLSASE---VEVQLIRESLKVAL--------QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQN 496
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEedlHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 497 REKqqrIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGH 576
Cdd:TIGR02169 832 EKE---IQELQEQRIDL---------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
....*.
gi 966915607 577 SLQDKQ 582
Cdd:TIGR02169 900 ELERKI 905
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
408-587 |
4.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQRENTFLRAQ---FAQKTEALSR---EKIDLEKKLSASEVEVQLIRESLKV--------ALQKHSEEVKKQEE 473
Cdd:COG4717 70 LKELKELEEELKEAEEKeeeYAELQEELEEleeELEELEAELEELREELEKLEKLLQLlplyqeleALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 474 RVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLAdlptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAi 553
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLS--------LATEEELQDLAEELEELQQRLAELEEELEEAQE- 220
|
170 180 190
....*....|....*....|....*....|....
gi 966915607 554 crdretQLESLRQREAEFSSAGHSLQDKQSVEET 587
Cdd:COG4717 221 ------ELEELEEELEQLENELEAAALEERLKEA 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
427-586 |
6.15e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 427 QKTEALSREKIDLEKKLSASEVEvqliRESLKvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERE----REELA-------EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 507 ERYLADL-PTLEDHQKQSQQL-----------KDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAE 570
Cdd:PRK02224 320 EDRDEELrDRLEECRVAAQAHneeaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRER 399
|
170
....*....|....*.
gi 966915607 571 FSSAGHSLQDKQSVEE 586
Cdd:PRK02224 400 FGDAPVDLGNAEDFLE 415
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-572 |
7.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 361 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 440
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERV---KGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-PTL 516
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeERI 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966915607 517 EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAIcRDRETQLESLRQREAEFS 572
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT 385
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
421-623 |
1.18e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 421 LRAQFAQKTEALSREKIDLEKKLSASEVEVQLiresLKVALQKHSEEVKKQEERVKGRDkhI-NNLKKKCQKESEQNREk 499
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMSTDALEQEI----LQVSSQLLEKSRQAQQEQDRARE--IsDSLSQLPQQQTEARRQ- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 500 qqrIETLERYLADLPTLEDHQKQSQqLKDSELKSTELQEKVTELEslLEE-----TQAICRDR----------------- 557
Cdd:PRK10929 153 ---LNEIERRLQTLGTPNTPLAQAQ-LTALQAESAALKALVDELE--LAQlsannRQELARLRselakkrsqqldaylqa 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915607 558 -ETQLESLRQREAEfssagHSLQDKQSVEETSGEGPEVEMESWQKQYDsLQKIVEKQQQKMDQLRSQ 623
Cdd:PRK10929 227 lRNQLNSQRQREAE-----RALESTELLAEQSGDLPKSIVAQFKINRE-LSQALNQQAQRMDLIASQ 287
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
317-591 |
1.60e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 317 LELIRLQMEQMQLQNGAicHHPAAFAPslpILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 391
Cdd:pfam15921 564 IEILRQQIENMTQLVGQ--HGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 392 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 460
Cdd:pfam15921 639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 461 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 532
Cdd:pfam15921 719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966915607 533 STELQEKVTELESLLEETQ---AICRD---RETQlESLRQReaefssaghsLQDKQSVEETSGEG 591
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASlqfAECQDiiqRQEQ-ESVRLK----------LQHTLDVKELQGPG 852
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
411-620 |
2.21e-05 |
|
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: 47.86 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 411 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCq 490
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 491 keSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAE 570
Cdd:pfam01576 422 --SESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966915607 571 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQL 620
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAL 543
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
498-611 |
2.59e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 498 EKQQRIETLERYLADLPT----LEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSS 573
Cdd:PRK02224 472 EDRERVEELEAELEDLEEeveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 966915607 574 AGHSLQDK-QSVEETSGEGPEVEMESWQKQ------YDSLQKIVE 611
Cdd:PRK02224 552 EAEEKREAaAEAEEEAEEAREEVAELNSKLaelkerIESLERIRT 596
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-625 |
3.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 487
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 488 KCQKESEQNREKQQRIETLERYLADlptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAiCRDRETQLESLRQR 567
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKAD-----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKK 1330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915607 568 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
410-564 |
3.52e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEErVKGRDKHINNLKKKC 489
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKE-YEALQKEIESLKRRI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966915607 490 QKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDselKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAEL--EAELAELEAELEE---KKAELDEELAELEAELEELEA---EREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-628 |
4.20e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 375 RKHISQLEQKVRESElqvhsallgrpapfgdvclLRLQELQRENTFL-----RAQFAQKTEALSREKIDLEKKLSASEVE 449
Cdd:COG3206 181 EEQLPELRKELEEAE-------------------AALEEFRQKNGLVdlseeAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 450 VQLIRESLKVALQKHSEEVkkqeervkgRDKHINNLKkkcqkeSEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKds 529
Cdd:COG3206 242 LAALRAQLGSGPDALPELL---------QSPVIQQLR------AQLAELEAELAELSARYTPNHPDVIALRAQIAALR-- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 530 ELKSTELQEKVTELESLLEETQAicrdretQLESLRQREAEFSSAGHSLQDKQsveetsgegpeVEMESWQKQYDSLQKI 609
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQA-------REASLQAQLAQLEARLAELPELE-----------AELRRLEREVEVAREL 366
|
250
....*....|....*....
gi 966915607 610 VEKQQQKMDQLRSQVQVAQ 628
Cdd:COG3206 367 YESLLQRLEEARLAEALTV 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
408-625 |
4.42e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGR-------- 478
Cdd:COG3096 428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTARellrryrs 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 479 DKHI----NNLKKKcQKESEQNREKQQRIETLeryLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtQAIC 554
Cdd:COG3096 507 QQALaqrlQQLRAQ-LAELEQRLRQQQNAERL---LEEF-----CQRIGQQLDAAEELEELLAELEAQLEELEEQ-AAEA 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915607 555 RDR----ETQLESLRQREAEFSS---AGHSLQDK-QSVEETSGEgpevemeswqkQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:COG3096 577 VEQrselRQQLEQLRARIKELAArapAWLAAQDAlERLREQSGE-----------ALADSQEVTAAMQQLLEREREATV 644
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
438-619 |
5.00e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.74 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 438 DLEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL- 513
Cdd:cd00176 18 EKEELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 514 ----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEETQAICRD---RETQLESLRQREAEFSSA 574
Cdd:cd00176 96 eerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKKHKELEEEleaHEPRLKSLNELAEELLEE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966915607 575 GHSLQDKQSveetsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQ 619
Cdd:cd00176 176 GHPDADEEI---------EEKLEELNERWEELLELAEERQKKLEE 211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
361-616 |
5.30e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 361 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 439
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 440 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 519
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 520 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSL----QDKQSVEETSGEGPEVE 595
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEERKRKKLELekekRDRKRAEEQRRKILEKE 500
|
250 260
....*....|....*....|....
gi 966915607 596 MESWQK---QYDSLQKIVEKQQQK 616
Cdd:pfam17380 501 LEERKQamiEEERKRKLLEKEMEE 524
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
408-570 |
5.61e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKK 487
Cdd:COG1579 9 LLDLQELDSE----LDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 488 KcQKESEQNRE---KQQRIETLERYLADLptlEDHQKQSQQLKDselkstELQEKVTELESLLEETQA----ICRDRETQ 560
Cdd:COG1579 81 Q-LGNVRNNKEyeaLQKEIESLKRRISDL---EDEILELMERIE------ELEEELAELEAELAELEAeleeKKAELDEE 150
|
170
....*....|
gi 966915607 561 LESLRQREAE 570
Cdd:COG1579 151 LAELEAELEE 160
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-625 |
8.77e-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: 45.83 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 466 EEVKKQEERVKGRDKHINNLKKKCQKESEQ-------NREKQQ--------RIETLERYL----ADLPTLEDHQKQSQQL 526
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKaeryqalLKEKREyegyellkEKEALERQKeaieRQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 527 KD-----------------------SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQs 583
Cdd:TIGR02169 260 ISelekrleeieqlleelnkkikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI- 338
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966915607 584 veetsgEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:TIGR02169 339 ------EELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
430-566 |
1.04e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 430 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 509
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 966915607 510 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
372-625 |
1.26e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 372 DKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQ 451
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 452 lireslkvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQ----SQQL 526
Cdd:pfam07888 140 --------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQrdtqVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 527 KDS----ELKSTELQEKVTELESLLEETQAIcRDR----ETQLESLRqreAEFSSAGhSLQDKQSVE---------ETSG 589
Cdd:pfam07888 212 QDTittlTQKLTTAHRKEAENEALLEELRSL-QERlnasERKVEGLG---EELSSMA-AQRDRTQAElhqarlqaaQLTL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 966915607 590 EGPEVEME------SWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:pfam07888 287 QLADASLAlregraRWAQERETLQQSAEADKDRIEKLSAELQ 328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
408-626 |
1.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQRENTFLRAQFAQKTEALSREkidlEKKLSASEV----EVQLIRESLKVALQKHSEE-----VKKQEERVKGR 478
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKA----EEKKKADELkkaeELKKAEEKKKAEEAKKAEEdknmaLRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 479 DKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTEleslLEETQAICRDRE 558
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK----AEEENKIKAAEE 1666
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915607 559 TQLESLRQREAEfsSAGHSLQDKQSVEETSGEGPEVemeswQKQYDSLQKIVEKQQQKMDQLRSQVQV 626
Cdd:PTZ00121 1667 AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
411-546 |
2.16e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 411 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 490
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 491 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 546
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
434-564 |
2.25e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 434 REKIDLEKKLSASEVEVQLIRESLKVAlqkhseEVKKQEERVKGRDKhINNLKKKCQKESEQNREK--------QQRIET 505
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLEAKEE-IHKLRNEFEKELRERRNElqklekrlLQKEEN 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 966915607 506 LERYLADLptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:PRK12704 98 LDRKLELL------EKREEELEKKEKELEQKQQELEKKEEELEELIE---EQLQELERI 147
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
465-590 |
2.77e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 43.03 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 465 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 544
Cdd:pfam15934 92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 966915607 545 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGE 590
Cdd:pfam15934 169 KLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIE 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-611 |
3.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQRENTFLRAQFAQKTEalsrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINN 484
Cdd:COG4372 37 LFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 485 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicRDRETQLESL 564
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDEL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966915607 565 RqREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVE 611
Cdd:COG4372 189 L-KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-628 |
4.66e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhinnlKKKC 489
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 490 QKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlESLRQREA 569
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---------DAAKKKAE 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 570 EFSSAGHSlqdKQSVEETSGEGPEV-EMESWQKQYDSLQKIVEkQQQKMDQLRSQVQVAQ 628
Cdd:PTZ00121 1389 EKKKADEA---KKKAEEDKKKADELkKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAK 1444
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-628 |
5.36e-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: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 454 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH-QKQSQQLKD---- 528
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEelae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 529 -----------SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEME 597
Cdd:COG4942 109 llralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELEAERAELEALLA 181
|
170 180 190
....*....|....*....|....*....|.
gi 966915607 598 SWQKQYDSLQKIVEKQQQKMDQLRSQVQVAQ 628
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
357-620 |
6.88e-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: 42.79 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 357 LNSNEHLLKEKELLIDKQRKHISQLE---QKVR---ESELQVHSALLGRPAPFGDVCLLrLQELQRENTFLRAQFAQKTE 430
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQfenEKVSlklEEEIQENKDLIKENNATRHLCNL-LKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 431 ALSREKIDL----EKKLSASE---VEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQRI 503
Cdd:pfam05483 180 ETRQVYMDLnnniEKMILAFEelrVQAENARLEMHFKLKEDHEKIQHLEEEYK---KEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 504 ETLERYLADLPTLEDHQKQSQQLKDSELK-STELQEKVT-ELESL-------------LEE-----TQAICR---DRETQ 560
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKeLIEKKDHLTkELEDIkmslqrsmstqkaLEEdlqiaTKTICQlteEKEAQ 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915607 561 LESLRQreaefSSAGHSL--QDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQL 620
Cdd:pfam05483 337 MEELNK-----AKAAHSFvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
406-596 |
7.37e-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: 42.79 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 406 VCLLRLQELQREN-----TFLRAQFAQKTEALsREKIDLE----KKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVK 476
Cdd:pfam05483 242 VSLLLIQITEKENkmkdlTFLLEESRDKANQL-EEKTKLQdenlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 477 GRDKHINNL--KKKCQKEsEQNREKQQRIETLERYLADLPTLEDHQKQSQQ-LKDSE----LKSTELQEKVTELESLLEE 549
Cdd:pfam05483 321 IATKTICQLteEKEAQME-ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrLEKNEdqlkIITMELQKKSSELEEMTKF 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 966915607 550 TQaicrDRETQLESLRQREAEFSSAghsLQDKQSVEETSGE--GPEVEM 596
Cdd:pfam05483 400 KN----NKEVELEELKKILAEDEKL---LDEKKQFEKIAEElkGKEQEL 441
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
413-614 |
8.44e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 413 ELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIREslKVALQKHSEEVKKQEERVKGRDKhinnLKKKCQK- 491
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEAKKKAEEKKKADE----AKKKAEEa 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 492 ----ESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKdselKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:PTZ00121 1444 kkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966915607 568 EAEFSSAGHSLQDKQSVEETSgEGPEVEMESWQKQYDSLQKIVEKQQ 614
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEKKK 1565
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-625 |
9.73e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 355 SILNSNEHLLKEKELL---IDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENTFLRAQFAQKTEA 431
Cdd:TIGR04523 381 SYKQEIKNLESQINDLeskIQNQEKLNQQKDEQIKKLQQE-------------------KELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 432 LSrekiDLEKKLSAsevevqliresLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLA 511
Cdd:TIGR04523 442 IK----DLTNQDSV-----------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 512 DLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREaefssaghslqdKQSVEETSGEG 591
Cdd:TIGR04523 507 EL---------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL------------KKENLEKEIDE 565
|
250 260 270
....*....|....*....|....*....|....
gi 966915607 592 PEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-625 |
9.81e-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: 42.35 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 479 DKHINNLKKKCQKeSEQNREKQQRIETLERYLA--DLPTLEDHQKQSQ--------QLKDSELKSTELQEKVTELESLLE 548
Cdd:TIGR02168 199 ERQLKSLERQAEK-AERYKELKAELRELELALLvlRLEELREELEELQeelkeaeeELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915607 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
428-567 |
1.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 428 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 507
Cdd:PRK12704 48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915607 508 RYLadlptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRD--RETQLESLRQR 567
Cdd:PRK12704 117 KEL------------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
375-586 |
1.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 375 RKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR--LQELQRENTFLRAQFAqkTEALSREKIDLEKK-LSASEVEVQ 451
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRerLEELEEERDDLLAEAG--LDDADAEAVEARREeLEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 452 LIRESLKVALQKHSEEVKKQEERVKGRDkhinnlkkkcqkesEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKDSEL 531
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLE--------------ERAEELREEAAELESELEE--AREAVEDRREEIEELEE 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 966915607 532 KSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDkqSVEE 586
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE--RVEE 444
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
439-625 |
1.40e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 439 LEKKLSAS----EVEVQLIR-ESLKVALQKHSEEVKKQEERVKGRDKHINNlkKKCQKESEQNREKQQRIETLERYLAdl 513
Cdd:COG2433 355 VEKKVPPDvdrdEVKARVIRgLSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVE-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 514 ptledhqkqsqqlkdselkstELQEKVTELESLLEEtqaicrdRETQLESLRQREaefssaghslqdKQSVEEtsgegpE 593
Cdd:COG2433 431 ---------------------ELEAELEEKDERIER-------LERELSEARSEE------------RREIRK------D 464
|
170 180 190
....*....|....*....|....*....|..
gi 966915607 594 VEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
466-623 |
1.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 466 EEVKKQEERVKGRDKH--INNLKKKCQKESEQ----NREKQQRIETLERylADLpTLEDHQKQSQQLKDSELKSTELQEK 539
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHerLNGLESELAELDEEieryEEQREQARETRDE--ADE-VLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 540 VTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQ 619
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
....
gi 966915607 620 LRSQ 623
Cdd:PRK02224 340 HNEE 343
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
494-625 |
1.61e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 494 EQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSE-LKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEF 571
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHeERVEALNELGEQLIEEGhPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915607 572 SSAGHSLQ---DKQSVEETSGEGPEVE-MESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 625
Cdd:cd00176 113 RDADDLEQwleEKEAALASEDLGKDLEsVEELLKKHKELEEELEAHEPRLKSLNELAE 170
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
421-611 |
1.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 421 LRAQFAQKTEALSREKI-DLEKKLSASEVEVQLI----------RESLKVALQKHSEevKKQE-ERVKGRDKHINNLKKK 488
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLnGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEE--RREElETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 489 CQKE----SEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESL 564
Cdd:PRK02224 270 TEREreelAEEVRDLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966915607 565 RQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVE 611
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
364-628 |
1.83e-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: 41.38 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 364 LKEKElliDKQRKHISQLEQKVRE--SELQVHSALLGrpaPFGDVCLLRLQELqrENTFlrAQFAQKTEA---------- 431
Cdd:pfam06160 112 LLESE---EKNREEVEELKDKYRElrKTLLANRFSYG---PAIDELEKQLAEI--EEEF--SQFEELTESgdylearevl 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 432 --LSREKIDLEKKLSA---------SEVEVQL--IRESLKVALQKH--------SEEVKKQEERVKGRDKHINNLKkkCQ 490
Cdd:pfam06160 182 ekLEEETDALEELMEDipplyeelkTELPDQLeeLKEGYREMEEEGyalehlnvDKEIQQLEEQLEENLALLENLE--LD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 491 KESEQNREKQQRI----ETLERYLADLPTLEDHQKQ-SQQLKDSELKSTELQEKVTELES---LLEETQAICRDRETQLE 562
Cdd:pfam06160 260 EAEEALEEIEERIdqlyDLLEKEVDAKKYVEKNLPEiEDYLEHAEEQNKELKEELERVQQsytLNENELERVRGLEKQLE 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915607 563 SLRQREAEfssaghslqDKQSVEEtsGEGPEVEMES-WQKQYDSLQKIvEKQQQKMDQ----LRSQVQVAQ 628
Cdd:pfam06160 340 ELEKRYDE---------IVERLEE--KEVAYSELQEeLEEILEQLEEI-EEEQEEFKEslqsLRKDELEAR 398
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-549 |
1.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 354 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 428
Cdd:PRK03918 541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 429 -----TEALSREKIDLEK---KLSASEVEVQLIRESLKVALQKHSEE---------------VKKQEERVKGRDKHINNL 485
Cdd:PRK03918 613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEeyeelreeylelsreLAGLRAELEELEKRREEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915607 486 KK---KCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselksTELQEKVTELESLLEE 549
Cdd:PRK03918 693 KKtleKLKEELEEREKAKKELEKLEKALERV--------------------EELREKVKKYKALLKE 739
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
472-628 |
2.36e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 472 EERVKGRDKHINNLKKKcqkESEQNREKQQRIETLeryladLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQ 551
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKK---NGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 552 AicrDRETQLESLrQREAEFSSAGHS----LQDKQSVEETSGEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVA 627
Cdd:PHA02562 265 A---KIKSKIEQF-QKVIKMYEKGGVcptcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
.
gi 966915607 628 Q 628
Cdd:PHA02562 340 L 340
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
355-570 |
2.42e-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: 41.10 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 355 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESE--------LQVHSALLGRPAPFGDVC---------LLRLQE--LQ 415
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidikkaTESLEEQLAAAEAEQELEeskretetgIQNLTAeiEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 416 RENTFLRAQFAQKTEALS----REKIDLEKKLSASEVEVQLIRESL---KVALQKHSEEVKKQEERVKGR-DKHINNLKK 487
Cdd:COG5185 348 GQESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLdeiPQNQRGYAQEILATLEDTLKAaDRQIEELQR 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 488 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQ-QLKDSELKST------ELQEKVTELES----LLEETQAICRD 556
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSvrskkeDLNEELTQIESrvstLKATLEKLRAK 507
|
250
....*....|....
gi 966915607 557 RETQLESLRQREAE 570
Cdd:COG5185 508 LERQLEGVRSKLDQ 521
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
412-567 |
3.02e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 412 QELQRENTFLRAQFAQKT---EALSREKIDLEKKLSASEVEVQLIRESLKVAlQKHSEEVKKQEERVKGRDKHINNLKKk 488
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEklmSEIQQENKRLTEPLQKAQEEVEELRKQLENY-EKDKQSLKNLKARLKVLEKELKDLKW- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 489 cqkeseQNREKQQRIETLERylaDLPTLEDHQKQSQQ--LKDSELKSTELQEKVTELESLLEEtqaicrdRETQLESLRQ 566
Cdd:pfam13851 107 ------EHEVLEQRFEKVER---ERDELYDKFEAAIQdvQQKTGLKNLLLEKKLQALGETLEK-------KEAQLNEVLA 170
|
.
gi 966915607 567 R 567
Cdd:pfam13851 171 A 171
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
454-625 |
3.23e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 454 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ---KESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQL 526
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEaisQASRKLRETQNTLNQLNKQIDELNAsiakLEQQQAAQERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 527 KDSELKSTELQEKVTELESLL--EETQAICR----------DRETQLESLRQREAEFSSAGHSLQDKQsveetsgegpev 594
Cdd:PRK11637 126 LAAQLDAAFRQGEHTGLQLILsgEESQRGERilayfgylnqARQETIAELKQTREELAAQKAELEEKQ------------ 193
|
170 180 190
....*....|....*....|....*....|.
gi 966915607 595 emeSWQKQYDSLQKiveKQQQKMDQLRSQVQ 625
Cdd:PRK11637 194 ---SQQKTLLYEQQ---AQQQKLEQARNERK 218
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-549 |
3.23e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 355 SILNSNEH---LLKEKELLIDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENtflraqfaqktEA 431
Cdd:TIGR04523 579 SLKKKQEEkqeLIDQKEKEKKDLIKEIEEKEKKISSLEKE-------------------LEKAKKEN-----------EK 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 432 LSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhINNLKKKCQKESEQNREKqqRIETLERYlA 511
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKELSLHYKK--YITRMIRI-K 704
|
170 180 190
....*....|....*....|....*....|....*...
gi 966915607 512 DLPTLEDHQKQSQQlkdsELKstELQEKVTELESLLEE 549
Cdd:TIGR04523 705 DLPKLEEKYKEIEK----ELK--KLDEFSKELENIIKN 736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
422-623 |
3.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 422 RAQFAQKTEALSREKIDLEKKLSASEVEVQLIREsLKVALQKHsEEVKKQEERVKGRDKHInnlkkkcqkeseqnREKQQ 501
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRL-AEYSWDEIDVASAEREI--------------AELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 502 RIETLERYLADLPTLEdhqkqsQQLKdselkstELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDK 581
Cdd:COG4913 676 ELERLDASSDDLAALE------EQLE-------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 966915607 582 QSVE----------ETSGEGPEVEM-ESWQKQYDSLQKIVEKQQQKMDQLRSQ 623
Cdd:COG4913 743 ARLElralleerfaAALGDAVERELrENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
410-593 |
3.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRENTFLRAQFA---QKTEALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhSEEVKKQEERVKGRdkhINNLK 486
Cdd:COG3883 24 ELSELQAELEAAQAELDalqAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGER---ARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 487 KKCQKESE--------------QNREKQQRI-----ETLERYLADLPTLEDHQKQ-SQQLKDSELKSTELQEKVTELESL 546
Cdd:COG3883 97 RSGGSVSYldvllgsesfsdflDRLSALSKIadadaDLLEELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966915607 547 LEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPE 593
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
497-628 |
4.38e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 497 REKQQRIETLE-------RYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG1196 196 GELERQLEPLErqaekaeRYRELKEELKELEAELLLLKLRELEAelEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915607 568 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVAQ 628
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
410-567 |
4.91e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 39.62 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 410 RLQELQRENTFLRAQFAQkteaLSREKIDLEKKlsasevEVQLIR---ESLKVA----------LQKHSEEVKKQEERVK 476
Cdd:pfam04849 172 KLRGLEEENLKLRSEASH----LKTETDTYEEK------EQQLMSdcvEQLSEAnqqmaelseeLARKMEENLRQQEEIT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 477 GRDKHINNLKKKCQKESEQNREKQQRIETleryladlptledhQKQSQQLKDSELKstELQEKVTELESLLEETQaicrd 556
Cdd:pfam04849 242 SLLAQIVDLQHKCKELGIENEELQQHLQA--------------SKEAQRQLTSELQ--ELQDRYAECLGMLHEAQ----- 300
|
170
....*....|.
gi 966915607 557 reTQLESLRQR 567
Cdd:pfam04849 301 --EELKELRKK 309
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
408-569 |
4.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQRENTFLRAQFAQKTEALSREKID-----LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE-RVKGRDKH 481
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 482 INNLKKKCQKESE-----------QNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEET 550
Cdd:COG4717 372 IAALLAEAGVEDEeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
170
....*....|....*....
gi 966915607 551 QAICRDRETQLESLRQREA 569
Cdd:COG4717 452 REELAELEAELEQLEEDGE 470
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-626 |
4.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 422 RAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVA--LQKHSEEVKKQEERVKGRD--KHINNLKKKCQkES 493
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK--AEEKkkadEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAE-EA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 494 EQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE-------LKSTELQEKVTELESLLEETQAICRDRETQL----- 561
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkadeAKKAEEAKKADEAKKAEEKKKADELKKAEELkkaee 1562
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915607 562 ----ESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQV 626
Cdd:PTZ00121 1563 kkkaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
408-586 |
5.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLS----ASEVEVQLIRESLKVALQKHSEeVKKQEERVKGRDKHIN 483
Cdd:PRK03918 548 LEKLEELKKK----LAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELK 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 484 NLKKKCQKESEQNREKQQRIETLERYLADLPTL---EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQ 560
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
170 180
....*....|....*....|....*.
gi 966915607 561 LESLRQREAEFSSAGHSLQDKQSVEE 586
Cdd:PRK03918 703 LEEREKAKKELEKLEKALERVEELRE 728
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
412-616 |
5.47e-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: 39.95 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 412 QELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKH---SEEVKKQEERVKgRDKHINNLKKK 488
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLK-KQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 489 CQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlesLRQRE 568
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-----------HVKQQ 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966915607 569 AEFSSAGHSLQDKQSVEETSGEGPEVEM---ESWQKQYDSLQKIVEKQQQK 616
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATsirEISCQQHTLTQHIHTLQQQK 388
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
365-627 |
8.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 365 KEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLE---K 441
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 442 KLSASEVEVQLIRE---SLKVALQKHSEEVKKQEERVKGRDKHINNLKK----------KCQKESEQNREK----QQRIE 504
Cdd:PRK02224 350 DADDLEERAEELREeaaELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREErdelREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915607 505 TLErylADLPTLEDHQKQSQQL-------------KDSELKST--ELQEKVTELESLL---EETQAICRDRETQLESLRQ 566
Cdd:PRK02224 430 ELE---ATLRTARERVEEAEALleagkcpecgqpvEGSPHVETieEDRERVEELEAELedlEEEVEEVEERLERAEDLVE 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915607 567 REAEFSsaghSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQVA 627
Cdd:PRK02224 507 AEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
|
| |
