|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
319-673 |
1.59e-102 |
|
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: 317.02 E-value: 1.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 319 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqihdvegrym 389
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 390 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 469
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 470 DELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdkalgalekqkehiaclrnerdvlreeladlrqtvttaE 549
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 550 KHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQ-KCSRN 628
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755532231 629 DGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 673
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-723 |
1.50e-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: 68.16 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHkmdE 471
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK---E 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKh 551
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 552 glviipdstpngdvHHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQI-RKLKLQLEEERQKCSRNDG 630
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELeALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 631 MSgDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDIATLEQSISRlegqvlRYKTAAENAEKIEDELKAERR 707
Cdd:TIGR02168 896 LE-ELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 755532231 708 KLQRELRTAQDKIEEM 723
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-724 |
8.15e-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: 62.39 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 349 NSSRRGSGDTSSliDPDTSLSELRDIYDLKDQIHDVegryMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVD 428
Cdd:TIGR02169 660 RAPRGGILFSRS--EPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 429 TLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLR--QRDELIEENQRLQQKVDTMTKEVFDLQET 506
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 507 LLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhEPVVGAITAVSQEAAQVle 586
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI------------------ENLNGKKEELEEELEEL-- 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 587 SAGEGPLDVRLRKLAGEKDELLSQIRKLKL---QLEEERQKcsRNDGMSGDLAGLQNGSD-LQFIEMQRDANRQISEYKF 662
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLSELKAKLEALEEeLSEIEDPKGEDEEIPEEEL 951
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532231 663 KLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 724
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-723 |
1.16e-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: 62.00 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 369 SELRDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 448
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 449 EEKSKELERQKHMCSVLQHKMDELkeglrqRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLR 528
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDEL------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 529 NERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgaITAVSQEAAQVLESAGEGpLDVRLRKLAGEKDELL 608
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLN-----------------------ERASLEEALALLRSELEE-LSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 609 SQIRKLKLQLEEERQKCSrndGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLeGQV-LR 687
Cdd:TIGR02168 915 RELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL-GPVnLA 990
|
330 340 350
....*....|....*....|....*....|....*.
gi 755532231 688 YKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 723
Cdd:TIGR02168 991 AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-724 |
9.85e-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: 58.91 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 415 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRE--NEEKS--------------KELERQKHMCSVLQHKM 469
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKElkAELRElelallvlrleelrEELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 470 DELKEGLRQRDELIEENQRLQQKVDtmtKEVFDLQETLLWKDKALGALEKQKEH------------------IACLRNER 531
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQIlrerlanlerqleeleaqLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 532 DVLREELADLRQTVTTAEKhglviipdstpngdvHHEPVVGAITAvSQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQI 611
Cdd:TIGR02168 333 DELAEELAELEEKLEELKE---------------ELESLEAELEE-LEAELEELESRLEE-LEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 612 RKLKLQLEEERQKCSRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEqdIATLEQSISRLEGQVLRYKTA 691
Cdd:TIGR02168 396 ASLNNEIERLEARLER-----------LEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEA 462
|
330 340 350
....*....|....*....|....*....|...
gi 755532231 692 AENAEKIEDELKAERRKLQRELRTAQDKIEEME 724
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-736 |
1.57e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 368 LSELRDIYDLKDQIHDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 447
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 448 NEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWkdKALGALEKQKEHIACL 527
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 528 RNERDVLREELADLRQTVTTAEKHGlviipDSTPNGDVHHEP------------VVGAITAVSQEAAQVLESAGE----- 590
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEL-----EQLENELEAAALeerlkearllllIAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 591 ----GPLDVRLRKLAGEKDELLSQIRKLKLQLEEERqkcSRNDGMSGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSK 666
Cdd:COG4717 280 flvlGLLALLFLLLAREKASLGKEAEELQALPALEE---LEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532231 667 AEQDIATLEQSISRLEGQVLRYKTAAENAEKIED--ELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 736
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
465-747 |
1.60e-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: 58.16 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 465 LQHKMDELKeglRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGAL----EKQKEHIACLRNERDVLREELAD 540
Cdd:TIGR02169 679 LRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 541 LRQTVTTAEKhglviipdstpngdvhhepVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEE 620
Cdd:TIGR02169 756 VKSELKELEA-------------------RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 621 ERQKCSRNDgmsgdlaglqngSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIE 699
Cdd:TIGR02169 817 IEQKLNRLT------------LEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755532231 700 DELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 747
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
430-748 |
8.09e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 430 LKDVIEEQEEQMaefyreneeksKELERQkhmcSVLQHKMDELKEGLRQRDelieenqrlqqkvdtmtkevfdLQETLLW 509
Cdd:COG1196 191 LEDILGELERQL-----------EPLERQ----AEKAERYRELKEELKELE----------------------AELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 510 KDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAVSQEAAQVLESAG 589
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------------------LELEELELELEEAQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 590 EgpldvRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQngsdlqfiEMQRDANRQISEYKFKLSKAEQ 669
Cdd:COG1196 288 A-----EEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELE--------EELEELEEELEELEEELEEAEE 351
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 670 DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 748
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
376-739 |
1.17e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 376 DLKDQI--------HDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 444
Cdd:PRK02224 191 QLKAQIeekeekdlHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 445 YRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQ---- 520
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE---AVEARREELEDRDEELRDRLEECRVAAQAHNEEaesl 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 521 KEHIACLRNERDVLREELADLRQTVTTAEkhglVIIPDSTpngdvhhepvvGAITAVSQEAAQVLESAGEGPLDV----- 595
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAR----EAVEDRR-----------EEIEELEEEIEELRERFGDAPVDLgnaed 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 596 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDIATLE 675
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEAL---LEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532231 676 QSISRLEGQVLRYKTAAENAEKIEDelKAERRKLQRELR-TAQDKIEEMEMTNSHLAKRLEKMKA 739
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
446-695 |
2.39e-07 |
|
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: 53.61 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 446 RENEEKSKELERQkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHia 525
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 526 cLRNERDVLREELADLRQTVTTAEKHG--LVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKLAGE 603
Cdd:COG4942 95 -LRAELEAQKEELAELLRALYRLGRQPplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 604 KDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEG 683
Cdd:COG4942 169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 755532231 684 QVLRYKTAAENA 695
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
365-721 |
3.78e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 365 DTSLSELRDIYDLKDQIHDVEGRY---MQGLKELKESLSEVEEKYKKA-----MVSNAQLDNEKnnlI--YQVDTLKdvI 434
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQEK---IerYQADLEE--L 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 435 EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTmtkevfdLQETLLWK 510
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARA---EAAEEEVDELKSQLADYQQALDVQQTraiqYQQAVQA-------LERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 511 DKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAVSQEAAQVLESage 590
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ--------------------------AAHSQFEQAYQL--- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 591 gpldvrLRKLAGEKD--ELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAE 668
Cdd:PRK04863 482 ------VRKIAGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532231 669 QDIATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAERRKLQR---ELRTAQDKIE 721
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQARIQRLAArapAWLAAQDALA 613
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
376-724 |
8.88e-07 |
|
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: 52.33 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 376 DLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 455
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 456 ERQKHMCSVLQHKMDELKEGLRQRDELIEEnqrLQQKVDTMTKEVFDLQETllwkdkalgaLEKQKEHIACLRNERDVLR 535
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKK---LQQEKELLEKEIERLKET----------IIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 536 EELADLRQTvTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLK 615
Cdd:TIGR04523 454 LIIKNLDNT-RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKIEKLE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 616 LQLEEERQKCSRndgMSGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDIATLEQSISRLEGQVLR 687
Cdd:TIGR04523 531 SEKKEKESKISD---LEDELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIKEIEE 607
|
330 340 350
....*....|....*....|....*....|....*..
gi 755532231 688 YKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 724
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
369-748 |
9.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 369 SELRDIYDLKDQIHDVEgrymQGLKELKESLSEVEEKYKK--AMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEfYR 446
Cdd:COG4717 85 EKEEEYAELQEELEELE----EELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEE-LR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 447 ENEEKSKELERQKHMcsvLQHKMDELKEGLRQRDE-----LIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQK 521
Cdd:COG4717 160 ELEEELEELEAELAE---LQEELEELLEQLSLATEeelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 522 EHIAclrnerdvLREELADLRQT-VTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAV--------SQEAAQVLESAGEGP 592
Cdd:COG4717 237 EAAA--------LEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 593 LDVRLRKLAGEK-------------------DELLSQIRKLKL------QLEEERQKCSRNDGMSGDLAGLQNGSDLQFI 647
Cdd:COG4717 309 ALPALEELEEEEleellaalglppdlspeelLELLDRIEELQEllreaeELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 648 EMQRDANRQIseykfklsKAEQDIATLEQSISRLEGQVLRYKTAAEnaekiEDELKAERRKLQRELRTAQDKIEEMEMTN 727
Cdd:COG4717 389 AALEQAEEYQ--------ELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREEL 455
|
410 420
....*....|....*....|.
gi 755532231 728 SHLAKRLEKMKANRTALLAQQ 748
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQ 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
510-747 |
1.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 510 KDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAVSQEAAQvlesag 589
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----------------------RIRALEQELAA------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 590 egpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQ 669
Cdd:COG4942 81 ---LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------RE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532231 670 DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 747
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-641 |
2.56e-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: 51.21 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 372 RDIYDLKDQIHDVEGRymqgLKELKESLSEVEEKYkkamvsnAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEK 451
Cdd:TIGR02168 253 EELEELTAELQELEEK----LEELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 452 SKELERQKHMCSVLQHKMDELKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKalgALEKQKEHIACLRNER 531
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEE---KLEELKEELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 532 DVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDV--RLRKLAGEKDELLS 609
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeeALEELREELEEAEQ 475
|
250 260 270
....*....|....*....|....*....|..
gi 755532231 610 QIRKLKLQLEEERQKCSRNDGMSGDLAGLQNG 641
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
442-739 |
4.33e-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: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 442 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGL----RQRDELIEENQRLQQKVDTMTKE-VFDLQETLLWKDKALGA 516
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 517 LEKQKEHIACLRNERDVLREELADLRQTVTTAEKHglviIPDSTPNGDVHHEPVVGAITA-VSQEAAQVLESAGE-GPLD 594
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERElEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 595 VRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAE 668
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532231 669 QDIATLEQSISRLEGQVLRYKTAAENAE-KIEDeLKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 739
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNaAIAG-IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
593-747 |
6.34e-06 |
|
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: 48.00 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 593 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 667
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 668 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 742
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 755532231 743 ALLAQ 747
Cdd:COG1579 167 ELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
593-739 |
8.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 593 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCsrnDGMSGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 671
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 672 ATLEQSI-----------SRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 739
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
392-736 |
1.57e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvlqhkmDE 471
Cdd:pfam07888 89 LRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK----------ER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkdkalgalEKQKEHIACLRNERDVLREELADLRQTVTTAEKH 551
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF----------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 552 glviipdstpngDVHHEPVVGAITAVsQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEerqkcsrndgM 631
Cdd:pfam07888 229 ------------EAENEALLEELRSL-QERLNASERKVEG-LGEELSSMAAQRDRTQAELHQARLQAAQ----------L 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 632 SGDLA--GLQNGSDLQFIEMQRDANRQISEY-KFKLSKAEQDIATLEQSI--SRLEGQVLRYKTAAE---------NAEK 697
Cdd:pfam07888 285 TLQLAdaSLALREGRARWAQERETLQQSAEAdKDRIEKLSAELQRLEERLqeERMEREKLEVELGREkdcnrvqlsESRR 364
|
330 340 350
....*....|....*....|....*....|....*....
gi 755532231 698 IEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 736
Cdd:pfam07888 365 ELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
392-736 |
2.93e-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: 47.41 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIE---------EQEEQMAE--FYRENEEKSKELERQKH 460
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrsmstqkalEEDLQIATktICQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 461 MCSVLQHKMDELKEGLRQRDELIE-ENQRLQQKVDTMTKEVFDLQETllwkdkalgalEKQKEHIACLRNERDVLREELA 539
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRtEQQRLEKNEDQLKIITMELQKK-----------SSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 540 DLrqtvtTAEKHGLViipdstpNGDVHHEPVVGAITAVSQEAAQVLESAGE--GPLDVRLRKLAGEKDELLSQIRKLKLQ 617
Cdd:pfam05483 412 KI-----LAEDEKLL-------DEKKQFEKIAEELKGKEQELIFLLQAREKeiHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 618 LEEERQKCSRndgmsgdlagLQNGSDLQFIEmQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVlryKTAAENAEK 697
Cdd:pfam05483 480 LEKEKLKNIE----------LTAHCDKLLLE-NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI---ENLEEKEMN 545
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 755532231 698 IEDELKAERRKLQR---ELRTAQDKIEEMEMTNSHLAKRLEK 736
Cdd:pfam05483 546 LRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
581-748 |
2.94e-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: 47.74 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 581 AAQVLESAGEG--PLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAGLQnGSDLQFIEMQRDANRQIS 658
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQ-KELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 659 EYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 738
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 755532231 739 ANRTALLAQQ 748
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
390-740 |
3.66e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 390 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 461
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 462 ------CSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEhiaclrNER 531
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE------RED 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 532 DVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEpvvgaitavSQEAAQVLESAGEgpldvrlrklagEKDellSQI 611
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLID---------LKEHASSLASSGL------------KKD---SKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 612 RKLKLQLEEERQKCSRndgMSGDLAGLQNgsdlqfIEMQRDANRQISEykfklskaeqdiatleqSISRLEGQVLRYKTA 691
Cdd:pfam10174 520 KSLEIAVEQKKEECSK---LENQLKKAHN------AEEAVRTNPEIND-----------------RIRLLEQEVARYKEE 573
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755532231 692 AENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 740
Cdd:pfam10174 574 SGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN 622
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
367-543 |
4.17e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 367 SLSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVE------EKYKKamvSNAQLDNEKNNLIYQVDTLKDVIEEQEE 439
Cdd:TIGR04523 336 IISQLNEqISQLKKELTNSESENSEKQRELEEKQNEIEklkkenQSYKQ---EIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 440 QMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE----NQRLQQKVDTMTKEVFDLQETLLWKDKALG 515
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
170 180
....*....|....*....|....*...
gi 755532231 516 alEKQKEHIAcLRNERDVLREELADLRQ 543
Cdd:TIGR04523 493 --SKEKELKK-LNEEKKELEEKVKDLTK 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
416-724 |
5.34e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 416 LDNEKNNLiyqvDTLKDVIEEQEEQ-----MAEFYRENEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQ 490
Cdd:PRK02224 182 LSDQRGSL----DQLKAQIEEKEEKdlherLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 491 QKVDTMTKEVFDLQETllwkdkalgalekqkehIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepv 570
Cdd:PRK02224 251 EELETLEAEIEDLRET-----------------IAETEREREELAEEVRDLRERLEELEE-------------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 571 vgAITAVSQEAAqvLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGlqNGSDLQfiEMQ 650
Cdd:PRK02224 294 --ERDDLLAEAG--LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE--RAEELR--EEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 651 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAER-------RKLQRELRTAQDKIEEM 723
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdelrereAELEATLRTARERVEEA 445
|
.
gi 755532231 724 E 724
Cdd:PRK02224 446 E 446
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
382-738 |
6.13e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 382 HDVEgryMQGLKELKESL-SEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKH 460
Cdd:pfam15921 276 HEVE---ITGLTEKASSArSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 461 MCSvlqhkmDELKEGLRQRDELIEENQRLQqkvDTMTKEVFDLQEtllwKDKALgALEKQKEHIACLRNER-----DVLR 535
Cdd:pfam15921 353 LAN------SELTEARTERDQFSQESGNLD---DQLQKLLADLHK----REKEL-SLEKEQNKRLWDRDTGnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 536 EELADLRQTVTTAEkhGLVIIPDSTPNGDVHHEPVV-----GAITAVSQEAAQvLESAGEGPLDVrLRKLAGEKDELLSQ 610
Cdd:pfam15921 419 RELDDRNMEVQRLE--ALLKAMKSECQGQMERQMAAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 611 IRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ---------RDANRQISEYKFKLSKAEQDIATLEQSI--- 678
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenm 574
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532231 679 SRLEGQVLRYKTAAE-NAEKIEDELKAERRKLQrELRTAQD----KIEEMEMTNSHLakRLEKMK 738
Cdd:pfam15921 575 TQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQ-EFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-744 |
7.01e-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: 46.59 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 517 LEKQKEHIACLRNERDVLREELADLRQTVTTA--EKHGLVIIPDSTPNGDVHHEPVVGAITA-VSQEAAQVLESAGE-GP 592
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLrkELEELSRQISALRKDLARLEAEVEQLEErIAQLSKELTELEAEiEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 593 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDIA 672
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA---LDELRAELTLLNEEAANLRER-LESLERRIAATERRLE 841
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 673 TLEQSISRLEGQVLRY----KTAAENAEKIEDELKA---ERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 744
Cdd:TIGR02168 842 DLEEQIEELSEDIESLaaeiEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-522 |
7.92e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 369 SELRDIYDLKDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEF---- 444
Cdd:TIGR04523 381 SYKQEIKNLESQINDLE----SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKelii 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 445 -----YREN-EEKSKELERQ-KHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEvfdlQETLLWKDKALGAL 517
Cdd:TIGR04523 457 knldnTRESlETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK----ISSLKEKIEKLESE 532
|
....*
gi 755532231 518 EKQKE 522
Cdd:TIGR04523 533 KKEKE 537
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-737 |
8.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 399 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSK---ELERQKHMCSVLQHKMDEL 472
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 473 KE---GLRQRDELIEENQR--------LQQKVDTMTKEVFDLQEtllwKDKALGALEKQKEHIACLRNERDVLREELADL 541
Cdd:PRK03918 237 KEeieELEKELESLEGSKRkleekireLEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 542 RQTVTTAEKHGLVIipdstpngdvhhepvvgaitavsQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKLK---LQL 618
Cdd:PRK03918 313 EKRLSRLEEEINGI-----------------------EERIKELEEKEE-----RLEELKKKLKELEKRLEELEerhELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 619 EEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDIATLEQSISRLEGQVLRYKTAAE----- 693
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvc 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755532231 694 NAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 737
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-741 |
9.54e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 370 ELRDIYDLKDQIHDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 445
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 446 RENEEKSKELERQKHMCSVLQHKMDELKEGLRQ----RDELIEENQrlQQKVDTMTKEVFDLQETLLWKDKALGALEKQK 521
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 522 EHI-ACLRNERDVLR-EELAD-LRQTVTTAEKHGLVIIPDSTPNgdvhHEPVVGAITAVSQEAAQVLESAGEG-PLDVRL 597
Cdd:PRK03918 483 RELeKVLKKESELIKlKELAEqLKELEEKLKKYNLEELEKKAEE----YEKLKEKLIKLKGEIKSLKKELEKLeELKKKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 598 RKLAGEKDELLSQIRKLKLQLEEERQKCSrnDGMSGDLAGLQNGSDlQFIEMqRDANRQISEYKFKLSKAEQDIATLEQS 677
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESV--EELEERLKELEPFYN-EYLEL-KDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 678 ISRLEGQVLRYKTAAENAEKIEDE-----LKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANR 741
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
378-744 |
1.11e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 378 KDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELER 457
Cdd:TIGR04523 116 KEQKNKLE----VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 458 QKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKalgALEKQKEHIACLRNERDVLREE 537
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT---EISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 538 LADLRQTVTTAEKhglvIIPDSTPNgdvhHEPVVGAITAVSQEAAQVLesagegpldvrLRKLAGEKDELLSQIRKLKLQ 617
Cdd:TIGR04523 269 LSEKQKELEQNNK----KIKELEKQ----LNQLKSEISDLNNQKEQDW-----------NKELKSELKNQEKKLEEIQNQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 618 LEEERQKCSR-NDGMSgDLAGLQNGSDLQFIEMQrdanRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAE 696
Cdd:TIGR04523 330 ISQNNKIISQlNEQIS-QLKKELTNSESENSEKQ----RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 755532231 697 KIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 744
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
596-741 |
1.53e-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: 43.76 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 596 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 668
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532231 669 QDIATLEQSISRLEGQVlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEmemtnsHLAKRLEKMKANR 741
Cdd:COG1579 124 EELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
373-592 |
1.55e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 373 DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 449
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 450 EKSKE----------------LERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETllwKDKA 513
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 514 LGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGP 592
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
376-739 |
1.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 376 DLKDQIHDVEGRYMQGLKELKE----------SLSEVEEKYKKaMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFY 445
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEisselpelreELEKLEKEVKE-LEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 446 RENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIA 525
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 526 CLRNERDVLRE---ELADLRQTVTTAEKHglviipdSTPNGDVHHEPVVGAITAVSQEAAQVLEsagegpldvRLRKLAG 602
Cdd:PRK03918 349 ELEKRLEELEErheLYEEAKAKKEELERL-------KKRLTGLTPEKLEKELEELEKAKEEIEE---------EISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 603 EKDELLSQIRKLKL---QLEEERQKCSrndgmsgdlaglQNGSDLQfiemQRDANRQISEYKFKLSKAEQDIATLEQSIS 679
Cdd:PRK03918 413 RIGELKKEIKELKKaieELKKAKGKCP------------VCGRELT----EEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755532231 680 RL-------------EGQVLRYKTAAENAEKIEDELKA----ERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 739
Cdd:PRK03918 477 KLrkelrelekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
365-744 |
2.18e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 365 DTSLSELRDIYDLKDQIHDVEGR--YMQG-LKELKESLSEVEEKYKKA-----MVSNAQLDNEKnnlI--YQ--VDTLKD 432
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRlvEMAReLEELSARESDLEQDYQAAsdhlnLVQTALRQQEK---IerYQedLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 433 VIEEQEEQMAEfyrENEEKSkELERQKHMCsvlQHKMDELKEGLRQRDELIEENQR----LQQKVDTMTKEVFDLQETLL 508
Cdd:COG3096 362 RLEEQEEVVEE---AAEQLA-EAEARLEAA---EEEVDSLKSQLADYQQALDVQQTraiqYQQAVQALEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 509 wkdkalgALEKQKEHIACLRNERDVLREELADLRQTVttaekhglviipdstpngdvhhepvvgaitAVSQEAAQVLESA 588
Cdd:COG3096 435 -------TPENAEDYLAAFRAKEQQATEEVLELEQKL------------------------------SVADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 589 GEgpldvRLRKLAGEKD---------ELLSQIRKLKLQLEeerqkcsRNDGMSGDLAGLQngsdlQFIEMQRDANRQISE 659
Cdd:COG3096 478 YE-----LVCKIAGEVErsqawqtarELLRRYRSQQALAQ-------RLQQLRAQLAELE-----QRLRQQQNAERLLEE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 660 YKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAERRKL-QREL--RTAQDKIEEM-EMTNS 728
Cdd:COG3096 541 FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAveqrselRQQLEQLRARIKELaARAPawLAAQDALERLrEQSGE 620
|
410
....*....|....*.
gi 755532231 729 HLAKRLEKMKANRTAL 744
Cdd:COG3096 621 ALADSQEVTAAMQQLL 636
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
576-748 |
2.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 576 AVSQEAAQVLESAgEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNgsDLQFIEMQRDAN- 654
Cdd:TIGR02168 263 QELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRER----------LANLER--QLEELEAQLEELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 655 RQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDEL-------KAERRKLQRELRTAQDKIEEMEMTN 727
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlRSKVAQLELQIASLNNEIERLEARL 409
|
170 180
....*....|....*....|.
gi 755532231 728 SHLAKRLEKMKANRTALLAQQ 748
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKL 430
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
368-595 |
2.78e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 368 LSELR-DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSN------------AQLDNEKNNLIYQVDTL---- 430
Cdd:pfam06160 181 LEKLEeETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalehlnvdkeiQQLEEQLEENLALLENLelde 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 431 -KDVIEEQEEQMAEFYR--ENEEKSKE--LERQKHMCSVLQHKMDELKEGL------------------------RQRDE 481
Cdd:pfam06160 261 aEEALEEIEERIDQLYDllEKEVDAKKyvEKNLPEIEDYLEHAEEQNKELKeelervqqsytlnenelervrgleKQLEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 482 LIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQ----KEHIACLRNERDVLREELADLRQTVTT----AEKHGL 553
Cdd:pfam06160 341 LEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEqeefKESLQSLRKDELEAREKLDEFKLELREikrlVEKSNL 420
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755532231 554 VIIPDStpngdvhhepVVGAITAVSQEAAQVLESAGEGPLDV 595
Cdd:pfam06160 421 PGLPES----------YLDYFFDVSDEIEDLADELNEVPLNM 452
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
394-748 |
2.86e-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: 44.65 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 394 ELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQ---------MAEFYRENEEKSKELERQKHmcsv 464
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIAQQAA---- 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 465 lqhKMDELkEGLRQRDELIEENQRLQQKVDTMTKEVFDLQEtllwkdkalgALEKQKEHIACLRNERDVLREELADLRQT 544
Cdd:TIGR00606 814 ---KLQGS-DLDRTVQQVNQEKQEKQHELDTVVSKIELNRK----------LIQDQQEQIQHLKSKTNELKSEKLQIGTN 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 545 VTTAEKHGLVIIPDSTPngdvhhepVVGAITAVSQEAAQVLesagegPLDVRLRKLAGEKDELLSQI----RKLKLQLEE 620
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTE--------VQSLIREIKDAKEQDS------PLETFLEKDQQEKEELISSKetsnKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 621 ERQKCSRNDGMSGDLAG-LQNGSDLQFIEMQRDANR---QISEYKFKLSKAEQDIATLEQSIsrlEGQVLRYKTAAENA- 695
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENkIQDGKDDYLKQKETELNTvnaQLEECEKHQEKINEDMRLMRQDI---DTQKIQERWLQDNLt 1022
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755532231 696 -EKIEDELKAERRKLQRELR-TAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 748
Cdd:TIGR00606 1023 lRKRENELKEVEEELKQHLKeMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ 1077
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
368-747 |
3.45e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 368 LSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLkdvieeqeeqMAEFYR 446
Cdd:pfam15921 319 LSDLEStVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL----------LADLHK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 447 ENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALG-ALEKQKEHIA 525
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNeSLEKVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 526 CLRNERDVLR---EELADLRQTVTTAEKhglviipdstpngdvhhepVVGAITAVSQEAAQVLESAG------EGPLDVR 596
Cdd:pfam15921 469 QLESTKEMLRkvvEELTAKKMTLESSER-------------------TVSDLTASLQEKERAIEATNaeitklRSRVDLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 597 LRKLAGEKDE------LLSQIRKLKLQLEEE-------RQKCSRND---GMSGDLAGLQNGSDLQFIEMQRDANRQISEY 660
Cdd:pfam15921 530 LQELQHLKNEgdhlrnVQTECEALKLQMAEKdkvieilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEF 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 661 KFKLSKAEQDIATLEQSISRLEGQVLR---------------------------------------YKTAAENAEKIEDE 701
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDLELEKVKlvnagserlravkdikqerdqllnevktsrnelnslsedYEVLKRNFRNKSEE 689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 755532231 702 LKAERRKLQRELRTAQDKIEE-------MEMTNSHLAKRLEKMKANRTALLAQ 747
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQtrntlksMEGSDGHAMKVAMGMQKQITAKRGQ 742
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
596-748 |
3.56e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 596 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAglQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDIATL 674
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELE--QARSELEQLEEElEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755532231 675 EQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 748
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
527-724 |
3.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 527 LRNERDVLREELADLRQTVTTAE--------KHGLViipdstpngdvhhepvvgaitAVSQEAAQVLESAGEgpLDVRLR 598
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEaaleefrqKNGLV---------------------DLSEEAKLLLQQLSE--LESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 599 KLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgDLAGLQNGSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQS 677
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPD----------ALPELLQSPVIQQLRAQLaELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755532231 678 ISRLEGQVlryktaAENAEKIEDELKAERRKLQRELRTAQDKIEEME 724
Cdd:COG3206 300 IAALRAQL------QQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
365-624 |
3.84e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 365 DTSLSELRD-IYDLKDQIHDVEGRYMqglkELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 443
Cdd:COG1196 266 EAELEELRLeLEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 444 fyrENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEH 523
Cdd:COG1196 342 ---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 524 iacLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAGE 603
Cdd:COG1196 419 ---LEEELEELEEALAELEEEEEEEEE----------------------ALEEAAEEEAELEEEEEA--LLELLAELLEE 471
|
250 260
....*....|....*....|.
gi 755532231 604 KDELLSQIRKLKLQLEEERQK 624
Cdd:COG1196 472 AALLEAALAELLEELAEAAAR 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
434-739 |
4.07e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 434 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVD--------------TMTKE 499
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEelkgkeqelifllqAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 500 VFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQ 579
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 580 EAAQVlESAGEGPLDVRlRKLAGEKDELLSQIRKLKLQLEEerqkcSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISE 659
Cdd:pfam05483 532 MLKQI-ENLEEKEMNLR-DELESVREEFIQKGDEVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 660 YKFKlskaeqDIATLEQsisrlEGQVLRYKTAAENAE---------KIEDELKAERRKLQRELRTAQDKIEEMEMTNSHL 730
Cdd:pfam05483 605 NKNK------NIEELHQ-----ENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL 673
|
....*....
gi 755532231 731 AKRLEKMKA 739
Cdd:pfam05483 674 LEEVEKAKA 682
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
388-748 |
4.68e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 388 YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL-- 465
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELek 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 466 -----------------QHKMDELKEGLRQRDELIEENQ-----------RLQQKVDTMTKEVFDLQETLLWKDKALGal 517
Cdd:TIGR04523 289 qlnqlkseisdlnnqkeQDWNKELKSELKNQEKKLEEIQnqisqnnkiisQLNEQISQLKKELTNSESENSEKQRELE-- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 518 EKQKEhIACLRNERDVLREELADLRQTVTTAEKHglviipdstpngdvhhepvvgaITAVSQEAAQvlesagegpLDVRL 597
Cdd:TIGR04523 367 EKQNE-IEKLKKENQSYKQEIKNLESQINDLESK----------------------IQNQEKLNQQ---------KDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 598 RKLAGEKDELLSQIRKLKLQLEEERQKCSrndgmsgDLAGLQNGSDLQFIEMQR---DANRQISEYKFKLSKAEQD---- 670
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNtreSLETQLKVLSRSINKIKQNleqk 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 671 ----------IATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTN---------SHLA 731
Cdd:TIGR04523 488 qkelkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKN 567
|
410
....*....|....*..
gi 755532231 732 KRLEKMKANRTALLAQQ 748
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQ 584
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
390-543 |
5.62e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 390 QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL---- 465
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 466 --QHKMDELKEGLRQRD--ELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADL 541
Cdd:COG4942 114 yrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
..
gi 755532231 542 RQ 543
Cdd:COG4942 194 KA 195
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
395-744 |
5.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 395 LKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM---------AEFYRENEEKSKELERQKHmcSVL 465
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREER--DEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 466 QHKMDELKEGLRQRDELIEENQRLQQ--KVDTMTKEVFDlqetllwkDKALGALEKQKEHIACLRNERDVLREELADLRQ 543
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEagKCPECGQPVEG--------SPHVETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 544 TVTTAEKhgLVIIPDSTPNGDVHHEPVVGAIT-------------AVSQEAAQVLESAGEGPLDvRLRKLAGEKDELLSQ 610
Cdd:PRK02224 497 RLERAED--LVEAEDRIERLEERREDLEELIAerretieekreraEELRERAAELEAEAEEKRE-AAAEAEEEAEEAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 611 IRKLKLQLEEERQKCSRNDGMSGDLAGLQN-GSDLQFIEMQRDA-NRQISEYKFKLSKAEQDIATLEQSI--SRLEGQVL 686
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLAAIADaEDEIERLREKREAlAELNDERRERLAEKRERKRELEAEFdeARIEEARE 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755532231 687 RYKTAAENAEKIE---DELKAERRKLQRELRTAQDKIEEMEmtnsHLAKRLEKMKANRTAL 744
Cdd:PRK02224 654 DKERAEEYLEQVEeklDELREERDDLQAEIGAVENELEELE----ELRERREALENRVEAL 710
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
393-739 |
7.35e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 393 KELKESLSEVEE-KYKKAMVSNAQldnEKNNLIYQVDTL---KDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 468
Cdd:TIGR00618 260 QLLKQLRARIEElRAQEAVLEETQ---ERINRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 469 MDELKEGLRQRDELIEENQRLQQKVD--TMTKEVFDLQETLLwkdKALGALEKQKEHIA----CLRNERDVLREELA--D 540
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLT---QHIHTLQQQKTTLTqklqSLCKELDILQREQAtiD 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 541 LRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQvlesagEGPLDVRLRKLAGEKDELLSQIRKLKLQLEE 620
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL------EKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 621 ERQKcsrndgmsgdlaglqngsDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIED 700
Cdd:TIGR00618 488 KKAV------------------VLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
330 340 350
....*....|....*....|....*....|....*....
gi 755532231 701 ELKAERRKLQRElrtaQDKIEEMEMTNSHLAKRLEKMKA 739
Cdd:TIGR00618 550 QLTSERKQRASL----KEQMQEIQQSFSILTQCDNRSKE 584
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
380-735 |
9.04e-04 |
|
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: 42.85 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 380 QIHDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 458
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 459 khmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKE---------------- 522
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtqellqeetrqklnl 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 523 --HIACLRNERDVLREELADLRQTVTTAEKHGLViipdstpngdvhHEPVVGAITAVSQEAAQVLESAGEGpldvrlrkl 600
Cdd:pfam01576 488 stRLRQLEDERNSLQEQLEEEEEAKRNVERQLST------------LQAQLSDMKKKLEEDAGTLEALEEG--------- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 601 ageKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGlqngsDLQFIEMQRDANRQI-SEYKFKLSKAEQDIATlEQSIS 679
Cdd:pfam01576 547 ---KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQLvSNLEKKQKKFDQMLAE-EKAIS 617
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755532231 680 rlegqvLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLE 735
Cdd:pfam01576 618 ------ARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
653-748 |
9.80e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 653 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAK 732
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 755532231 733 RLEKMKAnrtaLLAQQ 748
Cdd:COG4942 98 ELEAQKE----ELAEL 109
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
651-739 |
1.09e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 651 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaerRKLQRELRTAQDKIEEMEMTNSHL 730
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491
|
....*....
gi 755532231 731 AKRLEKMKA 739
Cdd:COG2433 492 KRKLERLKE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
601-747 |
1.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 601 AGEKDELLSQIRKLKLQLEEERQKCSRNDGmsgdlagLQNGSDLQFIEMQRDANRQiseykfKLSKAEQDIATLEQSISR 680
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA------ELEELRAELARLEAELER 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532231 681 LEGQvlryktaaenaekiEDELKAERRKLQRELRTAQ-DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 747
Cdd:COG4913 314 LEAR--------------LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-724 |
1.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMcsvlqHKMDE 471
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-----EADYE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKQ---------KEHIACLRNERDVLREEL---- 538
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL---EAALAAALQNivveddevaAAAIEYLKAAKAGRATFLpldk 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 539 ----ADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGE--GPLDVRLRKLAGEKDELLS--- 609
Cdd:COG1196 582 irarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRraVTLAGRLREVTLEGEGGSAggs 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 610 ----QIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQV 685
Cdd:COG1196 662 ltggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
330 340 350
....*....|....*....|....*....|....*....
gi 755532231 686 LRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 724
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
593-747 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 593 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFklskAEQDIA 672
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQE--------------------------RREALQRLAEYSW----DEIDVA 664
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532231 673 TLEQSISRLEGQvlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 747
Cdd:COG4913 665 SAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-740 |
1.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 368 LSELRDIY-DLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAmvsnAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 446
Cdd:PRK03918 298 LSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 447 ENEEKSK----ELERQKHMCSVLQHKMDELKEglrQRDELIEENQRLQQKVDTMTKEVFDLQET---------LLWKDKA 513
Cdd:PRK03918 374 LERLKKRltglTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 514 LGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngDVHHEPVVGAITAVSQEAAQVLESAGEGPL 593
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK-------------VLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 594 DvRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNgsDLQFIEMQR-DANRQISEYKFKlskaeqDIA 672
Cdd:PRK03918 518 E-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--KLDELEEELaELLKELEELGFE------SVE 588
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532231 673 TLEQSISRLEGQVLRYKTAAENAEKIEDELKaERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 740
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-594 |
1.55e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 372 RDIYDLKDQIHDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 448
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 449 EEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE-NQRL------QQKVDTMTKEVFDLQETLLWKDKALGA-LEKQ 520
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADlNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAAdLSKY 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 521 KEHIACLRNERDVLREELADLRQTVTTAEKHGLVI---IPDSTPNGDVHHEPVVGAITAVSQ------EAAQVLESAGEG 591
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeerVRGGRAVEEVLKASIQGVHGTVAQlgsvgeRYATAIEVAAGN 547
|
...
gi 755532231 592 PLD 594
Cdd:TIGR02169 548 RLN 550
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
368-500 |
1.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 368 LSELRDIYD-LKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 441
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 442 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQR-DELIEENQRLQQKVDTMTKEV 500
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
392-744 |
1.94e-03 |
|
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: 41.70 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdviEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 471
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNAL-----------QEQLQAETELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEglrqrdELIEENQRLQQKVDTMTKEVFDLQETL-----------LWKDKALGALEKQKEHIACLRN-------ERDV 533
Cdd:pfam01576 83 RLE------EEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaarqklqLEKVTTEAKIKKLEEDILLLEDqnsklskERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 534 LREELADLRQTVTTAEKHGlviipDSTPNGDVHHEPVVGAItavsqEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRK 613
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKA-----KSLSKLKNKHEAMISDL-----EERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 614 LKLQLEEERQKCSRNDgmsGDLAGLQNGSD------LQFIEMQRDANRQISEYKFKL-------SKAEQDIATLEQSISR 680
Cdd:pfam01576 227 LQAQIAELRAQLAKKE---EELQAALARLEeetaqkNNALKKIRELEAQISELQEDLeseraarNKAEKQRRDLGEELEA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532231 681 LEGQVLRY--KTAA--ENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSH----LAKRLEKMKANRTAL 744
Cdd:pfam01576 304 LKTELEDTldTTAAqqELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANL 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
653-722 |
2.13e-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: 2.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 653 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEE 722
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
392-731 |
2.45e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 471
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALG----ALEKQKEHIACLRNERDVLREELADLRQTVTT 547
Cdd:PRK02224 361 LRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDELREREAELEATLRT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 548 AEKhglviipdstpngdvhhepvvgaitavSQEAAQVLESAGEGP---LDVRLRKLAGEKDELLSQIRKLKLQLEEERQK 624
Cdd:PRK02224 438 ARE---------------------------RVEEAEALLEAGKCPecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 625 CSRNDgmsgdlaglqngSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEqsiSRLEGQVLRYKTAAENAEKIEDELKA 704
Cdd:PRK02224 491 VEEVE------------ERLERAEDLVEAEDRIERLEERREDLEELIAERR---ETIEEKRERAEELRERAAELEAEAEE 555
|
330 340
....*....|....*....|....*..
gi 755532231 705 ERRKLQRELRTAQDKIEEMEMTNSHLA 731
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
392-547 |
2.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN---EEKSKELERqkhmcsvLQHK 468
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIER-------LEWR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 469 MDELKEGLRQRDELIEENQRLQQKVDTMTKEvfdlqetllwkdkalgalEKQKEHIACLRNERDVLREELADLRQTVTT 547
Cdd:COG1340 125 QQTEVLSPEEEKELVEKIKELEKELEKAKKA------------------LEKNEKLKELRAELKELRKEAEEIHKKIKE 185
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-713 |
2.58e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEekykkamvsnAQLDNEKnnliyqvDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 471
Cdd:COG1196 255 LEELEAELAELE----------AELEELR-------LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHiacLRNERDVLREELADLRQTVTTAEKh 551
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALR- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 552 glviipdstpngdvhhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKcsrndgm 631
Cdd:COG1196 394 ---------------------AAAELAAQLEELEEAEEA--LLERLERLEEELEELEEALAELEEEEEEEEEA------- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 632 sgdlAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQR 711
Cdd:COG1196 444 ----LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
..
gi 755532231 712 EL 713
Cdd:COG1196 520 RG 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
394-741 |
2.87e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 394 ELKESLSEVEEKYKKAMVSNAQLDNE-KNNLIYQVDTLKDVIEEQEEQMAE------FYRENEEKSKELERQKHMCSVLQ 466
Cdd:pfam17380 244 NLAEDVTTMTPEYTVRYNGQTMTENEfLNQLLHIVQHQKAVSERQQQEKFEkmeqerLRQEKEEKAREVERRRKLEEAEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 467 HKMDELK-------EGLRQRDELIEENQRLQQKVDTMTKEVFDLQETL--LWKDKALGALEKQKEHiaclRNERdvLREE 537
Cdd:pfam17380 324 ARQAEMDrqaaiyaEQERMAMERERELERIRQEERKRELERIRQEEIAmeISRMRELERLQMERQQ----KNER--VRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 538 LADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPvvgaiTAVSQEAAQVLESAGEGPLDvRLRKlagEKDELLSQIRKLKLQ 617
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQ-----EEARQREVRRLEEERAREME-RVRL---EEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 618 LEEERQKCSRNDGMSGDLAGLQNgSDLQFIEMQRDANRQ-ISEYKFKLSKAEQDIATLEQSISRLEGqvlRYKTAAENAE 696
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEE-QRRKILEKELEERKQaMIEEERKRKLLEKEMEERQKAIYEEER---RREAEEERRK 544
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 755532231 697 KIEDElkaERRKLQRELRTAQD---KIEEMEMTNSHLAKRLEKMKANR 741
Cdd:pfam17380 545 QQEME---ERRRIQEQMRKATEersRLEAMEREREMMRQIVESEKARA 589
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
389-744 |
3.30e-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: 41.19 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 389 MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN--NLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQ 466
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERELSKAEKNSLteTLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 467 HKMDE----LKEGLRQRDELIEE------NQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIaclRNERDVLRE 536
Cdd:TIGR00606 543 DKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI---NNELESKEE 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 537 ELADLRQTV-----TTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVL-ESAGEGPLDVRLRKLAGEKDELLSQ 610
Cdd:TIGR00606 620 QLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQSCCPVCQRVFQTEAELQEFISD 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 611 IR--------KLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAEQ------- 669
Cdd:TIGR00606 700 LQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNRDIQRLKNDIEEQETllgtimp 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 670 ----------DIATLEQSISRLEGQVLRYKTAAENAEKIE-----DELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRL 734
Cdd:TIGR00606 780 eeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
410
....*....|
gi 755532231 735 EKMKANRTAL 744
Cdd:TIGR00606 860 QHLKSKTNEL 869
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
600-744 |
3.32e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 600 LAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglQNGSDLQfiemqrDANRQISEYKFKLSKAEQ----DIATLE 675
Cdd:pfam15742 81 LTAEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLA--QEKSRVA------DAEEKILELQQKLEHAHKvcltDTCILE 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532231 676 QSisRLEGQVlryKTAAENAEKIEDELKAERRK----------LQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 744
Cdd:pfam15742 153 KK--QLEERI---KEASENEAKLKQQYQEEQQKrklldqnvneLQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQL 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
648-746 |
3.37e-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: 40.52 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 648 EMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtn 727
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90
....*....|....*....
gi 755532231 728 shlaKRLEKMKANRTALLA 746
Cdd:COG4942 97 ----AELEAQKEELAELLR 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
574-748 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 574 ITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCS-------RNDGMSGDLAGLQNGSDLQ- 645
Cdd:COG3883 39 LDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 646 FIE-------MQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQD 718
Cdd:COG3883 117 FLDrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|
gi 755532231 719 KIEEMEMTNSHLAKRLEKMKANRTALLAQQ 748
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
387-724 |
3.66e-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: 40.80 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 387 RYMQGLKELKESLSEVEEKYKKAMvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHmcSVLQ 466
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ--RTVR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 467 HKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVfdlqetllwkdkalGALEKQKEHIACLRNERDVLREELAdlrqtvT 546
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQ--------------GRLQLQADRHQEHIRARDSLIQSLA------T 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 547 TAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCS 626
Cdd:TIGR00606 376 RLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK-ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 627 RNDGMSGDLAGLQNGSDlqfiemqrdanrQISEYKFKLSKAEQDIATLEQSisrlegqvlrykTAAENAEKIEDELKAER 706
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSD------------RILELDQELRKAERELSKAEKN------------SLTETLKKEVKSLQNEK 510
|
330
....*....|....*...
gi 755532231 707 RKLQRELRTAQDKIEEME 724
Cdd:TIGR00606 511 ADLDRKLRKLDQEMEQLN 528
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
368-559 |
4.49e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 368 LSELR-DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNekNNLIYQVDTLKDVIEEQEEQMAEFYR 446
Cdd:PRK04778 200 LDQLEeELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELDL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 447 EN-EEKSKELERQ-KHMCSVLQH----------KMDELKEGL----RQRDELIEENQRLQQK-----------------V 493
Cdd:PRK04778 278 DEaEEKNEEIQERiDQLYDILERevkarkyvekNSDTLPDFLehakEQNKELKEEIDRVKQSytlneselesvrqlekqL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 494 DTMTKEVFD--------------LQETLLWKDKALGALEKQ----KEHIACLRNERDVLREELADLRQTVTTA----EKH 551
Cdd:PRK04778 358 ESLEKQYDEiteriaeqeiayseLQEELEEILKQLEEIEKEqeklSEMLQGLRKDELEAREKLERYRNKLHEIkrylEKS 437
|
....*...
gi 755532231 552 GLVIIPDS 559
Cdd:PRK04778 438 NLPGLPED 445
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
403-724 |
4.83e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 403 EEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDELKEGLRQRDEL 482
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENA---NNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 483 I----------------EENQRLQQKVDTMTKEVFDLQETLLWK----DKALGALEKQKEHIACLRNERDvLREELADLR 542
Cdd:COG5185 305 IdikkatesleeqlaaaEAEQELEESKRETETGIQNLTAEIEQGqeslTENLEAIKEEIENIVGEVELSK-SSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 543 QTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVlesagEGPLDVRLRKLAgekdellsQIRKLKLQLEEER 622
Cdd:COG5185 384 DTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEEL-----QRQIEQATSSNE--------EVSKLLNELISEL 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 623 QKCSRNdgmsgdlagLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISR-LEGQVLRYKTAAENAEKIEDE 701
Cdd:COG5185 451 NKVMRE---------ADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAtLEKLRAKLERQLEGVRSKLDQ 521
|
330 340
....*....|....*....|...
gi 755532231 702 LKAERRKLQRELRTAQDKIEEME 724
Cdd:COG5185 522 VAESLKDFMRARGYAHILALENL 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-724 |
5.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 374 IYDLKDQIHDVEGrymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyRENEEKSK 453
Cdd:PRK03918 275 IEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 454 ELERqkhmcsvlqhKMDELKEglrqRDELIEENQRLQQKVDTMTKEVFDLQETLLwkDKALGALEKQKEHIaclRNERDV 533
Cdd:PRK03918 349 ELEK----------RLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKL--EKELEELEKAKEEI---EEEISK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 534 LREELADLRQTVTTAEKhglVIIPDSTPNGDVhhePVVGAITAVSQEAAQVLESAGEgpldvrLRKLAGEKDELLSQIRK 613
Cdd:PRK03918 410 ITARIGELKKEIKELKK---AIEELKKAKGKC---PVCGRELTEEHRKELLEEYTAE------LKRIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 614 LKLQLEEERQKCSRNDGMSgdlaglqngSDLQFIEMQRDANRQISEYKF-KLSKAEQDIATLEQSISRLEGQVLRYKtaa 692
Cdd:PRK03918 478 LRKELRELEKVLKKESELI---------KLKELAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLK--- 545
|
330 340 350
....*....|....*....|....*....|..
gi 755532231 693 ENAEKIEdELKAERRKLQRELRTAQDKIEEME 724
Cdd:PRK03918 546 KELEKLE-ELKKKLAELEKKLDELEEELAELL 576
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
470-743 |
5.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 470 DELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLqetllwKDKALGALEKQKEH---IACLRNERDVLREELADLRQTVt 546
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKEL------REEAQELREKRDELnekVKELKEERDELNEKLNELREEL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 547 taEKHGLVIIPDSTPNGDVHhepvvgaitAVSQEAAQVLESAGEGPLDVRlrklagEKDELLSQIRKLKLQLEEERQKCS 626
Cdd:COG1340 95 --DELRKELAELNKAGGSID---------KLRKEIERLEWRQQTEVLSPE------EEKELVEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 627 RNDgmsgDLAGLQNGSDLQFIEMqRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAER 706
Cdd:COG1340 158 KNE----KLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 755532231 707 RKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTA 743
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
393-743 |
6.64e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 393 KELKESLSEVEEKYKKAMVSNAQLDNEKNNLIY-QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 471
Cdd:pfam02463 215 LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKh 551
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 552 glviipdstpngdvhhepvvgaitavSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIrklKLQLEEERQKcsrndgm 631
Cdd:pfam02463 374 --------------------------ELLAKKKLESERLSSAAKLKEEELELKSEEEKEA---QLLLELARQL------- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 632 sGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQR 711
Cdd:pfam02463 418 -EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
330 340 350
....*....|....*....|....*....|..
gi 755532231 712 ELRTAQDKIEEMEMTNSHLAKRLEKMKANRTA 743
Cdd:pfam02463 497 ERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
510-747 |
6.79e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 510 KDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHglviipdstpngdvhhepvvGAITAVSQEAAQVLESAG 589
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--------------------QALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 590 EGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSrndgmsgdlaglqngsdlQFIEMQRDANRQISeykfKLSKAEQ 669
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLE------------------EIEQLLEELNKKIK----DLGEEEQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 670 -----DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 744
Cdd:TIGR02169 290 lrvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
...
gi 755532231 745 LAQ 747
Cdd:TIGR02169 370 RAE 372
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-738 |
7.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 390 QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 469
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 470 DELKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHiacLRNERDVLREELADLRQTVTTAE 549
Cdd:COG4372 111 EELQE---ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES---LQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 550 KHGLViipdSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRND 629
Cdd:COG4372 185 LDELL----KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 630 GMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISR-LEGQVLRYKTAAENAEKIEDELKAERRK 708
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGaLEDALLAALLELAKKLELALAILLAELA 340
|
330 340 350
....*....|....*....|....*....|
gi 755532231 709 LQRELRTAQDKIEEMEMTNSHLAKRLEKMK 738
Cdd:COG4372 341 DLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
392-744 |
7.59e-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: 39.70 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKamvsnaqldnEKNNLIYQVDTLKDVIEEQEEQMAE---FYRENEEKSKELERQKHMCSvlqhk 468
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK----------EINDKEKQVSLLLIQITEKENKMKDltfLLEESRDKANQLEEKTKLQD----- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 469 mDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKE-HIACLRNERDVLREELADLRQTVTT 547
Cdd:pfam05483 282 -ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaQMEELNKAKAAHSFVVTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 548 AEKHgLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDV-RLRKLAGEKDELLSQIRKLKlQLEEERQkcs 626
Cdd:pfam05483 361 LEEL-LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELeELKKILAEDEKLLDEKKQFE-KIAEELK--- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 627 rndGMSGDLAGLQNGSDLQF--IEMQRDANRQISEYkfkLSKAEQDIATleqsisRLEGQVLRYKTAAENAEKI---EDE 701
Cdd:pfam05483 436 ---GKEQELIFLLQAREKEIhdLEIQLTAIKTSEEH---YLKEVEDLKT------ELEKEKLKNIELTAHCDKLlleNKE 503
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 755532231 702 LKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 744
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-543 |
8.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 370 ELRDIYDLKDQIHDVEGRymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQE-EQMAEFYREN 448
Cdd:COG4913 270 RLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 449 EEKSKELERQKHMCSVLQHKMDELKEGLRQ-RDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKqkehiacL 527
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRD-------L 417
|
170
....*....|....*.
gi 755532231 528 RNERDVLREELADLRQ 543
Cdd:COG4913 418 RRELRELEAEIASLER 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-741 |
9.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 372 RDIYDLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNE-KNNLI--YQVDtLKDV---IEEQEEQMAEFY 445
Cdd:PRK03918 405 EEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELTEEhRKELLeeYTAE-LKRIekeLKEIEEKERKLR 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 446 RENEEKSKELERQKHMcSVLQHKMDELKE--------GLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkdKALGAL 517
Cdd:PRK03918 480 KELRELEKVLKKESEL-IKLKELAEQLKEleeklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL----EKLEEL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 518 EKQKEHiacLRNERDVLREELADLRQTVttaEKHGLVIIPDStpngdvhhepvvgaitavsQEAAQVLESAGEGPLdvRL 597
Cdd:PRK03918 555 KKKLAE---LEKKLDELEEELAELLKEL---EELGFESVEEL-------------------EERLKELEPFYNEYL--EL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 598 RKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdlaglqngsdlqfIEMQRdanRQISEYKFKLSkaEQDIATLEQS 677
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKR---------------LEELR---KELEELEKKYS--EEEYEELREE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755532231 678 ISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMtnshLAKRLEKMKANR 741
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
392-545 |
9.38e-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: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 392 LKELKESLSEVEEKYKKAMvsnAQLDNEKNNLIYQvdTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 471
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQA---AKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532231 472 LK-------EGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLRE-ELADLRQ 543
Cdd:TIGR00606 869 LKseklqigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKE 948
|
..
gi 755532231 544 TV 545
Cdd:TIGR00606 949 KV 950
|
|
| |
