|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
196-485 |
6.07e-114 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 340.52 E-value: 6.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 196 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqihdvegrym 266
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 267 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 346
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 347 DELKEGLRQRDELIEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKL 426
Cdd:pfam09738 166 AELKEQLKQRDELIEKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 427 KLQLEEERQ-KCSRNDGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 485
Cdd:pfam09738 246 KLQLEEEKSkRNSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
307-560 |
9.79e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 307 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMDELKEGLRQRDELIEKHGLVIipdstpngdv 377
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAEL---------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 378 hhepvvgaitAVSQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQ 457
Cdd:COG1196 256 ----------EELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 458 FIEMQR---DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEE 534
Cdd:COG1196 325 LAELEEeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260
....*....|....*....|....*.
gi 1907200293 535 MEMTNSHLAKRLEKMKANRTALLAQQ 560
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEAL 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-535 |
1.22e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 246 SELRDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 325
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 326 EEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIekhglviipDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpl 405
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEA---------ANLRERLESLERRIAATERRLEDLEEQIEELSE--- 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 406 dvRLRKLAGEKDELLSQIRKLKLQLEE-ERQKCSRNDGMSGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQD 482
Cdd:TIGR02168 853 --DIESLAAEIEELEELIEELESELEAlLNERASLEEALALLRSELEElSEELRELESKRsELRRELEELREKLAQLELR 930
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907200293 483 IATLEQSISRLEGQVL-RYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 535
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-559 |
7.82e-07 |
|
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: 52.38 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 270 KELKESLSEVEEKYKKamvsnaqLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDEL 349
Cdd:TIGR02169 670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 350 KEGLRQRDELIEkhglviipdstpNGDVHHEPVVGAITAVSQEAAQV---LESAGEGPLDVRLRKLAGEKDELLSQIRKL 426
Cdd:TIGR02169 743 EEDLSSLEQEIE------------NVKSELKELEARIEELEEDLHKLeeaLNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 427 KLQLEEERQKCSRNDgmsgdlaglqngSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAE 505
Cdd:TIGR02169 811 EARLREIEQKLNRLT------------LEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907200293 506 NAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 559
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
249-536 |
1.11e-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: 51.61 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 249 RDIYDLKDQIHDVEGRY-MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMaefyRENEE 327
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR----IDLKE 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 328 KSKELERQkhmcsvlqhkMDELKEGLRQRDELIEKHglviipdstpngdvhhepvvgaitavsqeAAQVLEsagegpLDV 407
Cdd:TIGR02169 848 QIKSIEKE----------IENLNGKKEELEEELEEL-----------------------------EAALRD------LES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 408 RLRKLAGEKDELLSQIRKLKL---QLEEERQKcsRNDGMSGDLAGLQNGSD-LQFIEMQRDANRQISEYKFKLSKAEQDI 483
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLSELKAKLEALEEeLSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907200293 484 ATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 536
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
242-533 |
1.17e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 242 DTSLSELRDIYDLKDQIHDVEGRY---MQGLKELKESLSEVEEKYKKA-----MVSNAQLDNEK--------NNLIYQVD 305
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQEKieryqadlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 306 TLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKE---GLRQRDELIEK-HGLVIIPDSTPNG--DVHH 379
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERaKQLCGLPDLTADNaeDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 380 EpvvgaITAVSQEAAQVLESAgEGPLDVR-------------LRKLAGEKD--ELLSQIRKLKLQLEEERQKCSRNDGMS 444
Cdd:PRK04863 446 E-----FQAKEQEATEELLSL-EQKLSVAqaahsqfeqayqlVRKIAGEVSrsEAWDVARELLRRLREQRHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 445 GDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAE 517
Cdd:PRK04863 520 MRLSELE-----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQAR 594
|
330
....*....|....*....
gi 1907200293 518 RRKLQR---ELRTAQDKIE 533
Cdd:PRK04863 595 IQRLAArapAWLAAQDALA 613
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
269-559 |
1.93e-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: 50.83 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 269 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 348
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 349 LKEGLRQRDELIEKHGLVIIPDSTpngdvhhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLKL 428
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEA------------EIEELEAQIEQLKEELKA--LREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 429 QLEEERQKCSRNDGMSGDLAglQNGSDLQfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAE 508
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLE--EQIEELS--EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907200293 509 KIEDELKAERRKLQRELRTAQDKIEEMEMtnshlakRLEKMKANRTALLAQ 559
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLEL-------RLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
245-557 |
3.08e-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: 50.45 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 245 LSELRD-IYDLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyr 323
Cdd:TIGR02169 704 LDELSQeLSDASRKIGEIEKE----IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-- 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 324 enEEKSKELERqkhmcSVLQHKMDELKEGLRQRDELIEKhglviipdstpngdvhhepvvgaITAVSQEAAQVLESageg 403
Cdd:TIGR02169 778 --EEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSR-----------------------IEARLREIEQKLNR---- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 404 pLDVRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQN------GSDLQFIEMQRDANRQISEYKFKLS 477
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEeleeleAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 478 KAEQDIATLEQSISRLEGQVLRYKTAAENAEK--------------------IEDELKAERRKLQRELRT-------AQD 530
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEelseiedpkgedeeipeeelSLEDVQAELQRVEEEIRAlepvnmlAIQ 979
|
330 340
....*....|....*....|....*..
gi 1907200293 531 KIEEMEMTNSHLAKRLEKMKANRTALL 557
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
292-560 |
4.34e-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: 49.67 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 292 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRENEEKSKELERqkhmcSVLQHKMDELKEGLRQRDELIEK 362
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKELKAELRELEL-----ALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 363 hglviipdstpNGDVHHEPVVGAitAVSQEAAQVLESAgEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKcsrndg 442
Cdd:TIGR02168 251 -----------AEEELEELTAEL--QELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRER------ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 443 msgdLAGLQNgsDLQFIEMQRDAN-RQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDEL------- 514
Cdd:TIGR02168 311 ----LANLER--QLEELEAQLEELeSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletl 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907200293 515 KAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 560
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-551 |
1.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 405 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCsrnDGMSGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 483
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200293 484 ATLEQSI-----------SRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 551
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
405-559 |
2.39e-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: 46.07 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 405 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 479
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 480 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 554
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 1907200293 555 ALLAQ 559
Cdd:COG1579 167 ELAAK 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-536 |
2.60e-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: 47.36 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 255 KDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN-------NLIYQVDTLKDVIEEQEEQMAEFYRENEE 327
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 328 KSKELERqkhmcsvLQHKMDELKEGLRQRDELIEKhglviipdstpngdvhHEPVVGAITAVSQEAAQVLESAGEGP--L 405
Cdd:TIGR02168 321 LEAQLEE-------LESKLDELAEELAELEEKLEE----------------LKEELESLEAELEELEAELEELESRLeeL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 406 DVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEqdIAT 485
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLER-----------LEDRRERLQQEIEELLKKLEEAELKELQAE--LEE 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907200293 486 LEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 536
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-535 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 256 DQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQ---MAEFYRENEEKSKEL 332
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESL 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 333 ERQKHMCSVLQHKMDELKEGLRQRDELIEKHglviIPDSTPNGDVHHEPVVGA--ITAVSQEAAQVLESAGEGpLDVRLR 410
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALlnERASLEEALALLRSELEE-LSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 411 KLAGEKDELLSQIRKLKLQLEEERQKCSrndGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSI 490
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907200293 491 SRLeGQV-LRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 535
Cdd:TIGR02168 982 KEL-GPVnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
267-507 |
3.29e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 267 QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 346
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 347 DELKEGLRQRDELIEKHG-----LVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKLAGEKDELLS 421
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 422 QIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYK 501
Cdd:COG4942 175 ELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*.
gi 1907200293 502 TAAENA 507
Cdd:COG4942 241 ERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
405-559 |
4.63e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 405 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIA 484
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAE 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200293 485 TLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 559
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
269-560 |
1.17e-04 |
|
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: 45.04 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 269 LKELKESLSEVEEKYKKAMvsnAQLDNEKNNLIYQvdTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 348
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQA---AKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 349 LKEGLRQRDELIEKHGLVIIPDSTPNGDVHHepvvgAITAVSQEAAQVLesagegPLDVRLRKLAGEKDELLSQI----R 424
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQS-----LIREIKDAKEQDS------PLETFLEKDQQEKEELISSKetsnK 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 425 KLKLQLEEERQKCSRNDGMSGDLAG-LQNGSDLQFIEMQRDANR---QISEYKFKLSKAEQDIATLEQSISRlEGQVLRY 500
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDYLKQKETELNTvnaQLEECEKHQEKINEDMRLMRQDIDT-QKIQERW 1016
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200293 501 KTAAENAEKIEDELKAERRKLQRELR-TAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 560
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKeMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ 1077
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-556 |
1.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 270 KELKESLSEVEEKykkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDEL 349
Cdd:TIGR02169 214 QALLKEKREYEGY---------ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 350 KEG--LRQRDELIEKHGLViipdstpngdvhhEPVVGAITAVSQEAAQvlesagegpLDVRLRKLAGEKDELLSQIRKLK 427
Cdd:TIGR02169 285 GEEeqLRVKEKIGELEAEI-------------ASLERSIAEKERELED---------AEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 428 LQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSK---------------------AE 480
Cdd:TIGR02169 343 REIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKlkreinelkreldrlqeelqrLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 481 QDIATLEQSISRLEGQVLRYKTAAENA----EKIEDELK---AERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANR 553
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
...
gi 1907200293 554 TAL 556
Cdd:TIGR02169 500 RAS 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
269-560 |
2.73e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 269 LKELKESLSEVEEkykkamvsnaqldneknnliyQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDE 348
Cdd:COG1196 255 LEELEAELAELEA---------------------ELEELRLELEELELELEEAQAEEYELLAELARLE---QDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 349 LKEGLRQRDELIEKHglviipdstpngdvhhepvvgaitavsQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKLKL 428
Cdd:COG1196 311 RRELEERLEELEEEL---------------------------AELEEELEELEE-----ELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 429 QLEEERQKCSRNDGMSGDLAGLQngsdLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAE 508
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEEL----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907200293 509 KIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 560
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
408-553 |
6.07e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 408 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 480
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200293 481 QDIATLEQSISRLEGQVlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEmemtnsHLAKRLEKMKANR 553
Cdd:COG1579 124 EELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
463-551 |
9.81e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 463 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaerRKLQRELRTAQDKIEEMEMTNSHL 542
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491
|
....*....
gi 1907200293 543 AKRLEKMKA 551
Cdd:COG2433 492 KRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
465-560 |
1.13e-03 |
|
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: 41.29 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 465 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAK 544
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 1907200293 545 RLEKMKAnrtaLLAQQ 560
Cdd:COG4942 98 ELEAQKE----ELAEL 109
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
413-559 |
1.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 413 AGEKDELLSQIRKLKLQLEEERQKCSRNDGmsgdlagLQNGSDLQFIEMQRDANRQiseykfKLSKAEQDIATLEQSISR 492
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA------ELEELRAELARLEAELER 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200293 493 LEGQvlryktaaenaekiEDELKAERRKLQRELRTAQ-DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 559
Cdd:COG4913 314 LEAR--------------LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
465-534 |
1.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 465 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEE 534
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-559 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 405 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFklskAEQDIA 484
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQE--------------------------RREALQRLAEYSW----DEIDVA 664
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200293 485 TLEQSISRLEGQvlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 559
Cdd:COG4913 665 SAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
240-536 |
2.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 240 DPDTSLSELRDIYDLKDQ--IHDVEGRYMQGLKELKESLSEVEEKYKKAmvsnaqldneknnlIYQVDTLKDVIEEQEEQ 317
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQA--------------RETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 318 MAEF------YRENEEKSKELERQKhmcsvlqhkmDELKEGLRQRDELIEKHGlviipdstpngdvhhepvvGAITAVSQ 391
Cdd:PRK02224 250 REELetleaeIEDLRETIAETERER----------EELAEEVRDLRERLEELE-------------------EERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 392 EAAqvLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGlqNGSDLQfiEMQRDANRQISE 471
Cdd:PRK02224 301 EAG--LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE--RAEELR--EEAAELESELEE 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200293 472 YKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAER-------RKLQRELRTAQDKIEEME 536
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdelrereAELEATLRTARERVEEAE 446
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
244-550 |
2.19e-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: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 244 SLSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVE------EKYKKamvSNAQLDNEKNNLIYQVDTLKDVIEEQEE 316
Cdd:TIGR04523 336 IISQLNEqISQLKKELTNSESENSEKQRELEEKQNEIEklkkenQSYKQ---EIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 317 QMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKhglviipdstpngdvhhepvvgaitavsqeaaqv 396
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN---------------------------------- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 397 lesagegpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglQNGSDLQfiEMQRDANRQISEYKFKL 476
Cdd:TIGR04523 459 --------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN--EEKKELE--EKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200293 477 SKAEQDIATLEQSISRLEgqvlryktaaENAEKIEDELKaeRRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 550
Cdd:TIGR04523 527 EKLESEKKEKESKISDLE----------DELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ 588
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
386-560 |
2.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 386 ITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCS-------RNDGMSGDLAGLQNGSDLQ- 457
Cdd:COG3883 39 LDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 458 FIE-------MQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQD 530
Cdd:COG3883 117 FLDrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|
gi 1907200293 531 KIEEMEMTNSHLAKRLEKMKANRTALLAQQ 560
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
463-535 |
2.97e-03 |
|
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: 40.13 E-value: 2.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200293 463 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 535
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-560 |
3.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 408 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAglQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDIATL 486
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELE--QARSELEQLEEElEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200293 487 EQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 560
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
303-535 |
3.82e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 303 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQkhmcSVLQhKMDELKEGLRQ-RDELIEKHGLViipdstpngdvhhEP 381
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSEEAK----LLLQ-QLSELESQLAEaRAELAEAEARL-------------AA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 382 VVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLS-------QIRKLKLQLEEERQkcsrndgmsgdlaglqngs 454
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRA------------------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 455 dlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKtaaenaekiedELKAERRKLQRELRTAQDKIEE 534
Cdd:COG3206 306 -----QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP-----------ELEAELRRLEREVEVARELYES 369
|
.
gi 1907200293 535 M 535
Cdd:COG3206 370 L 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
460-558 |
3.83e-03 |
|
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: 39.75 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 460 EMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtn 539
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90
....*....|....*....
gi 1907200293 540 shlaKRLEKMKANRTALLA 558
Cdd:COG4942 97 ----AELEAQKEELAELLR 111
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
311-548 |
4.15e-03 |
|
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: 40.09 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 311 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKHGLViipdstpngdvhhEPVVGAITAVS 390
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-------------EKIAEELKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 391 QEAAQVLESAGE--GPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgmsgdlagLQNGSDLQFIEmQRDANRQ 468
Cdd:pfam05483 439 QELIFLLQAREKeiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE----------LTAHCDKLLLE-NKELTQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 469 ISEYKFKLSKAEQDIATLEQSISRLEGQVlryKTAAENAEKIEDELKAERRKLQR---ELRTAQDKIEEMEMTNSHLAKR 545
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQI---ENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLK 584
|
...
gi 1907200293 546 LEK 548
Cdd:pfam05483 585 KEK 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
245-549 |
4.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 245 LSELRD-IYDLKDQIHDVEGRYmQGLKELKESLSEVEEKYKKamvsnaqLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyR 323
Cdd:PRK03918 209 INEISSeLPELREELEKLEKEV-KELEELKEEIEELEKELES-------LEGSKRKLEEKIRELEERIEELKKEIEEL-E 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 324 ENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKhglviipdstpngdvhhepvvgaitaVSQEAAQVLESAGEG 403
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR--------------------------LEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 404 PLDV-RLRKLAGEKDELLSQIRKLK---LQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKA 479
Cdd:PRK03918 334 EEKEeRLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKI 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200293 480 EQDIATLEQSISRLEGQVLRYKTAAE-----NAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 549
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
385-528 |
5.34e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 385 AITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRD 464
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200293 465 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKiEDELKAERRKLQRELRTA 528
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLL 252
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
293-524 |
6.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 293 LDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKElerqkHMCSVLQHKMDELkeglRQRDELIEkhglVIIPDST 372
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE-----LVEEAKTIKAEIE----ELTDELLN----LVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 373 PNGdvhhepvvgAITAVSQEAAQV-------------LESAGEGPL--------DVRLRKLAGEKDELLSQIRKLKLQLE 431
Cdd:PHA02562 253 PSA---------ALNKLNTAAAKIkskieqfqkvikmYEKGGVCPTctqqisegPDRITKIKDKLKELQHSLEKLDTAID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 432 EERQKCSrndgmsgdlaglqngsdlQFIEMQR---DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAE 508
Cdd:PHA02562 324 ELEEIMD------------------EFNEQSKkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
250
....*....|....*.
gi 1907200293 509 KIEDELKAERRKLQRE 524
Cdd:PHA02562 386 DELDKIVKTKSELVKE 401
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
244-542 |
6.74e-03 |
|
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: 39.64 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 244 SLSELRDIYDLKDQIHDVEGRYmqgLKELKESLSEVEEKYkkaMVSNAQLDNEKN---NLIYQVDTLKDVIEEQEEQMAE 320
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKY---LKQYKEKACEIRDQI---TSKEAQLESSREivkSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 321 FYRENEE----KSKELERQKhMCSVLQHKMDELKEGL-RQRDELIEKHGLVIIPDSTPNGDVHHEpvvgaITAVSQEAaq 395
Cdd:TIGR00606 264 IMKLDNEikalKSRKKQMEK-DNSELELKMEKVFQGTdEQLNDLYHNHQRTVREKERELVDCQRE-----LEKLNKER-- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 396 vlesagegpldvrlRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRQISEY-KF 474
Cdd:TIGR00606 336 --------------RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSL---IQSLATRLELDGFERGPFSERQIKNFhTL 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200293 475 KLSKAEQDIATLEQSISRLEGQVlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHL 542
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCADLQSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-525 |
8.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 242 DTSLSELRD-IYDLKDQIHDVEGRYMqglkELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 320
Cdd:COG1196 266 EAELEELRLeLEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 321 FYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKHglviipdstpngdvhhepvvgAITAVSQEAAQVLESA 400
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL---------------------AEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200293 401 GEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgmSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAE 480
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE----EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907200293 481 QDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQREL 525
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| |
