|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
443-697 |
1.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLN---EFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEkyladl 519
Cdd:COG1196 249 EELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 520 ptlddvqsqsLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLp 599
Cdd:COG1196 323 ----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 600 MLDAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKEGSLQRLTEALLENQRQ 679
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|....*...
gi 326368265 680 MGETYSLLDQGHEAEQSR 697
Cdd:COG1196 472 AALLEAALAELLEELAEA 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
443-792 |
5.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLNEfLKQRISQfseekkkLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTL 522
Cdd:PRK03918 217 PELREELEKLEKEVKELEE-LKEEIEE-------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 523 DDVQSQSLQLQVLEEKNK----NLQETLIDTEKQLEEIKKQCQD---KEVQLLCQKKKEKELVTSVQSLQQKVEKcLEdg 595
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLdelrEIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHEL-YE-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 596 irlpmlDAKQLQSENDNLREQNATASKiiesqqDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKEGSLQRLTEALLE 675
Cdd:PRK03918 366 ------EAKAKKEELERLKKRLTGLTP------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 676 NQRQMGETYSLLDQGHEAEQSRPQTIHSKWPLFDLTVIDQLFKEMsycLFDLKALCSILNqraqgKEPNLSLLLGIRSMN 755
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL---RKELRELEKVLK-----KESELIKLKELAEQL 505
|
330 340 350
....*....|....*....|....*....|....*..
gi 326368265 756 CSAEETENDHSPETLTKKLSDVCQLRRDIDELRTTIS 792
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
443-695 |
5.67e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEV---LQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADL 519
Cdd:TIGR02168 687 EELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 520 ptLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLlcqkKKEKELVTSVQSLQQKVEKCLEDGIRLp 599
Cdd:TIGR02168 767 --EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERR- 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 600 mldAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKEGSLQRLTEALLENQRQ 679
Cdd:TIGR02168 840 ---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250
....*....|....*.
gi 326368265 680 MGETYSLLDQGHEAEQ 695
Cdd:TIGR02168 917 LEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-697 |
1.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 501 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTS 580
Cdd:COG1196 219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 581 VQSLQQKVEKCLEDGIRLPmLDAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELG 660
Cdd:COG1196 297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190
....*....|....*....|....*....|....*..
gi 326368265 661 RKEGSLQRLTEALLENQRQMGETYSLLDQGHEAEQSR 697
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
441-689 |
2.21e-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: 54.68 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 441 HQEELEQKLASTEKEVLQLNEFLKQRISQFSeekkkleeklkTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYL---- 516
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSELEEEIEELQKELYALANEISRLEQQKqilr 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 517 ADLPTLDDVQSQ-SLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcLEDG 595
Cdd:TIGR02168 309 ERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 596 IRLPMLDAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKLTAR-----STVEELGRKEGSLQRLT 670
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeeleELQEELERLEEALEELR 467
|
250
....*....|....*....
gi 326368265 671 EALLENQRQMGETYSLLDQ 689
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQ 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
543-689 |
1.72e-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: 50.92 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 543 QETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcLEDGIRLPMLDAKQLQSENDNLREQNATASK 622
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326368265 623 IIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKEGSLQRLTEALLENQRQMGETYSLLDQ 689
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
443-679 |
1.99e-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: 48.09 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLNeflkQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPT- 521
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLN----EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESk 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 522 LDDVQSQSLQLQ-----------VLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLlcqkkkeKELVTSVQSLQQKVEK 590
Cdd:TIGR04523 400 IQNQEKLNQQKDeqikklqqekeLLEKEIERLKETIIKNNSEIKDLTNQDSVKELII-------KNLDNTRESLETQLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 591 cLEDGIRLPMLDAKQLQ-------SENDNLREQNatasKIIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKE 663
Cdd:TIGR04523 473 -LSRSINKIKQNLEQKQkelkskeKELKKLNEEK----KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
250
....*....|....*..
gi 326368265 664 GSL-QRLTEALLENQRQ 679
Cdd:TIGR04523 548 NKDdFELKKENLEKEID 564
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
443-715 |
2.42e-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: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQ-LNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQ-KESEQNKEKQRRIETLEKYLADLP 520
Cdd:COG5185 263 TDLRLEKLGENAESSKrLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQlAAAEAEQELEESKRETETGIQNLT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 521 TlDDVQSQSLQLQVLEEKNKNLQEtlIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLPM 600
Cdd:COG5185 343 A-EIEQGQESLTENLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 601 LDAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKL--TARSTVEELGRKEGSLQRLTEALLENQR 678
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYdeINRSVRSKKEDLNEELTQIESRVSTLKA 499
|
250 260 270
....*....|....*....|....*....|....*..
gi 326368265 679 QMGEtysLLDQGHEAEQSRPQTIHSKWPLFDLTVIDQ 715
Cdd:COG5185 500 TLEK---LRAKLERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-700 |
2.50e-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: 47.45 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 442 QEELEQKLASTEKEVLQLNEFLKQRISQfseeKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKyladlpt 521
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 522 lddvqsqslQLQVLEEKNKNLQETLidtEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEdgirlpml 601
Cdd:COG4942 91 ---------EIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 602 DAKQLQSENDNLREQNATaskiIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKEGSLQRLTEALLENQRQMG 681
Cdd:COG4942 151 QAEELRADLAELAALRAE----LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*....
gi 326368265 682 ETYSLLDQGHEAEQSRPQT 700
Cdd:COG4942 227 ALIARLEAEAAAAAERTPA 245
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
436-645 |
9.37e-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: 45.79 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 436 PLSHPHQEELEQKLASTEKEVLQLNEflkqrisQFSEEKKKLEEKLKTRDRYISSLKK---KCQKESEQNKEKQRRIEtL 512
Cdd:pfam05667 317 SSPPTKVETEEELQQQREEELEELQE-------QLEDLESSIQELEKEIKKLESSIKQveeELEELKEQNEELEKQYK-V 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 513 EKYLADLptLDDVQSQSLQLQ-VLEEKNKNLQE----------TLIdteKQLEEIKKQCQDKEVQllCQKKKEKelvtsV 581
Cdd:pfam05667 389 KKKTLDL--LPDAEENIAKLQaLVDASAQRLVElagqwekhrvPLI---EEYRALKEAKSNKEDE--SQRKLEE-----I 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 582 QSLQQKVEKCLEDgIRLPMLDAKQLQSENDNLREQ---NATASKIIES------QQDEINRMIL-------EIQSMQGKL 645
Cdd:pfam05667 457 KELREKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRILEIvknikkQKEEITKILSdtkslqkEINSLTGKL 535
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
443-657 |
1.00e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKE------------KQRRIE 510
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdklllenKELTQE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 511 TLEKYLADLPTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEK 590
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326368265 591 C----------LEDGIRLPMLDAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKLTARSTVE 657
Cdd:pfam05483 588 QmkilenkcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
319-708 |
1.01e-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: 46.12 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 319 SLAPWQQpQTEEFQQGSETPMQVLTGSSRQSYSPPGFQDFSKWESVLKIKEGLLRQKEIVIDRQKQQINHLHERIRDneL 398
Cdd:TIGR00618 346 LLQTLHS-QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD--L 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 399 RAQHAMLGHYVNCEDSYVSNLQpqyesSSGQSLFTEQPLSHPHQEELEQKLASTEKEVLQLNEFLKQrisqfseekkkle 478
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCA-----AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ------------- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 479 eklKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDdvqsqSLQLQVLEEKNKNLQETLIDTEKQLEEIKK 558
Cdd:TIGR00618 485 ---ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL-----TRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 559 QCQDkevqllcQKKKEKELVTSVQSLQQKVE--KCLEDGIRLPMLDAKQLQSENDNLREQNATASKIIESQ-QDEIN--R 633
Cdd:TIGR00618 557 QRAS-------LKEQMQEIQQSFSILTQCDNrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKlQPEQDlqD 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 634 MILEIQSMQGKLCEEKLTARSTVEELG----RKEGSLQRLTEALLENQRQMGETY------------SLLDQGHEAEQSR 697
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTqervREHALSIRVLPKELLASRQLALQKmqsekeqltywkEMLAQCQTLLREL 709
|
410
....*....|.
gi 326368265 698 PQTIHSKWPLF 708
Cdd:TIGR00618 710 ETHIEEYDREF 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
443-695 |
1.03e-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: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLNEFLKQRISQFSEEKKKleeklktrdryISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtl 522
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELL-----------LSNLKKKIQK----NKSLESQISELKKQNNQLK-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 523 DDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcledgirlpmLD 602
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD----------LN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 603 AKQLQSENDNLREQNATASK---IIESQQDEINRMILEIQSMQGKLCEEKLTARST----VEELGRKEGSLQRLTEallE 675
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKkleEIQNQISQNNKIISQLNEQISQLKKELTNSESEnsekQRELEEKQNEIEKLKK---E 378
|
250 260
....*....|....*....|
gi 326368265 676 NQRQMGETYSLLDQGHEAEQ 695
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLES 398
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
362-635 |
2.78e-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: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 362 ESVLKIKEGLLRQKEIVIDRQKQQINHLHERIRDneLRAQHAMLGHYVNCEDSYVSNLQPQYESSSGQSLFTEQPLshph 441
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL---- 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 442 qEELEQKLASTEKEVLQLNEFLKQrisqfseekkkLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKylaDLPT 521
Cdd:TIGR04523 485 -EQKQKELKSKEKELKKLNEEKKE-----------LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---ELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 522 LDDVQSQSLQLQVLEEKNKNL------QETLIDTEKQLEEIKKQCQDKEVQLlcqKKKEKELVTSVQSLQQKVEKCLEDG 595
Cdd:TIGR04523 550 DDFELKKENLEKEIDEKNKEIeelkqtQKSLKKKQEEKQELIDQKEKEKKDL---IKEIEEKEKKISSLEKELEKAKKEN 626
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 326368265 596 irlpmldaKQLQSENDNLREQNATASKIIESQQDEINRMI 635
Cdd:TIGR04523 627 --------EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-671 |
3.78e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLNEFLKQRisqfseekkklEEKLKTRDRYISSLKKKCQKESEqnkEKQRRI-ETLEKYLADLPT 521
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-----------EKRLEEIEQLLEELNKKIKDLGE---EEQLRVkEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 522 LDDVQSQS-LQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKevqllcQKKKEKeLVTSVQSLQQKVEKCLEdgirlpm 600
Cdd:TIGR02169 306 LERSIAEKeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEE------RKRRDK-LTEEYAELKEELEDLRA------- 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326368265 601 lDAKQLQSENDNLREQNATASKIIESQQDEINrmilEIQSMQGKLCEEKLTARSTVEELGRK-EGSLQRLTE 671
Cdd:TIGR02169 372 -ELEEVDKEFAETRDELKDYREKLEKLKREIN----ELKRELDRLQEELQRLSEELADLNAAiAGIEAKINE 438
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
444-590 |
6.42e-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: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 444 ELEQKLASTEKEVLQLNEFLKQRISQFSEEKKKleeklktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 523
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTE-----------LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326368265 524 DVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLlcqKKKEKELVTSVQSLQQKVEK 590
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAE 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-696 |
7.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 535 LEEKNKNLQETLIDTEKQLEEIKKQCQDKEvQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLPMLDAKQLQSENDNLR 614
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 615 EQNATASKIIESQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRKEGSLQRLTEALLENQRQMGetySLLDQGHEAE 694
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE---SLERRIAATE 837
|
..
gi 326368265 695 QS 696
Cdd:TIGR02168 838 RR 839
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
485-653 |
8.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 485 DRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKE 564
Cdd:COG4717 88 EEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 565 VQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRlpmlDAKQLQSENDNLREQNATASKIIESQQDEINRM--ILEIQSMQ 642
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALE 242
|
170
....*....|.
gi 326368265 643 GKLCEEKLTAR 653
Cdd:COG4717 243 ERLKEARLLLL 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
446-801 |
9.29e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 446 EQKLASTEKEVL---QLNEFLKQRISQFSEEkkkleeklktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTL 522
Cdd:pfam05557 124 ELELQSTNSELEelqERLDLLKAKASEAEQL--------------RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 523 DDVQSQSLQ-------LQVLEEKNKNLQETlIDTEKQLEEIKKQCQDKevqlLCQKKKEKELVTSVQSLQQKVEKCLED- 594
Cdd:pfam05557 190 KNSKSELARipelekeLERLREHNKHLNEN-IENKLLLKEEVEDLKRK----LEREEKYREEAATLELEKEKLEQELQSw 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 595 ---------GIRLPMLDA---KQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCEEKlTARSTVEELGRK 662
Cdd:pfam05557 265 vklaqdtglNLRSPEDLSrriEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLN-KKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 663 egsLQRltEALLENQ-----RQMGETYsllDQGHEAEQSRPQTIHSKWPLFDLTVIDQL-FKEMSYCLFDLKALCSILNQ 736
Cdd:pfam05557 344 ---LQR--RVLLLTKerdgyRAILESY---DKELTMSNYSPQLLERIEEAEDMTQKMQAhNEEMEAQLSVAEEELGGYKQ 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326368265 737 RAQGKEPNLSLLlgiRSMNCSAEETENDHSPETLTKKLSD----VCQLRRDIDELRTTISDRYAQDMGD 801
Cdd:pfam05557 416 QAQTLERELQAL---RQQESLADPSYSKEEVDSLRRKLETleleRQRLREQKNELEMELERRCLQGDYD 481
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
442-696 |
1.14e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 442 QEELEQKLASTEKEVLQLNEFLKQRI-SQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLP 520
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKkALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 521 TLDDVQSQSLQLQVLEEKNKNLQETLID-TEKQLEEIKKQCQDKEVQ-----------LLCQKKKEKELV-TSVQSLQQK 587
Cdd:pfam02463 262 KEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRkvddeeklkesEKEKKKAEKELKkEKEEIEELE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 588 VEKCLEDGIRLPMLDAKQLQS---ENDNLREQNATASKIIESQQdEINRMILEIQSMQGKLcEEKLTARSTVEELGRKEG 664
Cdd:pfam02463 342 KELKELEIKREAEEEEEEELEklqEKLEQLEEELLAKKKLESER-LSSAAKLKEEELELKS-EEEKEAQLLLELARQLED 419
|
250 260 270
....*....|....*....|....*....|..
gi 326368265 665 SLQRLTEALLEnQRQMGETYSLLDQGHEAEQS 696
Cdd:pfam02463 420 LLKEEKKEELE-ILEEEEESIELKQGKLTEEK 450
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
448-671 |
2.26e-03 |
|
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: 41.65 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 448 KLASTEKEVLQLNEFLKQRISQFSEEKKKLeeklktrDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQS 527
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDRESDRNQELQKRIRLLEKREAE-------AE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 528 QSLQLQVleEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQ----SLQQKVEKCLEDGIRLPMLDA 603
Cdd:pfam05557 69 EALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQraelELQSTNSELEELQERLDLLKA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326368265 604 KqlQSENDNLREQNATASKIIESQQDEINRMILEIQSmQGKLCEEKLTARSTVEELGRKEGSLQRLTE 671
Cdd:pfam05557 147 K--ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS-QEQDSEIVKNSKSELARIPELEKELERLRE 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
531-679 |
2.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 531 QLQVLEEKNKNLQETLIDTEKQLEEIKKQCQD-KEVQLLCQKKKE--------KELVTSVQSLQQKVEKCLEDGIRLPML 601
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAlQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 602 DA--KQLQSENDNLREQNATASKIIESQQDEINRMILEIQSmqgklCEEKLTARSTVEELGRKEGSLQRLTEALLENQRQ 679
Cdd:COG4913 691 EEqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-----LQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
490-642 |
2.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 490 SLKKKcqKESEQNKEKQRRIETLEKyladlptldDVQSQSLQLQVLEEKNKNLQETLidtEKQLEEIKKQCQ--DKEVQL 567
Cdd:PRK12704 53 AIKKE--ALLEAKEEIHKLRNEFEK---------ELRERRNELQKLEKRLLQKEENL---DRKLELLEKREEelEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 568 LCQKKKE-KELVTSVQSLQQKVEKCLEDGIRLPMLDAKQLQSEN--DNLREQnatASKII-------ESQQDEINRMILe 637
Cdd:PRK12704 119 LEQKQQElEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKveEEARHE---AAVLIkeieeeaKEEADKKAKEIL- 194
|
....*
gi 326368265 638 IQSMQ 642
Cdd:PRK12704 195 AQAIQ 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-606 |
2.67e-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: 41.58 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 362 ESVLKIKEGLLRQKEIVIDRQKQQINHLHERIRD-----NELRAQHAMLGHYVNCEDSYVSNLQPQYESSSGQSLFTEQp 436
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 437 lshpHQEELEQKLASTEKEVLQLN---EFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLE 513
Cdd:TIGR02168 331 ----KLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 514 KYLADL-----------------PTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKE 576
Cdd:TIGR02168 407 ARLERLedrrerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250 260 270
....*....|....*....|....*....|...
gi 326368265 577 L---VTSVQSLQQKVEKcLEDGIRLPMLDAKQL 606
Cdd:TIGR02168 487 LqarLDSLERLQENLEG-FSEGVKALLKNQSGL 518
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
442-705 |
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 326368265 442 QEELEQKLASTEKEVLQLNEFLKqrISQFSEEKKKLEEK-LKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKY--LAD 518
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEEEAA--GSRLKRKKKEALKKlIEETENLAELIIDLEELKLQELKLKEQAKKALEYYqlKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 519 LPTLDDVQSQSLQLQVLEEKNKNLQEtLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEdgirl 598
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQE-LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA----- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 599 pmLDAKQLQSENDNLREQNATASKIIESQQDEINRMILEIQSMQGKLCE---EKLTARSTVEELGRKEGSLQRLTEALLE 675
Cdd:pfam02463 293 --KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEElekELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270
....*....|....*....|....*....|
gi 326368265 676 NQRQMGETYSLLDQGHEAEQSRPQTIHSKW 705
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELK 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
517-672 |
3.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 517 ADLPTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKcLEDgi 596
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 597 RLPML----DAKQLQSENDNLREQNATASKII-------ESQQDEINRMILEIQSMQGKLcEEKLTARStvEELGRKEGS 665
Cdd:COG1579 81 QLGNVrnnkEYEALQKEIESLKRRISDLEDEIlelmeriEELEEELAELEAELAELEAEL-EEKKAELD--EELAELEAE 157
|
....*..
gi 326368265 666 LQRLTEA 672
Cdd:COG1579 158 LEELEAE 164
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-662 |
3.62e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLasteKEVLQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADlptl 522
Cdd:TIGR02169 815 REIEQKL----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---- 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 523 ddvqsqslqlqvLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLPMLD 602
Cdd:TIGR02169 887 ------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326368265 603 --AKQLQSENDNLREQNATASKIIEsQQDEINRMILEIQSMQGKLCEEKLTARSTVEELGRK 662
Cdd:TIGR02169 955 dvQAELQRVEEEIRALEPVNMLAIQ-EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
372-634 |
4.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 372 LRQKEIVIDRQKQQINHLHERIrdNELRAQHAMLGhyvncedSYVSNLQPQYESSSGQSLFTEQplshpHQEELEQKLAS 451
Cdd:COG1196 262 LAELEAELEELRLELEELELEL--EEAQAEEYELL-------AELARLEQDIARLEERRRELEE-----RLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 452 TEKEVLQLNEflkQRISQFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQ 531
Cdd:COG1196 328 LEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 532 LQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQSLQQKVEKCLEDGIRLpmldAKQLQSEND 611
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE----AALLEAALA 480
|
250 260
....*....|....*....|...
gi 326368265 612 NLREQNATASKIIESQQDEINRM 634
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADY 503
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
445-639 |
4.90e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 445 LEQKLASTEKEVLQLNEFLKQRISQFSEEKKKLEEKLKTRDRYISSLKkkcqKESEQNKEKQRRIetleKYLADLPTLDD 524
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAR----ADLEDIKIKINEL----KDKHDKYEEIK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 525 VQSQSLQLQVLEEK-----NKNLQETLIDTE---KQLEEIKKQCQDKEVQLlcqkkKEKEL-VTSVQSLQQKVEKCLEDG 595
Cdd:PRK01156 553 NRYKSLKLEDLDSKrtswlNALAVISLIDIEtnrSRSNEIKKQLNDLESRL-----QEIEIgFPDDKSYIDKSIREIENE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 326368265 596 IRL-----PMLDAKQLQSEN-----DNLREQNATASKIIESQQdEINRMILEIQ 639
Cdd:PRK01156 628 ANNlnnkyNEIQENKILIEKlrgkiDNYKKQIAEIDSIIPDLK-EITSRINDIE 680
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
443-633 |
4.93e-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: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 443 EELEQKLASTEKEVLQLNEFLKQRISQFSEekkkleeklkTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYLADL--- 519
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNE----------LQAE-LEALQAEIDKLQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 520 -----------------PTLDDVQSQSLQLQVLEEKNKNLQETLIDTEKQLEEIKKQCQDKEVQLLCQKKKEKELVTSVQ 582
Cdd:COG3883 95 lyrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 326368265 583 SLQQKVEKCLEdgirlpmldakQLQSENDNLREQNATASKIIESQQDEINR 633
Cdd:COG3883 175 AQQAEQEALLA-----------QLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
517-622 |
6.72e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 517 ADLPTLDDVQSQSLQLQ---VLEEKNKNLQETLIDTEKQLEEIKKQCQDKE--VQLLCQKKKE-KELVTSVQSLQQKVEK 590
Cdd:PRK11281 33 GDLPTEADVQAQLDALNkqkLLEAEDKLVQQDLEQTLALLDKIDRQKEETEqlKQQLAQAPAKlRQAQAELEALKDDNDE 112
|
90 100 110
....*....|....*....|....*....|..
gi 326368265 591 CLEDgiRLPMLDAKQLQSENDNLREQNATASK 622
Cdd:PRK11281 113 ETRE--TLSTLSLRQLESRLAQTLDQLQNAQN 142
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
497-703 |
8.74e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 497 KESEQNKEKQRRIETLEKYLADLptLDDVQSQslqlqvlEEKNKNLQETLIDTEKQLEEIKKQCQdkevQLLCQKKKEKE 576
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSL--QSELRRI-------ENRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368265 577 LVTSVQSLQQKVEKCLEDGIRlpMLDAkqLQSENDNLREQNATASKIIESQQDEINRMIL-EIQSMQGKLCEEKLTARST 655
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKS--ELKE--LEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 326368265 656 VEELGRKEGSLQrLTEALLENQRQmgETYSLLDQGHEAEQSRPQTIHS 703
Cdd:TIGR02169 814 LREIEQKLNRLT-LEKEYLEKEIQ--ELQEQRIDLKEQIKSIEKEIEN 858
|
|
| |
