|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
652-858 |
8.05e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 652 RHVPEVMESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDgieiEAEQQYTELTSEIDELCEIVQRKDQE 731
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS----SLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 732 LAILKEKVtnvinieNSLKDDVDSQKV-IVQRQKEIIENLREELDAITKKLGEvtKLRDKAVEEATLYKMKNMERDRFLS 810
Cdd:TIGR02169 774 LHKLEEAL-------NDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQ--KLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17567495 811 REAQMSM----------EIEDLQRELNKQKLILNQTSmAKLADtFDRKVLHLENELRE 858
Cdd:TIGR02169 845 LKEQIKSiekeienlngKKEELEEELEELEAALRDLE-SRLGD-LKKERDELEAQLRE 900
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-859 |
9.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 659 ESLQVEIDRLQGDLEKVKSGEKEL---LQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELAIL 735
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 736 KEKVTNViniENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMKNMERDRFLSREAQM 815
Cdd:COG1196 357 EAELAEA---EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17567495 816 SMEIEDLQRELNKQKLILNQTSMAKLADTFDRKVLHLENELRER 859
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
586-859 |
1.14e-05 |
|
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: 49.67 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 586 SAEVEQLVAAINAFGRDEEQqmsaymvgKKMAAEKKRKSAMDTTAMTSSCQDQTVQTD---NNSFILVDRHVPEVmESLQ 662
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAE--------LEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEV-EQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 663 VEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQ---QYTELTSEIDELCEIVQRkdqelaiLKEKV 739
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTL-------LNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 740 TNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEAT----LYKMKNMERDRFLSREAQM 815
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallnERASLEEALALLRSELEEL 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17567495 816 SMEIEDLQRELNK--QKLILNQTSMAKLA---DTFDRKVLHLENELRER 859
Cdd:TIGR02168 900 SEELRELESKRSElrRELEELREKLAQLElrlEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
656-858 |
1.47e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 656 EVMESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIdgieIEAEQQYTELTSEIDELCEIVQRKDQELAIL 735
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 736 KEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMK----NMERDRFLSR 811
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladlNAAIAGIEAK 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17567495 812 EAQMSMEIEDLQRELNKQKLILNQTsmAKLADTFDRKVLHLENELRE 858
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQL--AADLSKYEQELYDLKEEYDR 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
659-826 |
2.95e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 659 ESLQVEIDRLQGDLEKVKSG----EKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEI-------DELCEIVQR 727
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEiselEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaslersiAEKERELED 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 728 KDQELAILKEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMK------ 801
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklkr 399
|
170 180 190
....*....|....*....|....*....|
gi 17567495 802 -----NMERDRFLSREAQMSMEIEDLQREL 826
Cdd:TIGR02169 400 einelKRELDRLQEELQRLSEELADLNAAI 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
664-859 |
3.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 664 EIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVI 743
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 744 NIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATlyKMKNMERDRFLSREAQMSMEIEDLQ 823
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE--ALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190
....*....|....*....|....*....|....*.
gi 17567495 824 RELNKQKLILNQTSMAKLADTFDRKVLHLENELRER 859
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
652-794 |
3.05e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 652 RHVPEVMESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIE-----IEAEQQYTELTSEIDEL-CEIV 725
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnVRNNKEYEALQKEIESLkRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17567495 726 QRKDQELAILkEKVTNVINIENSLKDDVDSQKvivQRQKEIIENLREELDAITKKLGEVTKLRDKAVEE 794
Cdd:COG1579 107 DLEDEILELM-ERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
658-858 |
5.99e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 658 MESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAE---QQYTELTSEIDELCEIVQRKDQELAI 734
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 735 LKEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEAtlyKMKNMERDRFLSREAQ 814
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLE 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17567495 815 MSMEIEDLQRELnkQKLILNQTSMAKLADTFDRKVLHLENELRE 858
Cdd:COG1196 391 ALRAAAELAAQL--EELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
661-861 |
6.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 661 LQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQR----KD--QELAI 734
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelKDaeKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 735 LKEKVtnvinieNSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVT--KLRDKAVEEATLYKMKNMERDRFLSRE 812
Cdd:PRK03918 617 EEKEL-------KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeELREEYLELSRELAGLRAELEELEKRR 689
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17567495 813 AQMSMEIEDLQRELN-----KQKLILNQTSMAKLADtFDRKVLHLENELRERDM 861
Cdd:PRK03918 690 EEIKKTLEKLKEELEerekaKKELEKLEKALERVEE-LREKVKKYKALLKERAL 742
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-859 |
7.79e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 659 ESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIE---IEAEQQYTELTSEIDELCE-IVQRKDQELAI 734
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEaelAEAEEALLEAEAELAEAEEeLEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 735 LKEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLY---KMKNMERDRFLSR 811
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeeeEALLELLAELLEE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17567495 812 EAQMSMEIEDLQRELNKQKLILN-QTSMAKLADTFDRKVLHLENELRER 859
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
664-879 |
9.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 664 EIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELtseidelcEIVQRKDQELAILKEKVTNVI 743
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 744 NIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMKNMERD---RFLSREAQMSMEIE 820
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDelrEIEKRLSRLEEEIN 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17567495 821 DLQR---ELNKQKLILNQTSmaKLADTFDRKVLHLENELRERDMLICKQNQiINSHRKSPTG 879
Cdd:PRK03918 325 GIEErikELEEKEERLEELK--KKLKELEKRLEELEERHELYEEAKAKKEE-LERLKKRLTG 383
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
653-843 |
2.42e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 653 HVPEVMESLQVEIDRLQGDLEK-------VKSGEKELLQI-------NSKLKEELEESQQ--TIDGIEIEAEQQYTElts 716
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLLEKevdakkyVEKNLPEIEDYlehaeeqNKELKEELERVQQsyTLNENELERVRGLEK--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 717 eidELCEIVQRKDQELAILKEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLR----EELDAitkklgevtklRDKAV 792
Cdd:pfam06160 337 ---QLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEA-----------REKLD 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17567495 793 E-EATLYKMK-NMER-------DRFLSREAQMSMEIEDLQRELNK---------QKLILNQTSMAKLAD 843
Cdd:pfam06160 403 EfKLELREIKrLVEKsnlpglpESYLDYFFDVSDEIEDLADELNEvplnmdevnRLLDEAQDDVDTLYE 471
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
646-863 |
2.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 646 SFILVDRHVPEVMESLQVEIDRLQG---DLEKVKSGEKELLQINsKLKEELEESQQTIDGIEI--------EAEQQYTEL 714
Cdd:COG4913 215 EYMLEEPDTFEAADALVEHFDDLERaheALEDAREQIELLEPIR-ELAERYAAARERLAELEYlraalrlwFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 715 TSEIDELCEIVQRKDQELAILKEKVTNVINIENSLKDDVDSQKVivqrqkEIIENLREELDAITKKLGEVTKLRDKAVEE 794
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17567495 795 ATLYKMKNM-ERDRFLSREAQMSMEIEDLQRELNKQKLILNQTSMAKLADTFDRKVLHLE-NELRERDMLI 863
Cdd:COG4913 368 LAALGLPLPaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiASLERRKSNI 438
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
664-920 |
2.86e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 664 EIDRLQGDLEKVKsgeKELLQINSKLKEELEESQQTIDGIEiEAEQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVI 743
Cdd:COG4942 21 AAAEAEAELEQLQ---QEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 744 NIENSLKDDVDSQKVIVQRQ-------------------------KEIIENLREELDAITKKLGEVTKLRDKAVEeatly 798
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEA----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 799 kmknmERDRFLSREAQMSMEIEDLQRELNKQKLILNQTSmAKLADTFDRKVLHLENELRERDMLICKQNQIINSHRKSPT 878
Cdd:COG4942 172 -----ERAELEALLAELEEERAALEALKAERQKLLARLE-KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17567495 879 GSVITHRKMQP---RASVLAAAGNLPSAGSSSesfqNGLDVEARE 920
Cdd:COG4942 246 AGFAALKGKLPwpvSGRVVRRFGERDGGGGRN----KGIDIAAPP 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
658-860 |
4.23e-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: 44.28 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 658 MESLQVEIDRLQGDLEKVKSG----EKELLQINSKL------KEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQR 727
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEvselEEEIEELQKELyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 728 KDQELAILKEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELD----AITKKLGEVTKLRDKAVEEATLYKMKNM 803
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17567495 804 ERDRFLSREAQMSMEIEDLQRELNKQKLILNQTSMAKLADTFDRKVLHLENELRERD 860
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
658-844 |
4.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 658 MESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDgieiEAEQQYTELTSEIDELCEIVQRKDQELAILK- 736
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELGERARALYRSGGSVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 737 ----EKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMKNMERDRFLSR- 811
Cdd:COG3883 108 llgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQl 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 17567495 812 ---EAQMSMEIEDLQRELNKQKLILNQTSMAKLADT 844
Cdd:COG3883 188 saeEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
705-858 |
4.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 705 IEA-EQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVINIENSLKDDVDSQKviVQRQkeiIENLREELDAITKKLGE 783
Cdd:COG4913 612 LAAlEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AERE---IAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17567495 784 VTKLRDKAVEEATLYKMKNMERDRFLSREAQMSMEIEDLQRELNKQKLILNQTSMAKLADTFdrkvLHLENELRE 858
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR----ALLEERFAA 757
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-858 |
5.31e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 659 ESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIdgieIEAEQQYTELTSEIDELceiVQRKDQELAILKEK 738
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAEL---EEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 739 VTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMKNMERDRFLSREAQMSME 818
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17567495 819 IEDLQRELNKQKLILNQTSMAKLADtfDRKVLHLENELRE 858
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEA--AEEEAELEEEEEA 460
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
680-848 |
1.57e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 680 KELLQINSKLKEELEESQQTidgiEIEAEQQYTELTSEIDELCEIVQRKDQELAILKEKvtnvinIENSLKDdvdsqKVI 759
Cdd:pfam13851 22 RNNLELIKSLKEEIAELKKK----EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQ------LENYEKD-----KQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 760 VQRQKEIIENLREELDAItKKLGEVTKLRDKAVEEatlykmknmERDRFLSREAQMsmeIEDLQRELNKQKLILnQTSMA 839
Cdd:pfam13851 87 LKNLKARLKVLEKELKDL-KWEHEVLEQRFEKVER---------ERDELYDKFEAA---IQDVQQKTGLKNLLL-EKKLQ 152
|
....*....
gi 17567495 840 KLADTFDRK 848
Cdd:pfam13851 153 ALGETLEKK 161
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
668-844 |
1.83e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 668 LQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVINIEN 747
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 748 SLKDDVDS----QKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMKNMERDRFLSREAQMSMEIEDLQ 823
Cdd:pfam07888 112 ELSEEKDAllaqRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180
....*....|....*....|...
gi 17567495 824 RELNKQKLILNQ--TSMAKLADT 844
Cdd:pfam07888 192 KEFQELRNSLAQrdTQVLQLQDT 214
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
613-840 |
2.29e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 613 GKKMAAEKKRKSAMDTTAMtsscQDQTVQTDNNSFILVDRHVPEVMESLQVEIDRLQgDLEKVKSGEKELLQINSKLKEE 692
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAEL----CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQIHLQETRKKAVVLARLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 693 LEESQQTIDGIEIEAEQQYTELtSEIDELCEIVQRKDQELAILKEKVTNVINIENSLKDDvdsqkviVQRQKEIIENLRE 772
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDI-DNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-------RASLKEQMQEIQQ 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17567495 773 ELDAITKKLGEVTKLRDKA---VEEATLYKMKNMERDRFLSREAQmsMEIEDLQRELNKQKLILNQTSMAK 840
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLqniTVRLQDLTEKLSEAEDMLACEQH--ALLRKLQPEQDLQDVRLHLQQCSQ 639
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
565-862 |
3.11e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 565 DDELDSVGDEFDEDL-LAVKQISAEVEQLVAainafgrdeEQQMSayMVGKKMAAEKKRKSAMDTTAMTSSCQDQTvqTD 643
Cdd:pfam15921 244 EDQLEALKSESQNKIeLLLQQHQDRIEQLIS---------EHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQA--RN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 644 NNSFILvdRHVPEvmesLQVEIDRLQGDL--------EKVKSGEKELLQINSKLKEELEESQQTidgieieaEQQYTELT 715
Cdd:pfam15921 311 QNSMYM--RQLSD----LESTVSQLRSELreakrmyeDKIEELEKQLVLANSELTEARTERDQF--------SQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 716 SEIDELCEIVQRKDQELAILKEK--------VTNVINIENsLKDDVDSQKVIVQRQKEIIENLR---------------- 771
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQnkrlwdrdTGNSITIDH-LRRELDDRNMEVQRLEALLKAMKsecqgqmerqmaaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 772 -----EELDAITKKLGEVTKLRDKAVEEATLYKMKNMERDRFLSreaqmsmeieDLQRELNKQKLILNQTS--MAKLADT 844
Cdd:pfam15921 456 kneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS----------DLTASLQEKERAIEATNaeITKLRSR 525
|
330
....*....|....*...
gi 17567495 845 FDRKVLHLENELRERDML 862
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHL 543
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
649-858 |
3.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 649 LVDRHVPEVMESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDgiEIEAEQQYTELTSEIDEL-CEIVQR 727
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLKELEEKLKKYnLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 728 KDQELAILKEKVTNVINIENSLKDDVDSQKVIVQRQKEI---IENLREELDAITKKLGEVTKLRDKAVEEatlyKMKNME 804
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELekkLDELEEELAELLKELEELGFESVEELEE----RLKELE 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17567495 805 R--DRFLSREAQMSmEIEDLQRELNKQKLILNQTSmAKLADTfDRKVLHLENELRE 858
Cdd:PRK03918 599 PfyNEYLELKDAEK-ELEREEKELKKLEEELDKAF-EELAET-EKRLEELRKELEE 651
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
642-818 |
3.47e-03 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 41.16 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 642 TDNNSFILVDRHVPEVMESLQVEIDRLqgdLEKVKSGEKELLQINSKLKEELEESQQTID-------------GIEIEAE 708
Cdd:COG0466 107 VQEEPYLEAEVEPLEEEEEDDKELEAL---MRSLKEQFEEYVKLNPKIPPELLAALSNIEdpgrladfiashlPLKIEEK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 709 QQYTELTSeidelceIVQRKDQELAILKEKVtNVINIENSLKDDVDSQkvIVQRQKEIIenLREELDAITKKLG------ 782
Cdd:COG0466 184 QELLETLD-------VKERLEKLLELLEKEI-EVLELEKKIRSRVKEQ--MEKSQREYY--LREQLKAIQKELGekddge 251
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17567495 783 -EVTKLRDKaVEEATLYK------MKNMERdrfLSREAQMSME 818
Cdd:COG0466 252 dEIEELREK-IEKAKLPEevkekaEKELKK---LERMPPMSAE 290
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
654-828 |
3.78e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 654 VPEVMESLQVEidrLQGDLEKVKSGEKEL---------LQINSK---LKEELEESQQTIDGIEI-EAEQQYTELTSEIDE 720
Cdd:PRK04778 217 IPELLKELQTE---LPDQLQELKAGYRELveegyhldhLDIEKEiqdLKEQIDENLALLEELDLdEAEEKNEEIQERIDQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 721 LCEIVQRK-------DQELAILKEKVTNVINIENSLKDDVD--SQKVIVQ-RQKEIIENLREELDAITKklgEVTKLRDK 790
Cdd:PRK04778 294 LYDILEREvkarkyvEKNSDTLPDFLEHAKEQNKELKEEIDrvKQSYTLNeSELESVRQLEKQLESLEK---QYDEITER 370
|
170 180 190
....*....|....*....|....*....|....*...
gi 17567495 791 AVEEATLYkmkNMERDRFLSREAQMSmEIEDLQRELNK 828
Cdd:PRK04778 371 IAEQEIAY---SELQEELEEILKQLE-EIEKEQEKLSE 404
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
671-859 |
3.94e-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: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 671 DLEKVKSGEKELLQINSKLKEELEESQQTIDGIE---IEAEQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVINIE- 746
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 747 -NSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEatlYKMKNMERDRFLSreaqmsmEIEDLQRE 825
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELA-------ELEAELEE 160
|
170 180 190
....*....|....*....|....*....|....
gi 17567495 826 LNKQKlilnqtsmAKLADTFDRKVLHLENELRER 859
Cdd:COG1579 161 LEAER--------EELAAKIPPELLALYERIRKR 186
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
675-830 |
4.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 675 VKSGEKEllqINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRK----DQELAILKEKvtnvinienslK 750
Cdd:PRK12704 44 LEEAKKE---AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKeenlDRKLELLEKR-----------E 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 751 DDVDSQKVIVQRQKEIIENLREELDAITKKlgEVTKLRDKA---VEEATLYKMKNMERDrfLSREAQMSM-EIEDLQREL 826
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEE--QLQELERISgltAEEAKEILLEKVEEE--ARHEAAVLIkEIEEEAKEE 185
|
....
gi 17567495 827 NKQK 830
Cdd:PRK12704 186 ADKK 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
659-802 |
5.17e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 659 ESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELaiLKEK 738
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN--LEKE 562
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17567495 739 VTNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEATLYKMKN 802
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
656-782 |
6.52e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 656 EVMESLQVEIDRLQGDLEKVKSGEKELLQINSKLKEELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELAIL 735
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17567495 736 KEKV---TNVINIENSLKDDVDSQKVIVQRQKEI--------IENLREELDAITKKLG 782
Cdd:smart00787 231 EEELqelESKIEDLTNKKSELNTEIAEAEKKLEQcrgftfkeIEKLKEQLKLLQSLTG 288
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
656-781 |
7.59e-03 |
|
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: 40.01 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 656 EVMESLQVEIDRLQGDLEKVKSGEKELL----QINSKLKEELEESQQTIDGIEI---------EAEQQYTELTSEIDELc 722
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLEssikQVEEELEELKEQNEELEKQYKVkkktldllpDAEENIAKLQALVDAS- 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 723 eiVQRKdQELAILKEKV-TNVINIENSLKDDVDSQKVIVQRQKEIIENLREELDAITKKL 781
Cdd:pfam05667 414 --AQRL-VELAGQWEKHrVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEA 470
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
612-843 |
7.81e-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: 40.34 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 612 VGKKMAAEKKRKSAMDTTAMTSSCQDQTVQTDNNSFILVDRHVPEVMESLQVEIDRLQGDLEKVKSGEKELlqinSKLKE 691
Cdd:pfam02463 270 VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL----EKELK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 692 ELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVINIENSLKDDVDSQKVIVQRQKEIIENLR 771
Cdd:pfam02463 346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17567495 772 EELDAITKklgEVTKLRDKAVEEATLYKMKNMERDRFLSREAQMSMEIEDLQRELNKQKLILNQTSMAKLAD 843
Cdd:pfam02463 426 KEELEILE---EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
679-862 |
8.09e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 679 EKELLQINSKLK--EELEESQQTIDGIEIEAEQQYTELTSEIDELCEIVQRKDQELAILKEKVTNVINIENSLKDDVDSQ 756
Cdd:COG1196 221 ELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 757 KVIVQRQKEIIENLREELDAITKKLGEVTK-----------LRDKAVEEATLYKMKNMERDRFLSREAQMSMEIEDLQRE 825
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEeleeleeeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190
....*....|....*....|....*....|....*....
gi 17567495 826 LN--KQKLILNQTSMAKLADTFDRKVLHLENELRERDML 862
Cdd:COG1196 381 LEelAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
689-849 |
8.47e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 689 LKEELEEsqqTIDGIEIEaeqqYTELTSEIDELCEIVQRKDQELAILKEKVTNVINIE-----------NSLKDDVDSQK 757
Cdd:smart00787 145 LKEGLDE---NLEGLKED----YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEdeledcdptelDRAKEKLKKLL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567495 758 VIVQRQKEIIENLREELDAITKKLGEVTKLRDKAVEEAtlykmknMERDRFLSREAQMSM-EIEDLQRELNKQKLILN-- 834
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI-------AEAEKKLEQCRGFTFkEIEKLKEQLKLLQSLTGwk 290
|
170
....*....|....*..
gi 17567495 835 --QTSMAKLADTFDRKV 849
Cdd:smart00787 291 itKLSGNTLSMTYDREI 307
|
|
| |
