|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-555 |
1.70e-12 |
|
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: 70.87 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 197 LEQLAKEIASKK---SAIKDELKGIPGRIDSVRDAMPESE--------DWAVLEKEIADKKEKIKDIDSQLADKSKQIEA 265
Cdd:TIGR02169 676 LQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSDASrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 266 EFKAKSELQKQIGNKKLAKSQRENEIrqnaNKSYHDVLDNiskleyQVKSKDAEISRKQEEHSRIKANIEALNNDLEvlr 345
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLN--- 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 346 gkfyaidaetlqypegaficptcKRELEVEDIQAKQQELQDNFNLNKANRlKAVQNEGKEKAAKVEELKKQCSIIQATIT 425
Cdd:TIGR02169 823 -----------------------RLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 426 QLSNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDLENQLKaeakpidttELKEAKATLSEAIDELNKKL 505
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIE---------ELEAQIEKKRKRLS---------ELKAKLEALEEELSEIEDPK 940
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 506 GKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFL-VQDFQ---------KEKDNKLME 555
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaIQEYEevlkrldelKEKRAKLEE 1000
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-538 |
9.56e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 5 FLKKLILKNFKKIQDLT-VEFTDKNTFICGGNGTGKTTLQDAFLWLLfGKDSTN--RADTNFNIKTLGEDGKPILHLVhS 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTtINFDKGITGIVGPNGCGKSNIVDAIRWVL-GEQSAKalRGGKMEDVIFNGSETRKPLSLA-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 82 VTGVLS-INGRDVELQRNYVEkwgsgVNAGVLQNHATEFYLNGVKLKTKKEYD--------AEVAAILPEDVFRMITNPl 152
Cdd:TIGR02168 79 VELVFDnSDGLLPGADYSEIS-----ITRRLYRDGESEYFINGQPCRLKDIQDlfldtglgKRSYSIIEQGKISEIIEA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 153 yfptmKAQDQKAMLLEMAG---------------NVTNEEVANINPKFQELislisGRTLEQLAK--EIASKKSAIKDEL 215
Cdd:TIGR02168 153 -----KPEERRAIFEEAAGiskykerrketerklERTRENLDRLEDILNEL-----ERQLKSLERqaEKAERYKELKAEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 216 KGIpgridsvrdampeseDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQnA 295
Cdd:TIGR02168 223 REL---------------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-L 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 296 NKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQYPEgaficptcKRELEVE 375
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE--------ELESLEA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 376 DIQAKQQELQdnfnlNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPE---EQDTQ 452
Cdd:TIGR02168 359 ELEELEAELE-----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkKLEEA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 453 KIILSDPTWLSLSNEIVDLENQLKA--EAKPIDTTELKEAKATLSEAIDELNKKLGKRDTIERsnkVIEDLEDRRDKNNE 530
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERleEALEELREELEEAEQALDAAERELAQLQARLDSLER---LQENLEGFSEGVKA 510
|
....*...
gi 2796428067 531 ALAEQERL 538
Cdd:TIGR02168 511 LLKNQSGL 518
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-97 |
1.17e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 61.56 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 6 LKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGEDGkpilhlvhSVTG 84
Cdd:COG0419 2 LLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEA--------SVEL 73
|
90
....*....|...
gi 2796428067 85 VLSINGRDVELQR 97
Cdd:COG0419 74 EFEHGGKRYRIER 86
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-556 |
1.48e-10 |
|
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: 64.70 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 5 FLKKLILKNFKKIQDLTV-EFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTN-RADTNFNIKTLGEDGKPILHLvhSV 82
Cdd:TIGR02169 1 YIERIELENFKSFGKKKViPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAmRAERLSDLISNGKNGQSGNEA--YV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 83 TGVLSINGR-----DVELQRNYVEKwgsgvnagvlQNHATEFYLNGVKLkTKKEYDAEVAA--ILPE--------DVFRM 147
Cdd:TIGR02169 79 TVTFKNDDGkfpdeLEVVRRLKVTD----------DGKYSYYYLNGQRV-RLSEIHDFLAAagIYPEgynvvlqgDVTDF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 148 ITnplyfptMKAQDQKAMLLEMAG---------NVTNE-EVANINPKFQELISLISGRTLEQLAKE--IASKKSAIKDEL 215
Cdd:TIGR02169 148 IS-------MSPVERRKIIDEIAGvaefdrkkeKALEElEEVEENIERLDLIIDEKRQQLERLRREreKAERYQALLKEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 216 KGIPG--RIDSVRDAMPESEDwavLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIgnkklaKSQRENEIRQ 293
Cdd:TIGR02169 221 REYEGyeLLKEKEALERQKEA---IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI------KDLGEEEQLR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 294 nANKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGkfyaidaetlqypegaficptckrelE 373
Cdd:TIGR02169 292 -VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER--------------------------E 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 374 VEDIQAKQQELQDnfnlnkanRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQK 453
Cdd:TIGR02169 345 IEEERKRRDKLTE--------EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 454 iilsdptwlSLSNEIVDLENQLK-AEAKpidtteLKEAKATLSEAIDELNKKLGKRDTIersnkvIEDLEDRRDKNNEAL 532
Cdd:TIGR02169 417 ---------RLSEELADLNAAIAgIEAK------INELEEEKEDKALEIKKQEWKLEQL------AADLSKYEQELYDLK 475
|
570 580
....*....|....*....|....
gi 2796428067 533 AEQERLEFLVQDFQKEKDNKLMER 556
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-539 |
6.19e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADtnFNIKTLGEDGKPILhlvhSVTGV 85
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKG--LKKDDFTRIGGSGT----EIELK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 86 LSINGRDVELQRNyvekwgSGVNAGVLQNHAtefyLNGVKLKTKKEYDAEVAAILPEDVFrmiTNPLYFptmkAQDQKAM 165
Cdd:PRK03918 77 FEKNGRKYRIVRS------FNRGESYLKYLD----GSEVLEEGDSSVREWVERLIPYHVF---LNAIYI----RQGEIDA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 166 LLE-------MAGNVTN-EEVANINPKFQELISLISGRtLEQLAKEIAS------KKSAIKDELKGIPGRIDSVRDAMPE 231
Cdd:PRK03918 140 ILEsdesrekVVRQILGlDDYENAYKNLGEVIKEIKRR-IERLEKFIKRtenieeLIKEKEKELEEVLREINEISSELPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 232 -SEDWAVLEKEIAD---KKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKL------AKSQRENEIRQNANK---- 297
Cdd:PRK03918 219 lREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKeieeleEKVKELKELKEKAEEyikl 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 298 -----SYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDaetlqypegaficptcKREL 372
Cdd:PRK03918 299 sefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE----------------ERHE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 373 EVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKG--------N 444
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 445 MPEEQDTQKIILSDPTwLSLSN------EIVDLENQLKAEAKPIDTTELKEAK----ATLSEAIDELNKKLGKRDtIERS 514
Cdd:PRK03918 443 RELTEEHRKELLEEYT-AELKRiekelkEIEEKERKLRKELRELEKVLKKESEliklKELAEQLKELEEKLKKYN-LEEL 520
|
570 580
....*....|....*....|....*
gi 2796428067 515 NKVIEDLEDRRDKNNEALAEQERLE 539
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKSLK 545
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-214 |
1.03e-09 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 58.28 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 9 LILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTlgedGKPILHLVHSVTGVLSI 88
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVK----GDIRIGLEGKGKAYVEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 89 NGRDVELQRNYVEKWGSGVNagvlQNHATEFYLNGVKLKTKKEYDAEVAAILPEDvFRMITNPLYFPtmkaQDQKAMLLE 168
Cdd:pfam13476 77 TFENNDGRYTYAIERSRELS----KKKGKTKKKEILEILEIDELQQFISELLKSD-KIILPLLVFLG----QEREEEFER 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2796428067 169 MAgnvTNEEVANINPKFQELISLISGRTLEQLAKEIASKKSAIKDE 214
Cdd:pfam13476 148 KE---KKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
239-540 |
1.33e-09 |
|
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: 61.61 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 239 EKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRqNANKSYHDVLDNISKLEYQVKSKDA 318
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 319 EISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQYPEGAFicptcKRELEVEDIQAKQQELQDNFnLNKANRLKA 398
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-----ALREALDELRAELTLLNEEA-ANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 399 VQNEGKEKAAKVEELKKQcsiiqatITQLSNEKEILVHNINECKGNMPEEQDtqkiilsdptwlslsnEIVDLENQLKAE 478
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELES----------------ELEALLNERASL 885
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 479 AKPIDttELKEAKATLSEAIDELNKKLGK--------RDTIERSNKVIEDLEDRRDKNNEALAEQERLEF 540
Cdd:TIGR02168 886 EEALA--LLRSELEELSEELRELESKRSElrreleelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
5-58 |
3.70e-09 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 58.86 E-value: 3.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2796428067 5 FLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAfLWLLFGKDSTNR 58
Cdd:COG3593 2 KLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEA-LRLLLGPSSSRK 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
272-563 |
1.37e-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: 58.14 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 272 ELQKQIGNKKLAKSQRENEIR--------QNANKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEV 343
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 344 LRGKFYAIDAetlqypegaficptckrelEVEDIQAKQQELQDnfnlnkanRLKAVQNEGKEKAAKVEELKKQCSIIQAT 423
Cdd:TIGR02168 286 LQKELYALAN-------------------EISRLEQQKQILRE--------RLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 424 ITQLSNEKEILVHNINECKGNMPEEQDT-----QKIILSDPTWLSLSNEIVDLENQLKAEAKPIDT-----TELKEAKAT 493
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAEleeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERlearlERLEDRRER 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796428067 494 LSEAIDELNKKLGKRD------TIERSNKVIEDLEDRRDKNNEALAE-QERLEFLVQDFQKEKD--NKLMERINGMFSL 563
Cdd:TIGR02168 419 LQQEIEELLKKLEEAElkelqaELEELEEELEELQEELERLEEALEElREELEEAEQALDAAERelAQLQARLDSLERL 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-539 |
1.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 1 MKevfLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLfgkdstnradtnfnIKTLGEDGKPIlhlvh 80
Cdd:COG4717 1 MK---IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------LERLEKEADEL----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 81 svtgvLSINGRDVELQRNYVEKWGSgvnagvlqnhatefylngvKLKTKKEYDAEVAAilpedvfrmitnplyfptmkAQ 160
Cdd:COG4717 59 -----FKPQGRKPELNLKELKELEE-------------------ELKEAEEKEEEYAE--------------------LQ 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 161 DQKAMLlemagnvtNEEVANINPKFQELISLISGRTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMpesedwavleK 240
Cdd:COG4717 95 EELEEL--------EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL----------E 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 241 EIADKKEKIKDIDSQLADKSKQIEAEFKAKSElqkqignkklaksQRENEIRQNAnksyhdvlDNISKLEYQVKSKDAEI 320
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSL-------------ATEEELQDLA--------EELEELQQRLAELEEEL 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 321 SRKQEEHSRIKANIEALNNDLE----------------------VLRGKFYAIDAETLQYPEGAFIC---------PTCK 369
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEaaaleerlkearlllliaaallALLGLGGSLLSLILTIAGVLFLVlgllallflLLAR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 370 RELEVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSN----EKEILVHNINEC---- 441
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeelEEELQLEELEQEiaal 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 442 --KGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKAEAKPI-------DTTELKEAKATLSEAIDELNKKLGK-RDTI 511
Cdd:COG4717 376 laEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealDEEELEEELEELEEELEELEEELEElREEL 455
|
570 580
....*....|....*....|....*...
gi 2796428067 512 ERSNKVIEDLEDRRDKnNEALAEQERLE 539
Cdd:COG4717 456 AELEAELEQLEEDGEL-AELLQELEELK 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-431 |
2.15e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 184 KFQELISLISGRTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMPESE-DWAVLEKEIADKKEKIKDIDSQLADKSKQ 262
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 263 IEAEFKAKSELQKQIGNKKLAKSQREneirqnanKSYHDVLDNISKLEYQVKskdaEISRKQEEhsrIKANIEALNNDLE 342
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLE--------SRLGDLKKERDELEAQLR----ELERKIEE---LEAQIEKKRKRLS 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 343 VLRGKFYAIDAETLQY-PEGAFICPTCKRELEVEDIQAKQQELQDNFNLNKANRLKAVQ---------NEGKEKAAKVEE 412
Cdd:TIGR02169 921 ELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQeyeevlkrlDELKEKRAKLEE 1000
|
250
....*....|....*....
gi 2796428067 413 LKKQcsiIQATITQLSNEK 431
Cdd:TIGR02169 1001 ERKA---ILERIEEYEKKK 1016
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
196-557 |
1.38e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 196 TLEQLAKEIASKKSAIKDELKGIPGRIDSVR-DAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQ 274
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNeEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 275 KQIgnkklaksqRENEirqnanKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEvlrgkfyaiDAE 354
Cdd:PRK02224 391 EEI---------EELR------ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE---------EAE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 355 TLQyPEGAfiCPTCKRELE-------VEDIQAKQQELQDNFNlnkanRLKAVQNEGKEKAAKVEELKKQcsiiQATITQL 427
Cdd:PRK02224 447 ALL-EAGK--CPECGQPVEgsphvetIEEDRERVEELEAELE-----DLEEEVEEVEERLERAEDLVEA----EDRIERL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 428 SNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDLENqlKAEAKPIDTTELKEAKATLSEAIDELNKKLGK 507
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAE---------ELRERAAELEA--EAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796428067 508 -RDTIERSNKV------IEDLEDRRDKNNEALAEQERLEflvqDFQKEKDNKLMERI 557
Cdd:PRK02224 584 lKERIESLERIrtllaaIADAEDEIERLREKREALAELN----DERRERLAEKRERK 636
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8-551 |
2.19e-07 |
|
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: 54.20 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 8 KLILKNFKKIQDL-TVEFTDKNTF--ICGGNGTGKTTLQDAFLWLLFGK-----------DSTNRADTNFNIKTLGEDGK 73
Cdd:TIGR00618 5 RLTLKNFGSYKGThTIDFTALGPIflICGKTGAGKTTLLDAITYALYGKlprrsevirslNSLYAAPSEAAFAELEFSLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 74 PILHLVHSVTGVlSINGRDVEL--QRNYVEKWGSGVNAGVLQNHATEFYLNGVKLKTKKeydAEVAAILPEDVFRMITNP 151
Cdd:TIGR00618 85 TKIYRVHRTLRC-TRSHRKTEQpeQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKT---FTRVVLLPQGEFAQFLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 152 LyfPTMKAQ--------DQKAMLLEMAGNVTNEEVANINpKFQELISLISgRTLEQLAKEIASKKSAIKDELKgipgRID 223
Cdd:TIGR00618 161 K--SKEKKEllmnlfplDQYTQLALMEFAKKKSLHGKAE-LLTLRSQLLT-LCTPCMPDTYHERKQVLEKELK----HLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 224 SVRDAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKK-----LAKSQRENEIRQNANKS 298
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplAAHIKAVTQIEQQAQRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 299 YHDVLDNISKLE--------YQVKSKDAEISRK-------QEEHSRIKAN------------------IEALNNDLEVLR 345
Cdd:TIGR00618 313 HTELQSKMRSRAkllmkraaHVKQQSSIEEQRRllqtlhsQEIHIRDAHEvatsireiscqqhtltqhIHTLQQQKTTLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 346 GKFYAIDAETLQY-PEGAFICPTCKRELEV----------EDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELK 414
Cdd:TIGR00618 393 QKLQSLCKELDILqREQATIDTRTSAFRDLqgqlahakkqQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 415 KQCSIIQATITQLSNEKEILVHNINECKGNMPE--------EQDTQKIILSDPT----------WLSLSNEIVDLENQLK 476
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgscihpNPARQDIDNPGPLtrrmqrgeqtYAQLETSEEDVYHQLT 552
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796428067 477 AEAKpidttELKEAKATLSEAIDELNKKLGKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFLVQDFQKEKDN 551
Cdd:TIGR00618 553 SERK-----QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-355 |
3.80e-07 |
|
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: 51.46 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 195 RTLEQLAkEIASKKSAIKDELKGIPGRIDSVRDampeseDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQ 274
Cdd:COG1579 7 RALLDLQ-ELDSELDRLEHRLKELPAELAELED------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 275 KQIGNkklAKSQRE-----NEIRQNANKsyhdvldnISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFY 349
Cdd:COG1579 80 EQLGN---VRNNKEyealqKEIESLKRR--------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
....*.
gi 2796428067 350 AIDAET 355
Cdd:COG1579 149 EELAEL 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-548 |
5.61e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 233 EDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIgnkkLAKSQRENEIRQnanksyhdvldNISKLEyq 312
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL----EEAQAEEYELLA-----------ELARLE-- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 313 vkskdAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQypegaficptckRELEVEDIQAKQQELQDNFNLNK 392
Cdd:COG1196 302 -----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEE------------LEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 393 ANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHnineckgnmpEEQDTQKIIlsdptwlSLSNEIVDLE 472
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA----------EEALLERLE-------RLEEELEELE 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796428067 473 NQLKAEAKPIDTTELKEAKATLSEAiDELNKKLGKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFLVQDFQKE 548
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-64 |
8.32e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 51.15 E-value: 8.32e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796428067 5 FLKKLILKNFKKIQDLTVEFTDKN--TFICGGNGTGKTTLQDAfLWLLFGKDSTNRADTNFN 64
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPrlTVLVGENGSGKTTLLEA-IALALSGLLSRLDDVKFR 62
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-527 |
1.23e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 176 EEVANINPKFQELISLISGRtLEQLAKEIASKKSAIkDELKGIPGRIDSVRDAMPESEDWAVLE------KEIADKKEKI 249
Cdd:PRK03918 394 EELEKAKEEIEEEISKITAR-IGELKKEIKELKKAI-EELKKAKGKCPVCGRELTEEHRKELLEeytaelKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 250 KDIDSQLADKSKQIEAEFKAKSELQKqigNKKLAKSQRENEIR---------QNANKSYHDVLDNISKLEYQVKSKDAEI 320
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIK---LKELAEQLKELEEKlkkynleelEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 321 SRKQEehsrIKANIEALNNDLEVLRGKFYAIDAETLqypEGAFICptckreleVEDIQAKQQELQDNFNlnKANRLKAVQ 400
Cdd:PRK03918 549 EKLEE----LKKKLAELEKKLDELEEELAELLKELE---ELGFES--------VEELEERLKELEPFYN--EYLELKDAE 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 401 NEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKiilsDPTWLSLSNEIVDLENQLKAEAK 480
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL----REEYLELSRELAGLRAELEELEK 687
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2796428067 481 PIDttelkEAKATLSEAIDELNKKLGKRDTIERSNKVIEDLEDRRDK 527
Cdd:PRK03918 688 RRE-----EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-516 |
1.33e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 197 LEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMPESE----DWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSE 272
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 273 LQKQIGNKKLAKSQRENEIR------QNANKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRg 346
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE- 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 347 kfyaIDAETLQypegaficptckRELEVEDIQAKQQELQdnfnLNKAN-RLKAVQNEGKEKAAKVEELKKQCSIIQATIT 425
Cdd:TIGR02168 866 ----ELIEELE------------SELEALLNERASLEEA----LALLRsELEELSEELRELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 426 QLSNEKEILVHNINECKGNMPEE-QDTQKIILS-----DPTWLSLSNEIVDLENQLKA----------EAKPIDT----- 484
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEySLTLEEAEAlenkiEDDEEEARRRLKRLENKIKElgpvnlaaieEYEELKErydfl 1005
|
330 340 350
....*....|....*....|....*....|....*...
gi 2796428067 485 ----TELKEAKATLSEAIDELNKKLGKR--DTIERSNK 516
Cdd:TIGR02168 1006 taqkEDLTEAKETLEEAIEEIDREARERfkDTFDQVNE 1043
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
6-49 |
2.30e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 50.31 E-value: 2.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2796428067 6 LKKLILKNFKKIQDLTVEFTDKNTFIcGGNGTGKTTLQDAFLWL 49
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGPLTVLI-GANGSGKSNLLDALRFL 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-432 |
2.39e-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: 50.15 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 197 LEQLAKEIASKKSAIKDELKgipgRIDSVRDAMpesedwAVLEKEIADKKEKIKDIDSQLADKSKQIEaefkaksELQKQ 276
Cdd:COG4942 29 LEQLQQEIAELEKELAALKK----EEKALLKQL------AALERRIAALARRIRALEQELAALEAELA-------ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 277 IGNKKLAKSQRENEIRQNANKSYhdVLDNISKLEYQVKSKDA-EISRKQEEHSRI----KANIEALNNDLEVLRGKFYAI 351
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFlDAVRRLQYLKYLaparREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 352 DAETLQypegaficptcKRELEVEdIQAKQQELQDNFNlNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEK 431
Cdd:COG4942 170 EAERAE-----------LEALLAE-LEEERAALEALKA-ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
.
gi 2796428067 432 E 432
Cdd:COG4942 237 A 237
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
5-578 |
2.76e-06 |
|
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: 50.74 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 5 FLKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGEDGKPILHLvhSVT 83
Cdd:pfam02463 1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSA--EVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 84 GVLSINGRDVelqrnYVEKWGSGVNAGVLQNHATEFYLNGvKLKTKKEYdaevaAILPEDVFRMITNPlyfptmkaqdqk 163
Cdd:pfam02463 79 ITFDNEDHEL-----PIDKEEVSIRRRVYRGGDSEYYING-KNVTKKEV-----AELLESQGISPEAY------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 164 aMLLEMAGNVTNeeVANINPKFQELISLISGRTLEQLAKEIASKKSA-IKDELKGIPGRIDSVRDAMPESEDWAVLEKEI 242
Cdd:pfam02463 136 -NFLVQGGKIEI--IAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIeETENLAELIIDLEELKLQELKLKEQAKKALEY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 243 ADKKEKIKDIDS-QLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQNANKSYHDVLDNISKLEYQVKSKDAEIS 321
Cdd:pfam02463 213 YQLKEKLELEEEyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 322 RKQEEHSRIKANIEALNNDLEvlrgkfyaidaetlqypegaficptckRELEVEDIQAKQQELQDNFNLNKANRLKAVQN 401
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDE---------------------------EKLKESEKEKKKAEKELKKEKEEIEELEKELK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 402 EGKEKAAKVEELKKQCSiiqatitQLSNEKEILVHNINECKGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKAEAKP 481
Cdd:pfam02463 346 ELEIKREAEEEEEEELE-------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 482 IDTTELKEAKATLSEAIDELNKKLGKRDTIERSNkvIEDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLM-ERINGM 560
Cdd:pfam02463 419 DLLKEEKKEELEILEEEEESIELKQGKLTEEKEE--LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLE 496
|
570
....*....|....*...
gi 2796428067 561 FSLVKFSFISEKLNGNEA 578
Cdd:pfam02463 497 ERSQKESKARSGLKVLLA 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-421 |
2.87e-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: 50.84 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 184 KFQELISLISGR------TLEQLAKEIASKKS----AIKDELKGIPGRIDSVRDAMPESEDWAV-LEKEIADKKEKIKDI 252
Cdd:TIGR02169 255 KLTEEISELEKRleeieqLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 253 DSQLADKSKQIEAEFKAKSELQKQIGNKK--LAKSQRENEIRQNANKSYHDVLDN----ISKLEYQVKSKDAEISRKQEE 326
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKeeLEDLRAELEEVDKEFAETRDELKDyrekLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 327 HSRIKANIEALNNDLEVLRGKFYAIDAETLqypegAFICPTCKRELEVEDIQAKQQELQDNFnLNKANRLKAVQNEGKEK 406
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKE-----DKALEIKKQEWKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKL 488
|
250
....*....|....*
gi 2796428067 407 AAKVEELKKQCSIIQ 421
Cdd:TIGR02169 489 QRELAEAEAQARASE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
240-505 |
6.73e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 240 KEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIG--NKKLAKSQREneirqnanksyhdvldnISKLEYQVKSKD 317
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARR-----------------IRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDaetlQYPEGAFIcptckreLEVEDIQ--AKQQELQDNFNLNKANR 395
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLG----RQPPLALL-------LSPEDFLdaVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 396 LKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDL---E 472
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA---------ELAAELAELqqeA 222
|
250 260 270
....*....|....*....|....*....|...
gi 2796428067 473 NQLKAEAKPIDTTELKEAKATLSEAIDELNKKL 505
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
5-64 |
3.89e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 46.44 E-value: 3.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 5 FLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFN 64
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVL 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-416 |
4.32e-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: 46.97 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 172 NVTNEEVANINPKFQELISLISgrTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMPE-SEDWAVLEKEIADKKEKIK 250
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIE--ELEAQIEQLKEELKALREALDELRAELTLLNEEAANlRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 251 DIDSQLADKSKQIEA-------EFKAKSELQKQIgNKKLAKSQRENEIRQNANKSYHDVLDNISKLEYQVKSKDAEISRK 323
Cdd:TIGR02168 842 DLEEQIEELSEDIESlaaeieeLEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 324 QEEHSRIKANIEALNNDLEVLRGKFyaidAETLQYPEGAFICPTCKRELEVEDIQAKQQELQdnfnlNKANRLKAVQ--- 400
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERL----SEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----NKIKELGPVNlaa 991
|
250
....*....|....*..
gi 2796428067 401 -NEGKEKAAKVEELKKQ 416
Cdd:TIGR02168 992 iEEYEELKERYDFLTAQ 1008
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
246-557 |
4.58e-05 |
|
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: 46.64 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 246 KEKIKDIDSQLADKSKQIEAEFKAKSELqkQIGNKKLAkSQRENEIRQNANK-SYHDVLDNISKLEYQVKSKDAEISRKQ 324
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQEL--QFENEKVS-LKLEEEIQENKDLiKENNATRHLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 325 E-EHSRIKANIEALNNDLEVLRGKFYAIDAETlqypEGAFICPTCKRELEVEDIQAKQQELQDNFN-------------L 390
Cdd:pfam05483 175 EyEREETRQVYMDLNNNIEKMILAFEELRVQA----ENARLEMHFKLKEDHEKIQHLEEEYKKEINdkekqvsllliqiT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 391 NKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKIILSD-----PTWLSLS 465
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlqiatKTICQLT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 466 NEI-VDLENQLKAEAK-PIDTTELKEAKATLSEAIDELNKKLGKRD------TIERSNKVIEDLEDRRDKNNEALAEQER 537
Cdd:pfam05483 331 EEKeAQMEELNKAKAAhSFVVTEFEATTCSLEELLRTEQQRLEKNEdqlkiiTMELQKKSSELEEMTKFKNNKEVELEEL 410
|
330 340
....*....|....*....|
gi 2796428067 538 LEFLVQDFQKEKDNKLMERI 557
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKI 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-544 |
5.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 304 DNISKLEyqvkSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYA-----------IDAETLQypegaficptckrel 372
Cdd:COG4913 607 DNRAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswdeIDVASAE--------------- 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 373 evEDIQAKQQELQDnfnLNKAN-RLKAVQNEGKEKAAKVEELKKQcsiiqatITQLSNEKEILVHNINECKgnmpEEQDT 451
Cdd:COG4913 668 --REIAELEAELER---LDASSdDLAALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAE----EELDE 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 452 QKIILSDPTWLSLSNEIVDLENQLKAEAkpiDTTELKEAKATLSEAIDELNKKLGK-----RDTIERSNKVIEDLEDRRD 526
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAAL---GDAVERELRENLEERIDALRARLNRaeeelERAMRAFNREWPAETADLD 808
|
250
....*....|....*....
gi 2796428067 527 KNNEALAE-QERLEFLVQD 544
Cdd:COG4913 809 ADLESLPEyLALLDRLEED 827
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
373-556 |
5.19e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 373 EVEDIQAKQQELQDNFNLNKANRLKaVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQ 452
Cdd:pfam01576 97 EKKKMQQHIQDLEEQLDEEEAARQK-LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 453 KIIlsdpTWLSLSNE--IVDLENQLKAEAK------------PIDTTELKEAKATLSEAIDELNKKLGKRDtiERSNKVI 518
Cdd:pfam01576 176 KSL----SKLKNKHEamISDLEERLKKEEKgrqelekakrklEGESTDLQEQIAELQAQIAELRAQLAKKE--EELQAAL 249
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796428067 519 EDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLMER 556
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR 287
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
6-143 |
6.20e-05 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 45.37 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKdSTNRAdtnfNIKTLGEDGKPilhlVHSVTGV 85
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGK-SHRTS----RDKELIRWGAE----EAKISAV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 86 LSINGRDVELQRNYVEKWGSGVNagvlqnhatefyLNGVKLKTKKEYDAEVAAIL--PED 143
Cdd:cd03242 72 LERQGGELALELTIRSGGGRKAR------------LNGIKVRRLSDLLGVLNAVWfaPED 119
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
238-520 |
7.23e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQnANKSYHDVLDNISKLEYQVKSKD 317
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHINNELESKE 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQE-------------EHSRIKANIEALNNDLEVLRGKFYAIDAETLQ-YPEGAFICPTCKRELEVE-DIQAKQQ 382
Cdd:TIGR00606 619 EQLSSYEDklfdvcgsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQlTDENQSCCPVCQRVFQTEaELQEFIS 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 383 ELQdNFNLNKANRLKAVQNEGKEKAAKVEEL----KKQCSIIQ---ATITQLSNEKEILVHNINECKGNMpEEQDTQ--- 452
Cdd:TIGR00606 699 DLQ-SKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQSIIDlkeKEIPELRNKLQKVNRDIQRLKNDI-EEQETLlgt 776
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796428067 453 --------KIILSDPTWLS-LSNEIVDLENQLKAEAKPIDTTELKEAKATLSEAIDELNKKLGK-RDTIERSNKVIED 520
Cdd:TIGR00606 777 impeeesaKVCLTDVTIMErFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQD 854
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-62 |
1.14e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.80 E-value: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796428067 1 MKEVflkKLILKNF---KKIQdlTVEFTD---KNTF-ICGGNGTGKTTLQDAFLWLLFGKDSTNRADTN 62
Cdd:cd03279 1 MKPL---KLELKNFgpfREEQ--VIDFTGldnNGLFlICGPTGAGKSTILDAITYALYGKTPRYGRQEN 64
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
6-74 |
1.29e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 43.07 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796428067 6 LKKLILKNFKKIQDLT-VEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKD-STNRADtnfNIKTLGEDGKP 74
Cdd:cd03239 1 IKQITLKNFKSYRDETvVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAaKLRRGS---LLFLAGGGVKA 68
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-416 |
2.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 201 AKEIASKKSAIKDELKGIPGRIDSVRDAMPE-SEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEaefkaksELQKQIGn 279
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE-------ERREELG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 280 kKLAKSQRENEIRQNA------NKSYHDVLDNISKLEyQVKSKDAEI----SRKQEEHSRIKANIEALNNDLEVLRGKfy 349
Cdd:COG3883 90 -ERARALYRSGGSVSYldvllgSESFSDFLDRLSALS-KIADADADLleelKADKAELEAKKAELEAKLAELEALKAE-- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796428067 350 aidAETLQypegaficptckreLEVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQ 416
Cdd:COG3883 166 ---LEAAK--------------AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-50 |
2.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2796428067 5 FLKKLILKN---FKKIQdlTVEFTDKNTFICGGNGTGKTTLQDAFLWLL 50
Cdd:COG4913 2 RLQRLQLINwgtFDGVH--TIDFDGRGTLLTGDNGSGKSTLLDAIQTLL 48
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
6-430 |
3.99e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 43.57 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 6 LKKLI-LKNFKKIQDLTV-EFTDKNTFICGGNGTGKTTLQDAFLwLLFGKDSTNRADTNFNIKTLGEDGKP--------- 74
Cdd:COG4694 2 ITKIKkLKNVGAFKDFGWlAFFKKLNLIYGENGSGKSTLSRILR-SLELGDTSSEVIAEFEIEAGGSAPNPsvrvfnrdf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 75 ---ILHLVHSVTGVLSINGRDVELQrNYVEKwgsgvNAGVLQNHATEFylnGVKLKTKKEYDAEVAAILpEDVFRMITNP 151
Cdd:COG4694 81 veeNLRSGEEIKGIFTLGEENIELE-EEIEE-----LEKEIEDLKKEL---DKLEKELKEAKKALEKLL-EDLAKSIKDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 152 L--YFPTMKAQDQKAMLLEMAGNVTNEEVANINPKFQEL----------------ISLISGRTLEQLAKEIASKKSAIKD 213
Cdd:COG4694 151 LkkLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLkeeepepiapitplpdLKALLSEAETLLEKSAVSSAIEELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 214 ELKGIPGRIDSVRDAMPESEDWAV------LEKEIADKKEKIKD-IDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQ 286
Cdd:COG4694 231 ALIQNPGNSDWVEQGLAYHKEEEDdtcpfcQQELAAERIEALEAyFDDEYEKLLAALKDLLEELESAINALSALLLEILR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 287 RENEIRQNANKSYHDVLDN-ISKLEYQVKSKDAEISRK-----QEEHSRIKANIEALNNDLEvlrgkfyAIDAETLQYPE 360
Cdd:COG4694 311 TLLPSAKEDLKAALEALNAlLETLLAALEEKIANPSTSidlddQELLDELNDLIAALNALIE-------EHNAKIANLKA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796428067 361 GAFICPTCKRELEVEDIQAKQQELQDNFN--LNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNE 430
Cdd:COG4694 384 EKEEARKKLEAHELAELKEDLSRYKAEVEelIEELKTIKALKKALEDLKTEISELEAELSSVDEAADEINEE 455
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
6-70 |
5.18e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 5.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796428067 6 LKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGE 70
Cdd:cd03240 1 IDKLSIRNIRSFHErSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIRE 66
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
6-56 |
6.97e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 6.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2796428067 6 LKKLILKNFKKIQDLT-VEFTDKNTFICGGNGTGKTTLQDAFLWLLfGKDST 56
Cdd:cd03278 1 LKKLELKGFKSFADKTtIPFPPGLTAIVGPNGSGKSNIIDAIRWVL-GEQSA 51
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
242-324 |
8.72e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 242 IADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIgnkklaKSQrENEIRQnANKSYHDVLDNISKLEYQVKSKDAEIS 321
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQL------KKQ-EEAISQ-ASRKLRETQNTLNQLNKQIDELNASIA 113
|
...
gi 2796428067 322 RKQ 324
Cdd:PRK11637 114 KLE 116
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
246-510 |
1.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 246 KEKIKDIDSQLADKSKQIeaefkakSELQKQIG-NKKLAKSQRE--NEIRQNANKSYHDVLDNIskleyqvKSKDAEISR 322
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKI-------DHIQQQIKtYNKNIEEQRKknGENIARKQNKYDELVEEA-------KTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 323 KQEEHSRIKANIEALNNDLEVLRGKFYAIDA--ETLQ-----YPEGAfICPTCKRELEVEDiqAKQQELQDNfNLNKANR 395
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSkiEQFQkvikmYEKGG-VCPTCTQQISEGP--DRITKIKDK-LKELQHS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 396 LKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKgnmpeeqDTQKIIlsdptwlslsneivdleNQL 475
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK-------KVKAAI-----------------EEL 370
|
250 260 270
....*....|....*....|....*....|....*
gi 2796428067 476 KAEaKPIDTTELKEAKATLSEAIDELNKKLGKRDT 510
Cdd:PHA02562 371 QAE-FVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
6-558 |
1.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRadtnfnIKTLGEDGKPIL-------HL 78
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEK------IEDMIKKGKNNLevelefrIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 79 VHSVTGVLSINGRDVELQRN-YVEKWGSGVNAGVLQ----------NHATEFYLNGVKLKtKKEYDAEVAAILPE--DVF 145
Cdd:PRK01156 77 GHVYQIRRSIERRGKGSRREaYIKKDGSIIAEGFDDttkyieknilGISKDVFLNSIFVG-QGEMDSLISGDPAQrkKIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 146 RMITNplyfptMKAQDQKAMLLEMAGNVTNEEVANINPKFQELISLISgrTLEQLAKEIASKKSAIKDELKGIPGRIDSV 225
Cdd:PRK01156 156 DEILE------INSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNL--ELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 226 RDAMPES-------EDWAVLEKEIADKKEKIKDIDSQLADKSKQIeAEFKAKSELQKQIGNKKLAKSQreNEIRQnanks 298
Cdd:PRK01156 228 NNAMDDYnnlksalNELSSLEDMKNRYESEIKTAESDLSMELEKN-NYYKELEERHMKIINDPVYKNR--NYIND----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 299 YHDVLDNISKLEYQVKSKDAEISRKQEEHSRIkANIEALNNDLEVLRGKFYAIDAETLQYPEGAFICPTCKRELE----- 373
Cdd:PRK01156 300 YFKYKNDIENKKQILSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIEslkkk 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 374 VEDIQAKQQELQDNFNLNKANRL---KAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINE---------C 441
Cdd:PRK01156 379 IEEYSKNIERMSAFISEILKIQEidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvC 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 442 KGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKA-EAKPIDTTELKE--AKATLSEAIDELNKKLGKRDTIERSNKVI 518
Cdd:PRK01156 459 GTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDiDEKIVDLKKRKEylESEEINKSINEYNKIESARADLEDIKIKI 538
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2796428067 519 EDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLMERIN 558
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS 578
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
238-552 |
2.13e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFK-AKSELQKQIGNKKLAKSQR------------ENEIRQNANKSYH-DVL 303
Cdd:pfam13166 101 LKKEIKDHEEKLDAAEANLQKLDKEKEKLEAdFLDECWKKIKRKKNSALSEalngfkyeanfkSRLLREIEKDNFNaGVL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 304 DNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLR---GKFYAIDaETLQYP--------------EGAFICP 366
Cdd:pfam13166 181 LSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQkviGKSSAIE-ELIKNPdladwveqglelhkAHLDTCP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 367 TCKRELEvediQAKQQELQDNFNlnkaNRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMP 446
Cdd:pfam13166 260 FCGQPLP----AERKAALEAHFD----DEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 447 EEQDTQKiilsdptwlslSNEIVdLENQLKAEAKPIDTTELKEAKATLSEAIDELNkklgkrDTIERSNKVIEDLEDRRD 526
Cdd:pfam13166 332 VLNSQLD-----------GLRRA-LEAKRKDPFKSIELDSVDAKIESINDLVASIN------ELIAKHNEITDNFEEEKN 393
|
330 340
....*....|....*....|....*.
gi 2796428067 527 KNNEALaEQERLEFLVQDFQKEKDNK 552
Cdd:pfam13166 394 KAKKKL-RLHLVEEFKSEIDEYKDKY 418
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
236-353 |
2.35e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 236 AVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEiRQNANKSYHDVLDNISKLEYQVKS 315
Cdd:PRK09039 42 FFLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAE-RSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 2796428067 316 KDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDA 353
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEA 158
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-561 |
2.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 197 LEQLAKEIASKKSAIKdELKGIPGRIDSVRDAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQ 276
Cdd:PRK03918 261 IRELEERIEELKKEIE-ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 277 IG--NKKLAKSQRENEIRQNANKSYHDV---LDNISKLEYQVKSKDAE-ISRKQEEHSRIKANIEALNNDLEVLRGKFYA 350
Cdd:PRK03918 340 LEelKKKLKELEKRLEELEERHELYEEAkakKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 351 IDAE---TLQYPEGA-FICPTCKRELEVEDiqakQQELQDNFNLnkanRLKAVQNEGKEKAAKVEELKKQCSIIQATITQ 426
Cdd:PRK03918 420 EIKElkkAIEELKKAkGKCPVCGRELTEEH----RKELLEEYTA----ELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 427 LSN--------------EKEILVHNINECKGNMPE-EQDTQKIILSDPTWLSLS---NEIVDLENQLKAEAKPIDTTE-- 486
Cdd:PRK03918 492 ESEliklkelaeqlkelEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEee 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 487 LKEAKATLSE----AIDELNKKLG------------------KRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFLVQD 544
Cdd:PRK03918 572 LAELLKELEElgfeSVEELEERLKelepfyneylelkdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
410
....*....|....*..
gi 2796428067 545 FQKEKDNKLMERINGMF 561
Cdd:PRK03918 652 LEKKYSEEEYEELREEY 668
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
237-409 |
2.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 237 VLEKEIADKKEKIKDI--DSQLADKSKQIEAEFKAKSELQKQignkklaKSQRENEIRQNANKsyhdvldnISKLEYQVK 314
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIleEAKKEAEAIKKEALLEAKEEIHKL-------RNEFEKELRERRNE--------LQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 315 SKDAEISRKQEEHSRIKANIEALNNDLEVLRgkfyaidaETLQypegaficptcKRELEVEDIQAKQ-QELQDNFNLN-- 391
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQ--------QELE-----------KKEEELEELIEEQlQELERISGLTae 153
|
170 180
....*....|....*....|
gi 2796428067 392 --KANRLKAVQNEGKEKAAK 409
Cdd:PRK12704 154 eaKEILLEKVEEEARHEAAV 173
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
279-538 |
2.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 279 NKKLAKSQRENEIRQNANKSYHDVLDnisKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIdaETLqy 358
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDLHERLN---GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL--ETL-- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 359 pegaficptckrELEVEDIQAKQQELQ---DNFnlnkANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILV 435
Cdd:PRK02224 257 ------------EAEIEDLRETIAETErerEEL----AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 436 HNINECKGNMPEEQDTQKIILSDPTwlSLSNEIVDLENQ---LKAEAKPIDtTELKEAKATLS---EAIDELNKKLgkRD 509
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAE--SLREDADDLEERaeeLREEAAELE-SELEEAREAVEdrrEEIEELEEEI--EE 395
|
250 260
....*....|....*....|....*....
gi 2796428067 510 TIERSNKVIEDLEDRRDKNNEALAEQERL 538
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDEL 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-347 |
3.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 195 RTLEQLAKEIASKKSAIKDELKGIPGRIDS---VRDAMPESEDWAVLEKEIADKKEKIKDIDS------QLADKSKQIEA 265
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREAlqrLAEYSWDEIDVASAEREIAELEAELERLDAssddlaALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 266 EFKaksELQKQIGNKKLAKSQRENEIRQNAN--KSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANI-EALNNDLE 342
Cdd:COG4913 700 ELE---ELEEELDELKGEIGRLEKELEQAEEelDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELrENLEERID 776
|
....*
gi 2796428067 343 VLRGK 347
Cdd:COG4913 777 ALRAR 781
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
236-544 |
6.28e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 236 AVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQNANKSYHDVLDNISKLEYQVKS 315
Cdd:pfam12128 607 DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 316 KDAEisRKQEEHsRIKANIEALNNDLEVLRGKfyaiDAETLQYPEGAFicpTCKRELEVEDIQAKQQelqdnfnlNKANR 395
Cdd:pfam12128 687 LEAQ--LKQLDK-KHQAWLEEQKEQKREARTE----KQAYWQVVEGAL---DAQLALLKAAIAARRS--------GAKAE 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 396 LKAVQNEGKekaakvEELKKQcSIIQATITQLSNEKEILVHNINECKGNMPEeqdtqkiILSDPTWLslsNEIVDLENQl 475
Cdd:pfam12128 749 LKALETWYK------RDLASL-GVDPDVIAKLKREIRTLERKIERIAVRRQE-------VLRYFDWY---QETWLQRRP- 810
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796428067 476 kaeakpidttELKEAKATLSEAIDELNKKLGK--------RDTIERSNKVIEDLEDRRDKNNEAL-AEQERLEFLVQD 544
Cdd:pfam12128 811 ----------RLATQLSNIERAISELQQQLARliadtklrRAKLEMERKASEKQQVRLSENLRGLrCEMSKLATLKED 878
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
238-533 |
8.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIrQNANKSYHDVLDNISKLEYQVKSKD 317
Cdd:COG4372 64 LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQypegaficpTCKRELEVEDIQAKQQELQDNFNLNKANRLK 397
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE---------QALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 398 AVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKA 477
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2796428067 478 EAKPIDTTELKEAKATLSEAIDELNKKLGKRDTIERSNKVIEDLEDRRDKNNEALA 533
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
205-557 |
9.53e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 205 ASKKSAIKDELKGIPGR--IDSVRDAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKL 282
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 283 AKSQRENEIRQNANKSYHdvLDNISKlEYQVKSKDAEISRKQEEHSR---IKANIEALNNDLEVLRGKFYA-IDAETLQY 358
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKK--AEEAKK-KAEEAKKADEAKKKAEEAKKadeAKKKAEEAKKKADEAKKAAEAkKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 359 PEGAFICPTCKRELEVE--DIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEI-LV 435
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeEV 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 436 HNINECKGNMPEEQDTQKiilsdptwlslSNEIVDLENQLKAEAKPIDTTELKEAKATLSEAIDELnKKLGKRDTIERSN 515
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKA-----------EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAE 1665
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2796428067 516 KVIEDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLMERI 557
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
238-555 |
9.59e-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: 39.23 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIrQNANKSYHDVLDNISKLEYQVKSKD 317
Cdd:TIGR04523 73 SNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVEL-NKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQYPEGAFicptcKRELEVEDIQAKQQElqDNFNLNKANRLK 397
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-----KLELLLSNLKKKIQK--NKSLESQISELK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 398 AVQNE-GKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPE-EQDTQKIILSDPTWLSLSNEIVDLENQL 475
Cdd:TIGR04523 225 KQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKElEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 476 KAEAkpidTTELKEAKATLSEAIDELNKKLGKRD-TIERSNKVIEDLE-DRRDKNNEALAEQERLE---FLVQDFQKEKD 550
Cdd:TIGR04523 305 EQDW----NKELKSELKNQEKKLEEIQNQISQNNkIISQLNEQISQLKkELTNSESENSEKQRELEekqNEIEKLKKENQ 380
|
....*
gi 2796428067 551 NKLME 555
Cdd:TIGR04523 381 SYKQE 385
|
|
|