|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
285-639 |
6.11e-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: 314.71 E-value: 6.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 285 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqihdvegrym 355
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 356 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 435
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 436 DELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdkalgalekqkehiaclrnerdvlreeladlrqtvttaE 515
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 516 KHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQ-KCSRN 594
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755532247 595 DGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 639
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-689 |
2.87e-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: 67.00 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHkmdE 437
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK---E 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 438 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKh 517
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 518 glviipdstpngdvHHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQI-RKLKLQLEEERQKCSRNDG 596
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELeALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 597 MSgDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDIATLEQSISRlegqvlRYKTAAENAEKIEDELKAERR 673
Cdd:TIGR02168 896 LE-ELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 755532247 674 KLQRELRTAQDKIEEM 689
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
315-690 |
1.74e-09 |
|
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: 61.24 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 315 NSSRRGSGDTSSliDPDTSLSELRDIYDLKDQIHDVegryMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVD 394
Cdd:TIGR02169 660 RAPRGGILFSRS--EPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 395 TLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLR--QRDELIEENQRLQQKVDTMTKEVFDLQET 472
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 473 LLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhEPVVGAITAVSQEAAQVle 552
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI------------------ENLNGKKEELEEELEEL-- 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 553 SAGEGPLDVRLRKLAGEKDELLSQIRKLKL---QLEEERQKcsRNDGMSGDLAGLQNGSD-LQFIEMQRDANRQISEYKF 628
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLSELKAKLEALEEeLSEIEDPKGEDEEIPEEEL 951
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532247 629 KLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 690
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-689 |
2.05e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 335 SELRDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 414
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 415 EEKSKELERQKHMCSVLQHKMDELkeglrqRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLR 494
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDEL------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 495 NERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgaITAVSQEAAQVLESAGEGpLDVRLRKLAGEKDELL 574
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLN-----------------------ERASLEEALALLRSELEE-LSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 575 SQIRKLKLQLEEERQKCSrndGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLeGQV-LR 653
Cdd:TIGR02168 915 RELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL-GPVnLA 990
|
330 340 350
....*....|....*....|....*....|....*.
gi 755532247 654 YKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 689
Cdd:TIGR02168 991 AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-690 |
2.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 381 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRE--NEEKS--------------KELERQKHMCSVLQHKM 435
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKElkAELRElelallvlrleelrEELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 436 DELKEGLRQRDELIEENQRLQQKVDtmtKEVFDLQETLLWKDKALGALEKQKEH------------------IACLRNER 497
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQIlrerlanlerqleeleaqLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 498 DVLREELADLRQTVTTAEKhglviipdstpngdvHHEPVVGAITAvSQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQI 577
Cdd:TIGR02168 333 DELAEELAELEEKLEELKE---------------ELESLEAELEE-LEAELEELESRLEE-LEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 578 RKLKLQLEEERQKCSRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEqdIATLEQSISRLEGQVLRYKTA 657
Cdd:TIGR02168 396 ASLNNEIERLEARLER-----------LEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEA 462
|
330 340 350
....*....|....*....|....*....|...
gi 755532247 658 AENAEKIEDELKAERRKLQRELRTAQDKIEEME 690
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
431-713 |
2.90e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 431 LQHKMDELKeglRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGAL----EKQKEHIACLRNERDVLREELAD 506
Cdd:TIGR02169 679 LRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 507 LRQTVTTAEKhglviipdstpngdvhhepVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEE 586
Cdd:TIGR02169 756 VKSELKELEA-------------------RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 587 ERQKCSRNDgmsgdlaglqngSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIE 665
Cdd:TIGR02169 817 IEQKLNRLT------------LEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755532247 666 DELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 713
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-702 |
4.44e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 334 LSELRDIYDLKDQIHDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 413
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 414 NEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWkdKALGALEKQKEHIACL 493
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 494 RNERDVLREELADLRQTVTTAEKHGlviipDSTPNGDVHHEP------------VVGAITAVSQEAAQVLESAGE----- 556
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEL-----EQLENELEAAALeerlkearllllIAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 557 ----GPLDVRLRKLAGEKDELLSQIRKLKLQLEEERqkcSRNDGMSGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSK 632
Cdd:COG4717 280 flvlGLLALLFLLLAREKASLGKEAEELQALPALEE---LEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532247 633 AEQDIATLEQSISRLEGQVLRYKTAAENAEKIED--ELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 702
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-714 |
1.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 396 LKDVIEEQEEQMaefyreneeksKELERQkhmcSVLQHKMDELKEGLRQRDelieenqrlqqkvdtmtkevfdLQETLLW 475
Cdd:COG1196 191 LEDILGELERQL-----------EPLERQ----AEKAERYRELKEELKELE----------------------AELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 476 KDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAVSQEAAQVLESAG 555
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------------------LELEELELELEEAQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 556 EgpldvRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQngsdlqfiEMQRDANRQISEYKFKLSKAEQ 635
Cdd:COG1196 288 A-----EEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELE--------EELEELEEELEELEEELEEAEE 351
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 636 DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 714
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
342-705 |
2.50e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 342 DLKDQI--------HDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 410
Cdd:PRK02224 191 QLKAQIeekeekdlHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 411 YRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQ---- 486
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE---AVEARREELEDRDEELRDRLEECRVAAQAHNEEaesl 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 487 KEHIACLRNERDVLREELADLRQTVTTAEkhglVIIPDSTpngdvhhepvvGAITAVSQEAAQVLESAGEGPLDV----- 561
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAR----EAVEDRR-----------EEIEELEEEIEELRERFGDAPVDLgnaed 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 562 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDIATLE 641
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEAL---LEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755532247 642 QSISRLEGQVLRYKTAAENAEKIEDeLKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 705
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAEDRIER-LEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-661 |
3.18e-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: 53.23 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 412 RENEEKSKELERQkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHia 491
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 492 cLRNERDVLREELADLRQTVTTAEKHG--LVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKLAGE 569
Cdd:COG4942 95 -LRAELEAQKEELAELLRALYRLGRQPplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 570 KDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEG 649
Cdd:COG4942 169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 755532247 650 QVLRYKTAAENA 661
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
331-687 |
5.75e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 331 DTSLSELRDIYDLKDQIHDVEGRY---MQGLKELKESLSEVEEKYKKA-----MVSNAQLDNEKnnlI--YQVDTLKdvI 400
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQEK---IerYQADLEE--L 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 401 EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTmtkevfdLQETLLWK 476
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARA---EAAEEEVDELKSQLADYQQALDVQQTraiqYQQAVQA-------LERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 477 DKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAVSQEAAQVLESage 556
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ--------------------------AAHSQFEQAYQL--- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 557 gpldvrLRKLAGEKD--ELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAE 634
Cdd:PRK04863 482 ------VRKIAGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532247 635 QDIATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAERRKLQR---ELRTAQDKIE 687
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQARIQRLAArapAWLAAQDALA 613
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-690 |
2.43e-06 |
|
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: 50.79 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 342 DLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 421
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 422 ERQKHMCSVLQHKMDELKEGLRQRDELIEEnqrLQQKVDTMTKEVFDLQETllwkdkalgaLEKQKEHIACLRNERDVLR 501
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKK---LQQEKELLEKEIERLKET----------IIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 502 EELADLRQTvTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLK 581
Cdd:TIGR04523 454 LIIKNLDNT-RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKIEKLE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 582 LQLEEERQKCSRndgMSGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDIATLEQSISRLEGQVLR 653
Cdd:TIGR04523 531 SEKKEKESKISD---LEDELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIKEIEE 607
|
330 340 350
....*....|....*....|....*....|....*..
gi 755532247 654 YKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 690
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-713 |
2.57e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 476 KDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAVSQEAAQvlesag 555
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----------------------RIRALEQELAA------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 556 egpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQ 635
Cdd:COG4942 81 ---LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------RE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532247 636 DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 713
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-607 |
3.38e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 338 RDIYDLKDQIHDVEGRymqgLKELKESLSEVEEKYkkamvsnAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEK 417
Cdd:TIGR02168 253 EELEELTAELQELEEK----LEELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 418 SKELERQKHMCSVLQHKMDELKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKalgALEKQKEHIACLRNER 497
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEE---KLEELKEELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 498 DVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDV--RLRKLAGEKDELLS 575
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeeALEELREELEEAEQ 475
|
250 260 270
....*....|....*....|....*....|..
gi 755532247 576 QIRKLKLQLEEERQKCSRNDGMSGDLAGLQNG 607
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
408-705 |
8.31e-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: 49.30 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 408 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGL----RQRDELIEENQRLQQKVDTMTKE-VFDLQETLLWKDKALGA 482
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 483 LEKQKEHIACLRNERDVLREELADLRQTVTTAEKHglviIPDSTPNGDVHHEPVVGAITA-VSQEAAQVLESAGE-GPLD 560
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERElEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 561 VRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAE 634
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532247 635 QDIATLEQSISRLEGQVLRYKTAAENAE-KIEDeLKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 705
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNaAIAG-IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
559-705 |
1.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 559 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCsrnDGMSGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 637
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 638 ATLEQSI-----------SRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 705
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
559-713 |
1.20e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 559 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 633
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 634 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 708
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 755532247 709 ALLAQ 713
Cdd:COG1579 167 ELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
358-702 |
2.59e-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: 47.20 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvlqhkmDE 437
Cdd:pfam07888 89 LRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK----------ER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 438 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkdkalgalEKQKEHIACLRNERDVLREELADLRQTVTTAEKH 517
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF----------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 518 glviipdstpngDVHHEPVVGAITAVsQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEerqkcsrndgM 597
Cdd:pfam07888 229 ------------EAENEALLEELRSL-QERLNASERKVEG-LGEELSSMAAQRDRTQAELHQARLQAAQ----------L 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 598 SGDLA--GLQNGSDLQFIEMQRDANRQISEY-KFKLSKAEQDIATLEQSI--SRLEGQVLRYKTAAE---------NAEK 663
Cdd:pfam07888 285 TLQLAdaSLALREGRARWAQERETLQQSAEAdKDRIEKLSAELQRLEERLqeERMEREKLEVELGREkdcnrvqlsESRR 364
|
330 340 350
....*....|....*....|....*....|....*....
gi 755532247 664 IEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 702
Cdd:pfam07888 365 ELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
547-714 |
3.85e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 547 AAQVLESAGEG--PLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAGLQnGSDLQFIEMQRDANRQIS 624
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQ-KELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 625 EYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 704
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 755532247 705 ANRTALLAQQ 714
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
356-706 |
8.90e-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: 45.97 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 356 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 427
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 428 ------CSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEhiaclrNER 497
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE------RED 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 498 DVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEpvvgaitavSQEAAQVLESAGEgpldvrlrklagEKDellSQI 577
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLID---------LKEHASSLASSGL------------KKD---SKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 578 RKLKLQLEEERQKCSRndgMSGDLAGLQNgsdlqfIEMQRDANRQISEykfklskaeqdiatleqSISRLEGQVLRYKTA 657
Cdd:pfam10174 520 KSLEIAVEQKKEECSK---LENQLKKAHN------AEEAVRTNPEIND-----------------RIRLLEQEVARYKEE 573
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755532247 658 AENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 706
Cdd:pfam10174 574 SGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN 622
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
382-690 |
8.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 382 LDNEKNNLiyqvDTLKDVIEEQEEQ-----MAEFYRENEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQ 456
Cdd:PRK02224 182 LSDQRGSL----DQLKAQIEEKEEKdlherLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 457 QKVDTMTKEVFDLQETllwkdkalgalekqkehIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepv 536
Cdd:PRK02224 251 EELETLEAEIEDLRET-----------------IAETEREREELAEEVRDLRERLEELEE-------------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 537 vgAITAVSQEAAqvLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGlqNGSDLQfiEMQ 616
Cdd:PRK02224 294 --ERDDLLAEAG--LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE--RAEELR--EEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 617 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAER-------RKLQRELRTAQDKIEEM 689
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdelrereAELEATLRTARERVEEA 445
|
.
gi 755532247 690 E 690
Cdd:PRK02224 446 E 446
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
358-702 |
9.51e-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: 45.87 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIE---------EQEEQMAE--FYRENEEKSKELERQKH 426
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrsmstqkalEEDLQIATktICQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 427 MCSVLQHKMDELKEGLRQRDELIE-ENQRLQQKVDTMTKEVFDLQETllwkdkalgalEKQKEHIACLRNERDVLREELA 505
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRtEQQRLEKNEDQLKIITMELQKK-----------SSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 506 DLrqtvtTAEKHGLViipdstpNGDVHHEPVVGAITAVSQEAAQVLESAGE--GPLDVRLRKLAGEKDELLSQIRKLKLQ 583
Cdd:pfam05483 412 KI-----LAEDEKLL-------DEKKQFEKIAEELKGKEQELIFLLQAREKeiHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 584 LEEERQKCSRndgmsgdlagLQNGSDLQFIEmQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVlryKTAAENAEK 663
Cdd:pfam05483 480 LEKEKLKNIE----------LTAHCDKLLLE-NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI---ENLEEKEMN 545
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 755532247 664 IEDELKAERRKLQR---ELRTAQDKIEEMEMTNSHLAKRLEK 702
Cdd:pfam05483 546 LRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-509 |
9.54e-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: 45.78 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 333 SLSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVE------EKYKKamvSNAQLDNEKNNLIYQVDTLKDVIEEQEE 405
Cdd:TIGR04523 336 IISQLNEqISQLKKELTNSESENSEKQRELEEKQNEIEklkkenQSYKQ---EIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 406 QMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE----NQRLQQKVDTMTKEVFDLQETLLWKDKALG 481
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
170 180
....*....|....*....|....*...
gi 755532247 482 alEKQKEHIAcLRNERDVLREELADLRQ 509
Cdd:TIGR04523 493 --SKEKELKK-LNEEKKELEEKVKDLTK 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
483-710 |
1.03e-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: 45.82 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 483 LEKQKEHIACLRNERDVLREELADLRQTVTTA--EKHGLVIIPDSTPNGDVHHEPVVGAITA-VSQEAAQVLESAGE-GP 558
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLrkELEELSRQISALRKDLARLEAEVEQLEErIAQLSKELTELEAEiEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 559 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDIA 638
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA---LDELRAELTLLNEEAANLRER-LESLERRIAATERRLE 841
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 639 TLEQSISRLEGQVLRY----KTAAENAEKIEDELKA---ERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 710
Cdd:TIGR02168 842 DLEEQIEELSEDIESLaaeiEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
348-704 |
1.04e-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: 45.88 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 348 HDVEgryMQGLKELKESL-SEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKH 426
Cdd:pfam15921 276 HEVE---ITGLTEKASSArSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 427 MCSvlqhkmDELKEGLRQRDELIEENQRLQqkvDTMTKEVFDLQEtllwKDKALgALEKQKEHIACLRNER-----DVLR 501
Cdd:pfam15921 353 LAN------SELTEARTERDQFSQESGNLD---DQLQKLLADLHK----REKEL-SLEKEQNKRLWDRDTGnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 502 EELADLRQTVTTAEkhGLVIIPDSTPNGDVHHEPVV-----GAITAVSQEAAQvLESAGEGPLDVrLRKLAGEKDELLSQ 576
Cdd:pfam15921 419 RELDDRNMEVQRLE--ALLKAMKSECQGQMERQMAAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 577 IRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ---------RDANRQISEYKFKLSKAEQDIATLEQSI--- 644
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenm 574
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532247 645 SRLEGQVLRYKTAAE-NAEKIEDELKAERRKLQrELRTAQD----KIEEMEMTNSHLakRLEKMK 704
Cdd:pfam15921 575 TQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQ-EFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
335-488 |
1.59e-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: 45.01 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 335 SELRDIYDLKDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEF---- 410
Cdd:TIGR04523 381 SYKQEIKNLESQINDLE----SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKelii 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 411 -----YREN-EEKSKELERQ-KHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEvfdlQETLLWKDKALGAL 483
Cdd:TIGR04523 457 knldnTRESlETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK----ISSLKEKIEKLESE 532
|
....*
gi 755532247 484 EKQKE 488
Cdd:TIGR04523 533 KKEKE 537
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
339-558 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 339 DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 415
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 416 EKSKE----------------LERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETllwKDKA 479
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 480 LGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGP 558
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
365-703 |
1.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 365 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSK---ELERQKHMCSVLQHKMDEL 438
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 439 KE---GLRQRDELIEENQR--------LQQKVDTMTKEVFDLQEtllwKDKALGALEKQKEHIACLRNERDVLREELADL 507
Cdd:PRK03918 237 KEeieELEKELESLEGSKRkleekireLEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 508 RQTVTTAEKHGLVIipdstpngdvhhepvvgaitavsQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKLK---LQL 584
Cdd:PRK03918 313 EKRLSRLEEEINGI-----------------------EERIKELEEKEE-----RLEELKKKLKELEKRLEELEerhELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 585 EEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDIATLEQSISRLEGQVLRYKTAAE----- 659
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvc 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755532247 660 NAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 703
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
336-707 |
2.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 336 ELRDIYDLKDQIHDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 411
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 412 RENEEKSKELERQKHMCSVLQHKMDELKEGLRQ----RDELIEENQrlQQKVDTMTKEVFDLQETLLWKDKALGALEKQK 487
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 488 EHI-ACLRNERDVLR-EELAD-LRQTVTTAEKHGLVIIPDSTPNgdvhHEPVVGAITAVSQEAAQVLESAGEG-PLDVRL 563
Cdd:PRK03918 483 RELeKVLKKESELIKlKELAEqLKELEEKLKKYNLEELEKKAEE----YEKLKEKLIKLKGEIKSLKKELEKLeELKKKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 564 RKLAGEKDELLSQIRKLKLQLEEERQKCSrnDGMSGDLAGLQNGSDlQFIEMqRDANRQISEYKFKLSKAEQDIATLEQS 643
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESV--EELEERLKELEPFYN-EYLEL-KDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 644 ISRLEGQVLRYKTAAENAEKIEDE-----LKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANR 707
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
344-710 |
2.64e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 344 KDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELER 423
Cdd:TIGR04523 116 KEQKNKLE----VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 424 QKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKalgALEKQKEHIACLRNERDVLREE 503
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT---EISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 504 LADLRQTVTTAEKhglvIIPDSTPNgdvhHEPVVGAITAVSQEAAQVLesagegpldvrLRKLAGEKDELLSQIRKLKLQ 583
Cdd:TIGR04523 269 LSEKQKELEQNNK----KIKELEKQ----LNQLKSEISDLNNQKEQDW-----------NKELKSELKNQEKKLEEIQNQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 584 LEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQrdanRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEK 663
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQ----RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 755532247 664 IEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 710
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
562-707 |
2.97e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 562 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 634
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532247 635 QDIATLEQSISRLEGQVlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEmemtnsHLAKRLEKMKANR 707
Cdd:COG1579 124 EELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-714 |
3.05e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 542 AVSQEAAQVLESAgEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNgsDLQFIEMQRDAN- 620
Cdd:TIGR02168 263 QELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRER----------LANLER--QLEELEAQLEELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 621 RQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDEL-------KAERRKLQRELRTAQDKIEEMEMTN 693
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlRSKVAQLELQIASLNNEIERLEARL 409
|
170 180
....*....|....*....|.
gi 755532247 694 SHLAKRLEKMKANRTALLAQQ 714
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKL 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
493-690 |
3.39e-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: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 493 LRNERDVLREELADLRQTVTTAE--------KHGLViipdstpngdvhhepvvgaitAVSQEAAQVLESAGEgpLDVRLR 564
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEaaleefrqKNGLV---------------------DLSEEAKLLLQQLSE--LESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 565 KLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgDLAGLQNGSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQS 643
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPD----------ALPELLQSPVIQQLRAQLaELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755532247 644 ISRLEGQVlryktaAENAEKIEDELKAERRKLQRELRTAQDKIEEME 690
Cdd:COG3206 300 IAALRAQL------QQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-705 |
3.52e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 342 DLKDQIHDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 412
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 413 ENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIAC 492
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 493 LRNERDVLRE---ELADLRQTVTTAEKHglviipdSTPNGDVHHEPVVGAITAVSQEAAQVLEsagegpldvRLRKLAGE 569
Cdd:PRK03918 350 LEKRLEELEErheLYEEAKAKKEELERL-------KKRLTGLTPEKLEKELEELEKAKEEIEE---------EISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 570 KDELLSQIRKLKL---QLEEERQKCSrndgmsgdlaglQNGSDLQfiemQRDANRQISEYKFKLSKAEQDIATLEQSISR 646
Cdd:PRK03918 414 IGELKKEIKELKKaieELKKAKGKCP------------VCGRELT----EEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755532247 647 L-------------EGQVLRYKTAAENAEKIEDELKA----ERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 705
Cdd:PRK03918 478 LrkelrelekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
331-710 |
3.78e-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: 44.17 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 331 DTSLSELRDIYDLKDQIHDVEGR--YMQG-LKELKESLSEVEEKYKKA-----MVSNAQLDNEKnnlI--YQ--VDTLKD 398
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRlvEMAReLEELSARESDLEQDYQAAsdhlnLVQTALRQQEK---IerYQedLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 399 VIEEQEEQMAEfyrENEEKSkELERQKHMCsvlQHKMDELKEGLRQRDELIEENQR----LQQKVDTMTKEVFDLQETLL 474
Cdd:COG3096 362 RLEEQEEVVEE---AAEQLA-EAEARLEAA---EEEVDSLKSQLADYQQALDVQQTraiqYQQAVQALEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 475 wkdkalgALEKQKEHIACLRNERDVLREELADLRQTVttaekhglviipdstpngdvhhepvvgaitAVSQEAAQVLESA 554
Cdd:COG3096 435 -------TPENAEDYLAAFRAKEQQATEEVLELEQKL------------------------------SVADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 555 GEgpldvRLRKLAGEKD---------ELLSQIRKLKLQLEeerqkcsRNDGMSGDLAGLQngsdlQFIEMQRDANRQISE 625
Cdd:COG3096 478 YE-----LVCKIAGEVErsqawqtarELLRRYRSQQALAQ-------RLQQLRAQLAELE-----QRLRQQQNAERLLEE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 626 YKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAERRKL-QREL--RTAQDKIEEM-EMTNS 694
Cdd:COG3096 541 FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAveqrselRQQLEQLRARIKELaARAPawLAAQDALERLrEQSGE 620
|
410
....*....|....*.
gi 755532247 695 HLAKRLEKMKANRTAL 710
Cdd:COG3096 621 ALADSQEVTAAMQQLL 636
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-590 |
5.67e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 331 DTSLSELRD-IYDLKDQIHDVEGRYMqglkELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 409
Cdd:COG1196 266 EAELEELRLeLEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 410 fyrENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEH 489
Cdd:COG1196 342 ---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 490 iacLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAGE 569
Cdd:COG1196 419 ---LEEELEELEEALAELEEEEEEEEE----------------------ALEEAAEEEAELEEEEEA--LLELLAELLEE 471
|
250 260
....*....|....*....|.
gi 755532247 570 KDELLSQIRKLKLQLEEERQK 590
Cdd:COG1196 472 AALLEAALAELLEELAEAAAR 492
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
334-561 |
6.04e-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: 42.92 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 334 LSELR-DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSN------------AQLDNEKNNLIYQVDTL---- 396
Cdd:pfam06160 181 LEKLEeETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalehlnvdkeiQQLEEQLEENLALLENLelde 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 397 -KDVIEEQEEQMAEFYR--ENEEKSKE--LERQKHMCSVLQHKMDELKEGL------------------------RQRDE 447
Cdd:pfam06160 261 aEEALEEIEERIDQLYDllEKEVDAKKyvEKNLPEIEDYLEHAEEQNKELKeelervqqsytlnenelervrgleKQLEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 448 LIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQ----KEHIACLRNERDVLREELADLRQTVTT----AEKHGL 519
Cdd:pfam06160 341 LEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEqeefKESLQSLRKDELEAREKLDEFKLELREikrlVEKSNL 420
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755532247 520 VIIPDStpngdvhhepVVGAITAVSQEAAQVLESAGEGPLDV 561
Cdd:pfam06160 421 PGLPES----------YLDYFFDVSDEIEDLADELNEVPLNM 452
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
360-714 |
6.14e-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: 43.50 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 360 ELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQ---------MAEFYRENEEKSKELERQKHmcsv 430
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIAQQAA---- 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 431 lqhKMDELkEGLRQRDELIEENQRLQQKVDTMTKEVFDLQEtllwkdkalgALEKQKEHIACLRNERDVLREELADLRQT 510
Cdd:TIGR00606 814 ---KLQGS-DLDRTVQQVNQEKQEKQHELDTVVSKIELNRK----------LIQDQQEQIQHLKSKTNELKSEKLQIGTN 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 511 VTTAEKHGLVIIPDSTPngdvhhepVVGAITAVSQEAAQVLesagegPLDVRLRKLAGEKDELLSQI----RKLKLQLEE 586
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTE--------VQSLIREIKDAKEQDS------PLETFLEKDQQEKEELISSKetsnKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 587 ERQKCSRNDGMSGDLAG-LQNGSDLQFIEMQRDANR---QISEYKFKLSKAEQDIATLEQSIsrlEGQVLRYKTAAEN-- 660
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENkIQDGKDDYLKQKETELNTvnaQLEECEKHQEKINEDMRLMRQDI---DTQKIQERWLQDNlt 1022
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755532247 661 AEKIEDELKAERRKLQRELR-TAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 714
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKeMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ 1077
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
334-713 |
6.15e-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: 43.18 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 334 LSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLkdvieeqeeqMAEFYR 412
Cdd:pfam15921 319 LSDLEStVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL----------LADLHK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 413 ENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALG-ALEKQKEHIA 491
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNeSLEKVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 492 CLRNERDVLR---EELADLRQTVTTAEKhglviipdstpngdvhhepVVGAITAVSQEAAQVLESAG------EGPLDVR 562
Cdd:pfam15921 469 QLESTKEMLRkvvEELTAKKMTLESSER-------------------TVSDLTASLQEKERAIEATNaeitklRSRVDLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 563 LRKLAGEKDE------LLSQIRKLKLQLEEE-------RQKCSRND---GMSGDLAGLQNGSDLQFIEMQRDANRQISEY 626
Cdd:pfam15921 530 LQELQHLKNEgdhlrnVQTECEALKLQMAEKdkvieilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEF 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 627 KFKLSKAEQDIATLEQSISRLEGQVLR---------------------------------------YKTAAENAEKIEDE 667
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDLELEKVKlvnagserlravkdikqerdqllnevktsrnelnslsedYEVLKRNFRNKSEE 689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 755532247 668 LKAERRKLQRELRTAQDKIEE-------MEMTNSHLAKRLEKMKANRTALLAQ 713
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQtrntlksMEGSDGHAMKVAMGMQKQITAKRGQ 742
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
356-509 |
6.88e-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: 42.44 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 356 QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL---- 431
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 432 --QHKMDELKEGLRQRD--ELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADL 507
Cdd:COG4942 114 yrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
..
gi 755532247 508 RQ 509
Cdd:COG4942 194 KA 195
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
562-714 |
8.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 562 RLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAglQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDIATL 640
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELE--QARSELEQLEEElEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755532247 641 EQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 714
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
400-705 |
9.88e-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: 42.40 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 400 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVD--------------TMTKE 465
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEelkgkeqelifllqAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 466 VFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQ 545
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 546 EAAQVlESAGEGPLDVRlRKLAGEKDELLSQIRKLKLQLEEerqkcSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISE 625
Cdd:pfam05483 532 MLKQI-ENLEEKEMNLR-DELESVREEFIQKGDEVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 626 YKFKlskaeqDIATLEQsisrlEGQVLRYKTAAENAE---------KIEDELKAERRKLQRELRTAQDKIEEMEMTNSHL 696
Cdd:pfam05483 605 NKNK------NIEELHQ-----ENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL 673
|
....*....
gi 755532247 697 AKRLEKMKA 705
Cdd:pfam05483 674 LEEVEKAKA 682
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-710 |
1.06e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 361 LKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM---------AEFYRENEEKSKELERQKHmcSVL 431
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREER--DEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 432 QHKMDELKEGLRQRDELIEENQRLQQ--KVDTMTKEVFDlqetllwkDKALGALEKQKEHIACLRNERDVLREELADLRQ 509
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEagKCPECGQPVEG--------SPHVETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 510 TVTTAEKhgLVIIPDSTPNGDVHHEPVVGAIT-------------AVSQEAAQVLESAGEGPLDvRLRKLAGEKDELLSQ 576
Cdd:PRK02224 497 RLERAED--LVEAEDRIERLEERREDLEELIAerretieekreraEELRERAAELEAEAEEKRE-AAAEAEEEAEEAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 577 IRKLKLQLEEERQKCSRNDGMSGDLAGLQN-GSDLQFIEMQRDA-NRQISEYKFKLSKAEQDIATLEQSI--SRLEGQVL 652
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLAAIADaEDEIERLREKREAlAELNDERRERLAEKRERKRELEAEFdeARIEEARE 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755532247 653 RYKTAAENAEKIE---DELKAERRKLQRELRTAQDKIEEMEmtnsHLAKRLEKMKANRTAL 710
Cdd:PRK02224 654 DKERAEEYLEQVEeklDELREERDDLQAEIGAVENELEELE----ELRERREALENRVEAL 710
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-714 |
1.08e-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: 42.06 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 619 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAK 698
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 755532247 699 RLEKMKAnrtaLLAQQ 714
Cdd:COG4942 98 ELEAQKE----ELAEL 109
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
617-705 |
1.21e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 617 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaerRKLQRELRTAQDKIEEMEMTNSHL 696
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491
|
....*....
gi 755532247 697 AKRLEKMKA 705
Cdd:COG2433 492 KRKLERLKE 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
359-705 |
1.37e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 359 KELKESLSEVEE-KYKKAMVSNAQldnEKNNLIYQVDTL---KDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 434
Cdd:TIGR00618 260 QLLKQLRARIEElRAQEAVLEETQ---ERINRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 435 MDELKEGLRQRDELIEENQRLQQKVD--TMTKEVFDLQETLLwkdKALGALEKQKEHIA----CLRNERDVLREELA--D 506
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLT---QHIHTLQQQKTTLTqklqSLCKELDILQREQAtiD 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 507 LRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQvlesagEGPLDVRLRKLAGEKDELLSQIRKLKLQLEE 586
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL------EKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 587 ERQKcsrndgmsgdlaglqngsDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIED 666
Cdd:TIGR00618 488 KKAV------------------VLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
330 340 350
....*....|....*....|....*....|....*....
gi 755532247 667 ELKAERRKLQRElrtaQDKIEEMEMTNSHLAKRLEKMKA 705
Cdd:TIGR00618 550 QLTSERKQRASL----KEQMQEIQQSFSILTQCDNRSKE 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-713 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 567 AGEKDELLSQIRKLKLQLEEERQKCSRNDGmsgdlagLQNGSDLQFIEMQRDANRQiseykfKLSKAEQDIATLEQSISR 646
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA------ELEELRAELARLEAELER 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532247 647 LEGQvlryktaaenaekiEDELKAERRKLQRELRTAQ-DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 713
Cdd:COG4913 314 LEAR--------------LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
559-713 |
1.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 559 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFklskAEQDIA 638
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQE--------------------------RREALQRLAEYSW----DEIDVA 664
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532247 639 TLEQSISRLEGQvlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 713
Cdd:COG4913 665 SAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
354-714 |
1.73e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 354 YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL-- 431
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELek 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 432 -----------------QHKMDELKEGLRQRDELIEENQ-----------RLQQKVDTMTKEVFDLQETLLWKDKALGal 483
Cdd:TIGR04523 289 qlnqlkseisdlnnqkeQDWNKELKSELKNQEKKLEEIQnqisqnnkiisQLNEQISQLKKELTNSESENSEKQRELE-- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 484 EKQKEhIACLRNERDVLREELADLRQTVTTAEKHglviipdstpngdvhhepvvgaITAVSQEAAQvlesagegpLDVRL 563
Cdd:TIGR04523 367 EKQNE-IEKLKKENQSYKQEIKNLESQINDLESK----------------------IQNQEKLNQQ---------KDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 564 RKLAGEKDELLSQIRKLKLQLEEERQKCSrndgmsgDLAGLQNGSDLQFIEMQR---DANRQISEYKFK----------- 629
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNtreSLETQLKVLSRSinkikqnleqk 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 630 ---LSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTN---------SHLA 697
Cdd:TIGR04523 488 qkeLKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKN 567
|
410
....*....|....*..
gi 755532247 698 KRLEKMKANRTALLAQQ 714
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQ 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-690 |
1.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMcsvlqHKMDE 437
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-----EADYE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 438 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKQ---------KEHIACLRNERDVLREEL---- 504
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL---EAALAAALQNivveddevaAAAIEYLKAAKAGRATFLpldk 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 505 ----ADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGE--GPLDVRLRKLAGEKDELLS--- 575
Cdd:COG1196 582 irarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRraVTLAGRLREVTLEGEGGSAggs 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 576 ----QIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQV 651
Cdd:COG1196 662 ltggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
330 340 350
....*....|....*....|....*....|....*....
gi 755532247 652 LRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 690
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
346-701 |
2.38e-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: 41.31 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 346 QIHDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 424
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 425 khmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKE---------------- 488
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtqellqeetrqklnl 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 489 --HIACLRNERDVLREELADLRQTVTTAEKHGLViipdstpngdvhHEPVVGAITAVSQEAAQVLESAGEGpldvrlrkl 566
Cdd:pfam01576 488 stRLRQLEDERNSLQEQLEEEEEAKRNVERQLST------------LQAQLSDMKKKLEEDAGTLEALEEG--------- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 567 ageKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGlqngsDLQFIEMQRDANRQI-SEYKFKLSKAEQDIATlEQSIS 645
Cdd:pfam01576 547 ---KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQLvSNLEKKQKKFDQMLAE-EKAIS 617
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755532247 646 rlegqvLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLE 701
Cdd:pfam01576 618 ------ARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-688 |
2.42e-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: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 619 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEE 688
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
334-466 |
2.61e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 334 LSELRDIYD-LKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 407
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 408 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQR-DELIEENQRLQQKVDTMTKEV 466
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-560 |
2.69e-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: 41.21 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 338 RDIYDLKDQIHDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 414
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 415 EEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE-NQRL------QQKVDTMTKEVFDLQETLLWKDKALGA-LEKQ 486
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADlNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAAdLSKY 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 487 KEHIACLRNERDVLREELADLRQTVTTAEKHGLVI---IPDSTPNGDVHHEPVVGAITAVSQ------EAAQVLESAGEG 557
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeerVRGGRAVEEVLKASIQGVHGTVAQlgsvgeRYATAIEVAAGN 547
|
...
gi 755532247 558 PLD 560
Cdd:TIGR02169 548 RLN 550
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-706 |
2.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 334 LSELRDIY-DLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAmvsnAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 412
Cdd:PRK03918 298 LSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 413 ENEEKSK----ELERQKHMCSVLQHKMDELKEglrQRDELIEENQRLQQKVDTMTKEVFDLQET---------LLWKDKA 479
Cdd:PRK03918 374 LERLKKRltglTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 480 LGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngDVHHEPVVGAITAVSQEAAQVLESAGEGPL 559
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK-------------VLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 560 DvRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNgsDLQFIEMQR-DANRQISEYKFKlskaeqDIA 638
Cdd:PRK03918 518 E-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--KLDELEEELaELLKELEELGFE------SVE 588
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532247 639 TLEQSISRLEGQVLRYKTAAENAEKIEDELKaERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 706
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
358-697 |
3.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 437
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 438 LKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALG----ALEKQKEHIACLRNERDVLREELADLRQTVTT 513
Cdd:PRK02224 361 LRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDELREREAELEATLRT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 514 AEKhglviipdstpngdvhhepvvgaitavSQEAAQVLESAGEGP---LDVRLRKLAGEKDELLSQIRKLKLQLEEERQK 590
Cdd:PRK02224 438 ARE---------------------------RVEEAEALLEAGKCPecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 591 CSRNDgmsgdlaglqngSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEqsiSRLEGQVLRYKTAAENAEKIEDELKA 670
Cdd:PRK02224 491 VEEVE------------ERLERAEDLVEAEDRIERLEERREDLEELIAERR---ETIEEKRERAEELRERAAELEAEAEE 555
|
330 340
....*....|....*....|....*..
gi 755532247 671 ERRKLQRELRTAQDKIEEMEMTNSHLA 697
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
614-712 |
3.82e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 614 EMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtn 693
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90
....*....|....*....
gi 755532247 694 shlaKRLEKMKANRTALLA 712
Cdd:COG4942 97 ----AELEAQKEELAELLR 111
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-679 |
3.92e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEekykkamvsnAQLDNEKnnliyqvDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 437
Cdd:COG1196 255 LEELEAELAELE----------AELEELR-------LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 438 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHiacLRNERDVLREELADLRQTVTTAEKh 517
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALR- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 518 glviipdstpngdvhhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKcsrndgm 597
Cdd:COG1196 394 ---------------------AAAELAAQLEELEEAEEA--LLERLERLEEELEELEEALAELEEEEEEEEEA------- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 598 sgdlAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQR 677
Cdd:COG1196 444 ----LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
..
gi 755532247 678 EL 679
Cdd:COG1196 520 RG 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
360-707 |
4.34e-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: 40.49 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 360 ELKESLSEVEEKYKKAMVSNAQLDNE-KNNLIYQVDTLKDVIEEQEEQMAE------FYRENEEKSKELERQKHMCSVLQ 432
Cdd:pfam17380 244 NLAEDVTTMTPEYTVRYNGQTMTENEfLNQLLHIVQHQKAVSERQQQEKFEkmeqerLRQEKEEKAREVERRRKLEEAEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 433 HKMDELK-------EGLRQRDELIEENQRLQQKVDTMTKEVFDLQETL--LWKDKALGALEKQKEHiaclRNERdvLREE 503
Cdd:pfam17380 324 ARQAEMDrqaaiyaEQERMAMERERELERIRQEERKRELERIRQEEIAmeISRMRELERLQMERQQ----KNER--VRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 504 LADLRQTVTTAEKHGLVIIPDSTPNGDVHHEPvvgaiTAVSQEAAQVLESAGEGPLDvRLRKlagEKDELLSQIRKLKLQ 583
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQ-----EEARQREVRRLEEERAREME-RVRL---EEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 584 LEEERQKCSRNDGMSGDLAGLQNgSDLQFIEMQRDANRQ-ISEYKFKLSKAEQDIATLEQSISRLEGqvlRYKTAAENAE 662
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEE-QRRKILEKELEERKQaMIEEERKRKLLEKEMEERQKAIYEEER---RREAEEERRK 544
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 755532247 663 KIEDElkaERRKLQRELRTAQD---KIEEMEMTNSHLAKRLEKMKANR 707
Cdd:pfam17380 545 QQEME---ERRRIQEQMRKATEersRLEAMEREREMMRQIVESEKARA 589
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
540-714 |
4.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 540 ITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCS-------RNDGMSGDLAGLQNGSDLQ- 611
Cdd:COG3883 39 LDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 612 FIE-------MQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQD 684
Cdd:COG3883 117 FLDrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|
gi 755532247 685 KIEEMEMTNSHLAKRLEKMKANRTALLAQQ 714
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
358-710 |
4.51e-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: 40.54 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdviEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 437
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNAL-----------QEQLQAETELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 438 LKEglrqrdELIEENQRLQQKVDTMTKEVFDLQETL-----------LWKDKALGALEKQKEHIACLRN-------ERDV 499
Cdd:pfam01576 83 RLE------EEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaarqklqLEKVTTEAKIKKLEEDILLLEDqnsklskERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 500 LREELADLRQTVTTAEKHGlviipDSTPNGDVHHEPVVGAItavsqEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRK 579
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKA-----KSLSKLKNKHEAMISDL-----EERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 580 LKLQLEEERQKCSRNDgmsGDLAGLQNGSD------LQFIEMQRDANRQISEYKFKL-------SKAEQDIATLEQSISR 646
Cdd:pfam01576 227 LQAQIAELRAQLAKKE---EELQAALARLEeetaqkNNALKKIRELEAQISELQEDLeseraarNKAEKQRRDLGEELEA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532247 647 LEGQVLRY--KTAA--ENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSH----LAKRLEKMKANRTAL 710
Cdd:pfam01576 304 LKTELEDTldTTAAqqELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANL 375
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
358-513 |
5.50e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 358 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN---EEKSKELERqkhmcsvLQHK 434
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIER-------LEWR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 435 MDELKEGLRQRDELIEENQRLQQKVDTMTKEvfdlqetllwkdkalgalEKQKEHIACLRNERDVLREELADLRQTVTT 513
Cdd:COG1340 125 QQTEVLSPEEEKELVEKIKELEKELEKAKKA------------------LEKNEKLKELRAELKELRKEAEEIHKKIKE 185
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
566-710 |
5.80e-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: 39.66 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 566 LAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglQNGSDLQfiemqrDANRQISEYKFKLSKAEQ----DIATLE 641
Cdd:pfam15742 81 LTAEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLA--QEKSRVA------DAEEKILELQQKLEHAHKvcltDTCILE 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532247 642 QSisRLEGQVlryKTAAENAEKIEDELKAERRK----------LQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 710
Cdd:pfam15742 153 KK--QLEERI---KEASENEAKLKQQYQEEQQKrklldqnvneLQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQL 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
355-710 |
6.41e-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: 40.03 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 355 MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN--NLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQ 432
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERELSKAEKNSLteTLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 433 HKMDE----LKEGLRQRDELIEE------NQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIaclRNERDVLRE 502
Cdd:TIGR00606 543 DKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI---NNELESKEE 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 503 ELADLRQTV-----TTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVL-ESAGEGPLDVRLRKLAGEKDELLSQ 576
Cdd:TIGR00606 620 QLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQSCCPVCQRVFQTEAELQEFISD 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 577 IR--------KLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAEQ------- 635
Cdd:TIGR00606 700 LQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNRDIQRLKNDIEEQETllgtimp 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 636 ----------DIATLEQSISRLEGQVLRYKTAAENAEKIE-----DELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRL 700
Cdd:TIGR00606 780 eeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
410
....*....|
gi 755532247 701 EKMKANRTAL 710
Cdd:TIGR00606 860 QHLKSKTNEL 869
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
353-690 |
6.58e-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: 40.03 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 353 RYMQGLKELKESLSEVEEKYKKAMvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHmcSVLQ 432
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ--RTVR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 433 HKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVfdlqetllwkdkalGALEKQKEHIACLRNERDVLREELAdlrqtvT 512
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQ--------------GRLQLQADRHQEHIRARDSLIQSLA------T 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 513 TAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCS 592
Cdd:TIGR00606 376 RLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK-ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 593 RNDGMSGDLAGLQNGSDlqfiemqrdanrQISEYKFKLSKAEQDIATLEQSisrlegqvlrykTAAENAEKIEDELKAER 672
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSD------------RILELDQELRKAERELSKAEKN------------SLTETLKKEVKSLQNEK 510
|
330
....*....|....*...
gi 755532247 673 RKLQRELRTAQDKIEEME 690
Cdd:TIGR00606 511 ADLDRKLRKLDQEMEQLN 528
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
338-525 |
8.41e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.43 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 338 RDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNekNNLIYQVDTLKDVIEEQEEQMAEFYREN-EE 416
Cdd:PRK04778 205 EELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELDLDEaEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 417 KSKELERQ-KHMCSVLQH----------KMDELKEGL----RQRDELIEENQRLQQK-----------------VDTMTK 464
Cdd:PRK04778 283 KNEEIQERiDQLYDILERevkarkyvekNSDTLPDFLehakEQNKELKEEIDRVKQSytlneselesvrqlekqLESLEK 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 465 EVFD--------------LQETLLWKDKALGALEKQ----KEHIACLRNERDVLREELADLRQTVTTA----EKHGLVII 522
Cdd:PRK04778 363 QYDEiteriaeqeiayseLQEELEEILKQLEEIEKEqeklSEMLQGLRKDELEAREKLERYRNKLHEIkrylEKSNLPGL 442
|
...
gi 755532247 523 PDS 525
Cdd:PRK04778 443 PED 445
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
369-690 |
9.46e-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: 39.17 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 369 EEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDELKEGLRQRDEL 448
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENA---NNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 449 I----------------EENQRLQQKVDTMTKEVFDLQETLLWK----DKALGALEKQKEHIACLRNERDvLREELADLR 508
Cdd:COG5185 305 IdikkatesleeqlaaaEAEQELEESKRETETGIQNLTAEIEQGqeslTENLEAIKEEIENIVGEVELSK-SSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 509 QTVTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVlesagEGPLDVRLRKLAgekdellsQIRKLKLQLEEER 588
Cdd:COG5185 384 DTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEEL-----QRQIEQATSSNE--------EVSKLLNELISEL 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532247 589 QKCSRNdgmsgdlagLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISR-LEGQVLRYKTAAENAEKIEDE 667
Cdd:COG5185 451 NKVMRE---------ADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAtLEKLRAKLERQLEGVRSKLDQ 521
|
330 340
....*....|....*....|...
gi 755532247 668 LKAERRKLQRELRTAQDKIEEME 690
Cdd:COG5185 522 VAESLKDFMRARGYAHILALENL 544
|
|
| |
