|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
431-663 |
1.19e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLN---EFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEkyladl 507
Cdd:COG1196 249 EELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 508 ptlddvqsqsLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLp 587
Cdd:COG1196 323 ----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA- 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046876272 588 MLDAKQLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEESLQRLTEALLE 663
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
431-647 |
5.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLNEfLKQRISQfseekkkLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTL 510
Cdd:PRK03918 217 PELREELEKLEKEVKELEE-LKEEIEE-------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 511 DDVQSQSLQLQVLEEKNK----NLQETLIDTEKKLEEIKKQCQD---KEVQLLCQKKKEKELVTSVQSLQQKVEKcledg 583
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLdelrEIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHEL----- 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 584 irLPMLDAKQLQSENDSLREQNATASKI------IESQQDEINRMILEIQSMQGKLCKEKLSARSTVEEL 647
Cdd:PRK03918 364 --YEEAKAKKEELERLKKRLTGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
429-663 |
5.01e-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: 53.52 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 429 HQEELEQKLASTEKEVLQLNEFLKQRISQFSeekkkleeklkTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYL---- 504
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSELEEEIEELQKELYALANEISRLEQQKqilr 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 505 ADLPTLDDVQSQ-SLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcLEDG 583
Cdd:TIGR02168 309 ERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 584 IRLPMLDAKQLQSENDSLREQnataskiIESQQDEINRMILEIQSMQGKLCKEKLSA-RSTVEELGRKEESLQRLTEALL 662
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEAR-------LERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLE 460
|
.
gi 1046876272 663 E 663
Cdd:TIGR02168 461 E 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
431-663 |
1.03e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEV---LQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADL 507
Cdd:TIGR02168 687 EELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 508 ptLDDVQSQSLQLQVLEEKNKNLQEtlidtekKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcLEDGIRLP 587
Cdd:TIGR02168 767 --EERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 588 MLDAKQLQSENDSLREQNATASKIIESQQDEINRMILEIQ-------SMQGKLCKEKLSARSTVEELGRKEESLQRLTEA 660
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSEELRELESKRSELRRE 916
|
...
gi 1046876272 661 LLE 663
Cdd:TIGR02168 917 LEE 919
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-663 |
1.47e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 489 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTS 568
Cdd:COG1196 219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 569 VQSLQQKVEKCLEDGIRLPmLDAKQLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELG 648
Cdd:COG1196 297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170
....*....|....*
gi 1046876272 649 RKEESLQRLTEALLE 663
Cdd:COG1196 376 EAEEELEELAEELLE 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
531-663 |
7.47e-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: 48.99 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 531 QETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcLEDGIRLPMLDAKQLQSENDSLREQNATASK 610
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1046876272 611 IIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEESLQRLTEALLE 663
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE 150
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
431-663 |
1.92e-05 |
|
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: 48.48 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLNeflkQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPT- 509
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLN----EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESk 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 510 LDDVQSQSLQLQ-----------VLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLlcqkkkeKELVTSVQSLQQKVEK 578
Cdd:TIGR04523 400 IQNQEKLNQQKDeqikklqqekeLLEKEIERLKETIIKNNSEIKDLTNQDSVKELII-------KNLDNTRESLETQLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 579 cLEDGIRLPMLDAKQLQ-------SENDSLREQNatasKIIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKE 651
Cdd:TIGR04523 473 -LSRSINKIKQNLEQKQkelkskeKELKKLNEEK----KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
250
....*....|...
gi 1046876272 652 ESL-QRLTEALLE 663
Cdd:TIGR04523 548 NKDdFELKKENLE 560
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
431-667 |
2.57e-05 |
|
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: 47.64 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQ-LNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQ-KESEQNKEKQRRIETLEKYLADLP 508
Cdd:COG5185 263 TDLRLEKLGENAESSKrLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQlAAAEAEQELEESKRETETGIQNLT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 509 TlDDVQSQSLQLQVLEEKNKNLQEtlIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLPM 588
Cdd:COG5185 343 A-EIEQGQESLTENLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 589 LDAKQLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGKLCKEKLS--ARSTVEELGRKEESLQRLTEALLEVSS 666
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDeiNRSVRSKKEDLNEELTQIESRVSTLKA 499
|
.
gi 1046876272 667 S 667
Cdd:COG5185 500 T 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
430-661 |
2.89e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 430 QEELEQKLASTEKEVLQLNEFLKQRISQfseeKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKyladlpt 509
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 510 lddvqsqslQLQVLEEKNKNLQETLidtEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLpML 589
Cdd:COG4942 91 ---------EIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046876272 590 DAKQLQSENDSLREQNATASKIIESQQDEINRMILEI---QSMQGKLCKEKLSARSTVEELGRKEESLQRLTEAL 661
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKaerQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
424-633 |
3.71e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.33 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 424 PLSHPHQEELEQKLASTEKEVLQLNEflkqrisQFSEEKKKLEEKLKTRDRYISSLKK---KCQKESEQNKEKQRRIEtL 500
Cdd:pfam05667 317 SSPPTKVETEEELQQQREEELEELQE-------QLEDLESSIQELEKEIKKLESSIKQveeELEELKEQNEELEKQYK-V 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 501 EKYLADLptLDDVQSQSLQLQ-VLEEKNKNLQE----------TLIdteKKLEEIKKQCQDKEVQllCQKKKEKelvtsV 569
Cdd:pfam05667 389 KKKTLDL--LPDAEENIAKLQaLVDASAQRLVElagqwekhrvPLI---EEYRALKEAKSNKEDE--SQRKLEE-----I 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 570 QSLQQKVEKCLEDgIRLPMLDAKQLQSENDSLREQ---NATASKIIES------QQDEINRMIL-------EIQSMQGKL 633
Cdd:pfam05667 457 KELREKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRILEIvknikkQKEEITKILSdtkslqkEINSLTGKL 535
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
350-604 |
1.20e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 350 ESVLKIKEGLLRQKEIVIDRQKQQINHLHERIRDneLRAQHAMLGHYVNCEDSYMSSLQPQYESSSGQTPFTEQPLshph 429
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL---- 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 430 qEELEQKLASTEKEVLQLNEFLKQrisqfseekkkLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKylaDLPT 509
Cdd:TIGR04523 485 -EQKQKELKSKEKELKKLNEEKKE-----------LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---ELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 510 LDDVQSQSLQLQVLEEKNKNL------QETLIDTEKKLEEIKKQCQDKEVQLlcqKKKEKELVTSVQSLQQKVEKCLEDG 583
Cdd:TIGR04523 550 DDFELKKENLEKEIDEKNKEIeelkqtQKSLKKKQEEKQELIDQKEKEKKDL---IKEIEEKEKKISSLEKELEKAKKEN 626
|
250 260
....*....|....*....|.
gi 1046876272 584 IRLpMLDAKQLQSENDSLREQ 604
Cdd:TIGR04523 627 EKL-SSIIKNIKSKKNKLKQE 646
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
303-652 |
1.95e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 303 EDSYSLAPWQQpQTEEFQQGSETPMQVLTGSSRQTYSPPGFQDFSKWESVLKIKEGLLRQKEIVIDRQKQQINHLHERIR 382
Cdd:TIGR00618 342 EQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 383 DneLRAQHAMLGHYVNCEDSYMSSLQpqyesSSGQTPFTEQPLSHPHQEELEQKLASTEKEVLQLNEFLKQrisqfseek 462
Cdd:TIGR00618 421 D--LQGQLAHAKKQQELQQRYAELCA-----AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ--------- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 463 kkleeklKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDdvqsqSLQLQVLEEKNKNLQETLIDTEKKLE 542
Cdd:TIGR00618 485 -------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL-----TRRMQRGEQTYAQLETSEEDVYHQLT 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 543 EIKKQCQDkevqllcQKKKEKELVTSVQSLQQKVE--KCLEDGIRLPMLDAKQLQSENDSLREQNATASKIIESQ-QDEI 619
Cdd:TIGR00618 553 SERKQRAS-------LKEQMQEIQQSFSILTQCDNrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKlQPEQ 625
|
330 340 350
....*....|....*....|....*....|....*
gi 1046876272 620 N--RMILEIQSMQGKLCKEKLSARSTVEELGRKEE 652
Cdd:TIGR00618 626 DlqDVRLHLQQCSQELALKLTALHALQLTLTQERV 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
431-666 |
1.96e-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: 45.06 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLNEFLKQRisqfseekkklEEKLKTRDRYISSLKKKCQKESEqnkEKQRRI-ETLEKYLADLPT 509
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-----------EKRLEEIEQLLEELNKKIKDLGE---EEQLRVkEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 510 LDDVQSQS-LQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKevqllcQKKKEKeLVTSVQSLQQKVEKCLEdgirlpm 588
Cdd:TIGR02169 306 LERSIAEKeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEE------RKRRDK-LTEEYAELKEELEDLRA------- 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046876272 589 lDAKQLQSENDSLREQNATASKIIESQQDEINrmilEIQSMQGKLCKEKLSARSTVEELgrkEESLQRLTEALLEVSS 666
Cdd:TIGR02169 372 -ELEEVDKEFAETRDELKDYREKLEKLKREIN----ELKRELDRLQEELQRLSEELADL---NAAIAGIEAKINELEE 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-653 |
2.31e-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: 45.06 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 344 QDFSKWESVLKIKEGLLRQKEIVIDRQKQQINHLHERIRD-----NELRAQ----HAMLGH-YVNCEDSYMSSLQPQYES 413
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEleedlHKLEEAlndlEARLSHsRIPEIQAELSKLEEEVSR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 414 SSGQTPFTEQPLSHPHQEEleQKLASTEKEVLQLNEFLKQRISQfseekkkleeklktRDRYISSLKKKCQKESEQNKEK 493
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEK--EYLEKEIQELQEQRIDLKEQIKS--------------IEKEIENLNGKKEELEEELEEL 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 494 QRRIETLEKYLADlptlddvqsqslqlqvLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQ 573
Cdd:TIGR02169 874 EAALRDLESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 574 QKVEKCLEDGIRLPMLD--AKQLQSENDSLREQNATASKIIEsQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKE 651
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQ-EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
..
gi 1046876272 652 ES 653
Cdd:TIGR02169 1017 RE 1018
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
431-669 |
2.86e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLNEFLKQRISQFSEEKKKleeklktrdryISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtl 510
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELL-----------LSNLKKKIQK----NKSLESQISELKKQNNQLK-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 511 DDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcledgirlpmLD 590
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD----------LN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 591 AKQLQSENDSLREQNATASK---IIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEESLQRLTEALLEVSSS 667
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKkleEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
..
gi 1046876272 668 SK 669
Cdd:TIGR04523 382 YK 383
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
436-663 |
3.33e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 436 KLASTEKEVLQLNEFLKQRISQFSEEKKKLeeklktrDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQS 515
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDRESDRNQELQKRIRLLEKREAE-------AE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 516 QSLQLQVleEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLedgirlpmLDAKQLQ 595
Cdd:pfam05557 69 EALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTN--------SELEELQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046876272 596 SENDSLREQNATASKII---ESQQDEINRMILEIQSMQGKLCKE---KLSARSTVEELGRKEEsLQRLTEALLE 663
Cdd:pfam05557 139 ERLDLLKAKASEAEQLRqnlEKQQSSLAEAEQRIKELEFEIQSQeqdSEIVKNSKSELARIPE-LEKELERLRE 211
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
360-622 |
5.73e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 360 LRQKEIVIDRQKQQINHLHERIRDNELRAQHAmlghyvncedsymsslqpqyesssgqtpfTEQplshphQEELEQKLAS 439
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEEL-----------------------------EEE------LAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 440 TEKEVLQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQ 519
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 520 LQV-LEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKvekcledgirlpmldAKQLQSEN 598
Cdd:COG1196 415 RLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE---------------AALLEAAL 479
|
250 260
....*....|....*....|....
gi 1046876272 599 DSLREQNATASKIIESQQDEINRM 622
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADY 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
432-578 |
7.01e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 432 ELEQKLASTEKEVLQLNEFLKQRISQFSEEKKKleeklktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 511
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTE-----------LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046876272 512 DVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLlcqKKKEKELVTSVQSLQQKVEK 578
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAE 153
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
478-630 |
1.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 478 SLKKKcqKESEQNKEKQRRIETLEKyladlptldDVQSQSLQLQVLEEKNKNLQETLidtEKKLEEIKKQCQ--DKEVQL 555
Cdd:PRK12704 53 AIKKE--ALLEAKEEIHKLRNEFEK---------ELRERRNELQKLEKRLLQKEENL---DRKLELLEKREEelEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 556 LCQKKKE-KELVTSVQSLQQKVEKCLEDGIRLPMLDAKQL---QSENDSLREQNATASKIIESQQDEIN---RMILeIQS 628
Cdd:PRK12704 119 LEQKQQElEKKEEELEELIEEQLQELERISGLTAEEAKEIlleKVEEEARHEAAVLIKEIEEEAKEEADkkaKEIL-AQA 197
|
..
gi 1046876272 629 MQ 630
Cdd:PRK12704 198 IQ 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
473-641 |
1.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 473 DRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKE 552
Cdd:COG4717 88 EEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 553 VQLLCQKKKEKELVTSVQSLQQKVEKCLEDgirlpmldakqLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGK 632
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQD-----------LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
....*....
gi 1046876272 633 LCKEKLSAR 641
Cdd:COG4717 236 LEAAALEER 244
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
489-637 |
1.21e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.66 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 489 QNKEKQRRIETLEKYLADLPTLddVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLlcqKKKEK----- 563
Cdd:pfam15619 40 LQKRQEKALGKYEGTESELPQL--IARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQL---KRLEKlsedk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 564 ------ELVTSVQSLQQKVEKCLEDGIRLpmldAKQLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGKLcKEK 637
Cdd:pfam15619 115 nlaereELQKKLEQLEAKLEDKDEKIQDL----ERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKL-KEK 189
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
491-698 |
1.39e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 491 KEKQRRIE-TLEKYL-ADLPTLDDVQSQSLQlQVLEEknknLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKE-----K 563
Cdd:COG2433 349 KNKFERVEkKVPPDVdRDEVKARVIRGLSIE-EALEE----LIEKELPEEEPEAEREKEHEERELTEEEEEIRRleeqvE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 564 ELVTSVQSLQQKVEKcLEDGIrlpmldaKQLQSENDSLREQnaTASKIIESQqdEINRMILEIQSMQGKLCKEklsaRST 643
Cdd:COG2433 424 RLEAEVEELEAELEE-KDERI-------ERLERELSEARSE--ERREIRKDR--EISRLDREIERLERELEEE----RER 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1046876272 644 VEELGRKeesLQRLTEALLEVSSSSKYpqrespPLKVNACFVHENQRHMGETYSL 698
Cdd:COG2433 488 IEELKRK---LERLKELWKLEHSGELV------PVKVVEKFTKEAIRRLEEEYGL 533
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
431-621 |
1.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLNEFLKQRISQFSEekkkleeklkTRDRyISSLKKKCQKESEQNKEKQRRI----ETLEKYLAD 506
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNE----------LQAE-LEALQAEIDKLQAEIAEAEAEIeerrEELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 507 L----------------PTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQ 570
Cdd:COG3883 95 LyrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1046876272 571 SLQQKVEKCLEdgirlpmldakQLQSENDSLREQNATASKIIESQQDEINR 621
Cdd:COG3883 175 AQQAEQEALLA-----------QLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
430-663 |
1.90e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 430 QEELEQKLASTEKEVLQLNEFLKQRI-SQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLP 508
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKkALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 509 TLDDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQL------------LCQKKKEKELV-TSVQSLQQK 575
Cdd:pfam02463 262 KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeeklkeseKEKKKAEKELKkEKEEIEELE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 576 VEKCLEDGIRLPMLDAKQLQS---ENDSLREQNATASKIIESQQdEINRMILEIQSMQGKLcKEKLSARSTVEELGRKEE 652
Cdd:pfam02463 342 KELKELEIKREAEEEEEEELEklqEKLEQLEEELLAKKKLESER-LSSAAKLKEEELELKS-EEEKEAQLLLELARQLED 419
|
250
....*....|.
gi 1046876272 653 SLQRLTEALLE 663
Cdd:pfam02463 420 LLKEEKKEELE 430
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
430-674 |
2.86e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 430 QEELEQKLASTEKEVLQLNEFLKqrISQFSEEKKKLEEK-LKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKY--LAD 506
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEEEAA--GSRLKRKKKEALKKlIEETENLAELIIDLEELKLQELKLKEQAKKALEYYqlKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 507 LPTLDDVQSQSLQLQVLEEKNKNLQEtLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRL 586
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQE-LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 587 PMLDAKQLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQgklcKEKLSARSTVEELGRKEESLQRLTEALLEVSS 666
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE----KELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
....*...
gi 1046876272 667 SSKYPQRE 674
Cdd:pfam02463 374 ELLAKKKL 381
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
491-664 |
2.88e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 491 KEKQRRIET---LEKYLADLPTLDDVqsqslqlqvLEEKNKNLQETLIDTEK--KLEEIKKQCQDKEVQLLCQKKKE--K 563
Cdd:TIGR02168 169 KYKERRKETerkLERTRENLDRLEDI---------LNELERQLKSLERQAEKaeRYKELKAELRELELALLVLRLEElrE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 564 ELVTSVQSLQQKVEKCLEDGIRLPMLDAK--QLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGKLCKEKLSAR 641
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180
....*....|....*....|...
gi 1046876272 642 STVEELGRKEESLQRLTEALLEV 664
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAEL 342
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
431-666 |
5.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 431 EELEQKLASTEKEVLQLNEFLKQRISQFSEEKkkleeklktrdRYISSLKKKCQKESEQNKEKQRRIETLEkyladlptl 510
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLE-----------EELEELNEQLQAAQAELAQAQEELESLQ--------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 511 DDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLlcqkkkeKELVTSVQSLQQKVEKCLEDGIRLPMLD 590
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL-------KELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046876272 591 AKQLQSENDSLREQNATASKIIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEESLQRLTEALLEVSS 666
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
519-690 |
5.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 519 QLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEdgirlpmlDAKQLQSEN 598
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA--------ELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 599 DSLREQNATASKIIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEESLQRLTEALLEVSSSSKYPQRESPPL 678
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170
....*....|..
gi 1046876272 679 KVNACFVHENQR 690
Cdd:COG4372 184 ALDELLKEANRN 195
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-594 |
7.14e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 350 ESVLKIKEGLLRQKEIVIDRQKQQINHLHERIRD-----NELRAQHAMLGHYVNCEDSYMSSLQPQYESSSGQTPFTEQp 424
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 425 lshpHQEELEQKLASTEKEVLQLN---EFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLE 501
Cdd:TIGR02168 331 ----KLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 502 KYLADL-----------------PTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKKLEEIKKQCQDKEVQLLCQKKKEKE 564
Cdd:TIGR02168 407 ARLERLedrrerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250 260 270
....*....|....*....|....*....|...
gi 1046876272 565 L---VTSVQSLQQKVEKcLEDGIRLPMLDAKQL 594
Cdd:TIGR02168 487 LqarLDSLERLQENLEG-FSEGVKALLKNQSGL 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-663 |
7.46e-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: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 519 QLQVLEEKNKNLQETLIDTEKKLEEIKKQCQD-KEVQLLCQKKKE--------KELVTSVQSLQQKVEKCLEDGIRLPML 589
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAlQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046876272 590 DA--KQLQSENDSLREQNATASKIIESQQDEINRMILEIQSmqgklCKEKLSARSTVEELGRKEESLQRLTEALLE 663
Cdd:COG4913 691 EEqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-----LQDRLEAAEDLARLELRALLEERFAAALGD 761
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
433-661 |
8.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 433 LEQKLASTEKEVLQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKkkcqKESEQNKEKQRRIetleKYLADLPTLDD 512
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAR----ADLEDIKIKINEL----KDKHDKYEEIK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 513 VQSQSLQLQVLEEK-----NKNLQETLIDTE---KKLEEIKKQCQDKEVQLlcqkkKEKEL-VTSVQSLQQKVEKCLEDG 583
Cdd:PRK01156 553 NRYKSLKLEDLDSKrtswlNALAVISLIDIEtnrSRSNEIKKQLNDLESRL-----QEIEIgFPDDKSYIDKSIREIENE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 584 IRL-----PMLDAKQLQSEN-----DSLREQNATASKIIESQQdEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEES 653
Cdd:PRK01156 628 ANNlnnkyNEIQENKILIEKlrgkiDNYKKQIAEIDSIIPDLK-EITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
....*...
gi 1046876272 654 LQRLTEAL 661
Cdd:PRK01156 707 LRTRINEL 714
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
354-655 |
8.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 354 KIKEGLLRQKEIVIDRQKQ--QINHLHERIRDNELRAQHamLGHYVNCEDSYMSSLQPQYESSSGQTPFTEQPLSHPHQE 431
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEisNIDYLEEKLKSSNLELEN--IKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 432 EleQKLASTEKEVLQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 511
Cdd:PRK01156 241 L--NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046876272 512 DvqsqslQLQVLEEKNKNLQETLIDTEKkLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLPMLDA 591
Cdd:PRK01156 319 A------EINKYHAIIKKLSVLQKDYND-YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046876272 592 KQlqseNDSLREQNATASkIIESQQDEINRMILEIQSMQGKLCKEKLSARSTVEELGRKEESLQ 655
Cdd:PRK01156 392 FI----SEILKIQEIDPD-AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
|
| |
