|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
264-618 |
2.61e-101 |
|
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: 312.40 E-value: 2.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 264 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqihdvegrym 334
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 335 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 414
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 415 DELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdktigalekqkehiaclrnerdvlreeladlqqtvktaE 494
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 495 KHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAEEKDELLSQIRKLKLQLEEERQ-KCSRN 573
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 672063398 574 DGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 618
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-668 |
1.86e-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: 67.77 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 337 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHkmdE 416
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK---E 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 417 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKTIGALEKQKEHIACLRNERDVLREELADLQQTVKTAEKh 496
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 497 glviipestpngdvNHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAEEKDELLSQI-RKLKLQLEEERQKCSRNDG 575
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELeALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 576 MSgDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDIATLEQSISRlegqvlRYKTAAENAEKIEDELKAEKR 652
Cdd:TIGR02168 896 LE-ELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 672063398 653 KLQRELRTAQDKIEEM 668
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-668 |
1.75e-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: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 314 SELRDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 393
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 394 EEKSKELERQKHMCSVLQHKMDELKEGLRqrdELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIgalEKQKEHIACLR 473
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELT---LLNEEAANLRERLESLERRIAATERRLEDLEEQI---EELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 474 NERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgaITAVSQEAAQVLESAGEGpLDVRLRKLAEEKDELL 553
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLN-----------------------ERASLEEALALLRSELEE-LSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 554 SQIRKLKLQLEEERQKCSrndGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLeGQV-LR 632
Cdd:TIGR02168 915 RELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL-GPVnLA 990
|
330 340 350
....*....|....*....|....*....|....*.
gi 672063398 633 YKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEM 668
Cdd:TIGR02168 991 AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-669 |
1.94e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 291 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQIHDVegryMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIY 370
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 371 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLR--QRDELIEENQRLQQKVDTMTKEVFDL 448
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 449 QETLLWKDKTIGALEKQKEHiacLRNERDVLREELADLQQTVKTAEKHglviipestpngdvnhepvVGAITAVSQEAAQ 528
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEKE-------------------IENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 529 VLE--SAGEGPLDVRLRKLAEEKDELLSQIRKLKL---QLEEERQKcsRNDGMSGDLAGLQNGSD-LQFIEMQRDANRQI 602
Cdd:TIGR02169 869 ELEelEAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLSELKAKLEALEEeLSEIEDPKGEDEEI 946
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672063398 603 SEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEME 669
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
360-669 |
2.47e-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: 57.37 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 360 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRE--NEEKS--------------KELERQKHMCSVLQHKM 414
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKElkAELRElelallvlrleelrEELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 415 DELKEGLRQRDELIEENQRLQQKVDtmtKEVFDLQETLLWKDKTIGALEKQKEHI----ACLRNERDVLREELADLQQTV 490
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILrerlANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 491 KTAEKHgLVIIPESTPNGDVNHEPVVGAITAvSQEAAQVLESAGEGpLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKC 570
Cdd:TIGR02168 333 DELAEE-LAELEEKLEELKEELESLEAELEE-LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 571 SRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEqdIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAE 650
Cdd:TIGR02168 410 ER-----------LEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330
....*....|....*....
gi 672063398 651 KRKLQRELRTAQDKIEEME 669
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLE 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
313-681 |
5.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 313 LSELRDIYDLKDQIHDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 392
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 393 NEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWkdKTIGALEKQKEHIACL 472
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 473 RNERDVLREELADLQQTVKTAEK--HGLVIIPESTPNGDVNHEP-----VVGAITAVSQEAAQVLESAGE---------G 536
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEelEQLENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTiagvlflvlG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 537 PLDVRLRKLAEEKDELLSQIRKLKLQLEEERqkcSRNDGMSGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSKAEQDI 616
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEE---LEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672063398 617 ATLEQSISRLEGQVLRYKTAAENAEKIED--ELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 681
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
308-684 |
9.90e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 308 DPDTSLSELRDIYDLKDQ--IHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQ 382
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 383 EEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDLQETLLWKDKTIGAL 462
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE---AVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 463 EKQ----KEHIACLRNERDVLREELADLQQTVKTAEkhglviipestpngdVNHEPVVGAITAVSQEAAQVLESAGEGPL 538
Cdd:PRK02224 341 NEEaeslREDADDLEERAEELREEAAELESELEEAR---------------EAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 539 DV-----RLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAE 613
Cdd:PRK02224 406 DLgnaedFLEELREERDELREREAELEATLRTARERVEEAEAL---LEAGKCPECGQPVEGSPHVET-IEEDRERVEELE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672063398 614 QDIATLEQSISRLEGQVLRYKTAAENAEKIEDelKAEKRKLQRELR-TAQDKIEEMEMTNSHLAKRLEKMKA 684
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-640 |
2.98e-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: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 391 RENEEKSKELERQkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQkehIA 470
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 471 CLRNERDVLREELADLqqtVKTAEKHG-----LVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKL 545
Cdd:COG4942 94 ELRAELEAQKEELAEL---LRALYRLGrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 546 AEEKDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISR 625
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*
gi 672063398 626 LEGQVLRYKTAAENA 640
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-693 |
4.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 375 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMDELKEGLRQRDELIEENQRlqqkvdtmtkev 445
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEA------------ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 446 fdlqetllwkdktigALEKQKEHIACLRNERDVLREELADLQQTVKTAEkhglviipestpngdvnhepvvGAITAVSQE 525
Cdd:COG1196 254 ---------------ELEELEAELAELEAELEELRLELEELELELEEAQ----------------------AEEYELLAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 526 AAQVLEsagegpldvRLRKLAEEKDELLSQIRKLKLQLEEERQKcsrndgmsgdlaglqngsdlqfiemQRDANRQISEY 605
Cdd:COG1196 297 LARLEQ---------DIARLEERRRELEERLEELEEELAELEEE-------------------------LEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 606 KFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 685
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
....*...
gi 672063398 686 RTALLAQQ 693
Cdd:COG1196 423 LEELEEAL 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
462-692 |
3.89e-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: 49.76 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 462 LEKQKEHIACLRNERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQvlesagegpLDVR 541
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALAR----------------------RIRALEQELAA---------LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 542 LRKLAEEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIATLEQ 621
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672063398 622 SISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 692
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
538-684 |
4.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 538 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCsrnDGMSGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 616
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672063398 617 ATLEQSI-----------SRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 684
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-684 |
4.28e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 387 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGL----RQRDELIEENQRLQQKVDTMTKE-VFDLQETLLWKDKTIGA 461
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 462 LEKQKEHIACLRNERDVLREELADLQQTVKTAEKHglviIPESTPNGDVNHEPVVGAITA-VSQEAAQVLESAGE-GPLD 539
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERElEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 540 VRLRKLAEEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAE 613
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672063398 614 QDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 684
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
321-669 |
4.83e-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: 50.02 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 321 DLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 400
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 401 ERQKHMCSVLQHKMDELKEGLRQRDELIEEnqrLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQ----KEHIACLRNER 476
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKK---LQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 477 DVLREELADLQQTVKTAEKhglviipestpngdvNHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAEEKDELLSQI 556
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQ---------------NLEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 557 RKLKLQLEEERQKCSRndgMSGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDIATLEQSISRLEG 628
Cdd:TIGR04523 527 EKLESEKKEKESKISD---LEDELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 672063398 629 QVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEME 669
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-586 |
7.66e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 317 RDIYDLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNL-----IYQV--DTLKDVIEEQEEQMAEF 389
Cdd:TIGR02168 253 EELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLeqqkqILRErlANLERQLEELEAQLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 390 YRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE----NQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQ 465
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElesrLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 466 KEHIAclrNERDVLREELADLQQTVKTAEKhglviipestpngdvnhEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKL 545
Cdd:TIGR02168 409 LERLE---DRRERLQQEIEELLKKLEEAEL-----------------KELQAELEELEEELEELQEELER--LEEALEEL 466
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672063398 546 AEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNG 586
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-689 |
8.39e-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: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 341 KESLSEVEEKYKKAMVsnaqLDNEKNNliyQVDTLKDvieeqEEQMAEFYRENEEKSKELERQKHMCSVLQHKmDELKEG 420
Cdd:TIGR02169 176 LEELEEVEENIERLDL----IIDEKRQ---QLERLRR-----EREKAERYQALLKEKREYEGYELLKEKEALE-RQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 421 LRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQ-----KEHIACLRNERDVLREELADLQQTVKTAEK 495
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 496 HgLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLEsagegpldvRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRndg 575
Cdd:TIGR02169 323 R-LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE---------EYAELKEELEDLRAELEEVDKEFAETRDELKD--- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 576 MSGDLAGLQNGSDlqfiEMQRDANRQISEykfkLSKAEQDIATLEQSISRLEGQVLRYKTAAENA----EKIEDELK--- 648
Cdd:TIGR02169 390 YREKLEKLKREIN----ELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqla 461
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 672063398 649 AEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 689
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
460-680 |
1.08e-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: 48.90 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 460 GALEKQKEHIACLRNERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQVLEsagegpld 539
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE-------- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 540 vRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNgsdlqfiemqrDANRQISEYKFKLSKAEQDIATL 619
Cdd:TIGR02168 713 -ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-----------ELEAEIEELEERLEEAEEELAEA 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672063398 620 EQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLE 680
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
310-666 |
2.73e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 310 DTSLSELRDIYDLKDQIHDVEGRY---MQGLKELKESLSEVEEKYKKA-----MVSNAQLDNEKNNLiYQVDTLKdvIEE 381
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQEKIER-YQADLEE--LEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 382 QEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTmtkevfdLQETLLWKDK 457
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARA---EAAEEEVDELKSQLADYQQALDVQQTraiqYQQAVQA-------LERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 458 TIGALEKQKEHIACLRNERDVLREELADLQQTVKTAEkhglviipestpngdvnhepvvgaiTAVSQ--EAAQVLESAGe 535
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ-------------------------AAHSQfeQAYQLVRKIA- 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 536 GPLDvrlRKLAEEkdellsQIRKLKLQLEEERQKCSRNDGMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQD 615
Cdd:PRK04863 487 GEVS---RSEAWD------VARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLLAEFCKRLGKNLDD 552
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672063398 616 IATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAEKRKLQR---ELRTAQDKIE 666
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQARIQRLAArapAWLAAQDALA 613
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
526-693 |
3.15e-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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 526 AAQVLESAGEG--PLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAGLQnGSDLQFIEMQRDANRQIS 603
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQ-KELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 604 EYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 683
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 672063398 684 ANRTALLAQQ 693
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
344-682 |
3.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 344 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERqkhmcsvLQHKMDELKEG 420
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPE-------LREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 421 LRQRDELIEENQRLQQKVDTMTKEVFDLQEtllwkdkTIGALEKQkehIACLRNERDVLREELADLQQTVKTAEKHglVI 500
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEE-------KIRELEER---IEELKKEIEELEEKVKELKELKEKAEEY--IK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 501 IPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGPLDV-RLRKLAEEKDELLSQIRKLK---LQLEEERQKCSRNDGM 576
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 577 SGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDIATLEQSISRLEGQVLRYKTAAE-----NAEKIEDELKAEK 651
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGRELTEEHRKELL 454
|
330 340 350
....*....|....*....|....*....|.
gi 672063398 652 RKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 682
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
462-689 |
3.23e-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: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 462 LEKQKEHIACLRNERDVLREELADLQQTVKTA--EKHGLVIIPESTPNGDVNHEPVVGAITA-VSQEAAQVLESAGE-GP 537
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLrkELEELSRQISALRKDLARLEAEVEQLEErIAQLSKELTELEAEiEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 538 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDL---AGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQ 614
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672063398 615 DIATLEQSISRLEGQVLRYKTAAEnaeKIEDELKA---EKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 689
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIE---ELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
335-685 |
4.03e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 335 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 406
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 407 ------CSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEhiaclrNER 476
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE------RED 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 477 DVLREELADLQQTVKTAEKHGLVIIPESTPNGDVNHEpvvgaitavSQEAAQVLESAGEgpldvrlrklaeEKDellSQI 556
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLID---------LKEHASSLASSGL------------KKD---SKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 557 RKLKLQLEEERQKCSRndgMSGDLAGLQNgsdlqfIEMQRDANRQISEykfklskaeqdiatleqSISRLEGQVLRYKTA 636
Cdd:pfam10174 520 KSLEIAVEQKKEECSK---LENQLKKAHN------AEEAVRTNPEIND-----------------RIRLLEQEVARYKEE 573
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 672063398 637 AENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 685
Cdd:pfam10174 574 SGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN 622
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
538-692 |
4.39e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 538 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 612
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 613 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 687
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 672063398 688 ALLAQ 692
Cdd:COG1579 167 ELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
323-689 |
7.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 323 KDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELER 402
Cdd:TIGR04523 116 KEQKNKLE----VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 403 QKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKTIGALEKQKEHIACLRNERDVLREE 482
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 483 LADLQQTVKTAEKhglVIIPESTPNGDVNHEpvvgaITAVSQEAAQVLesagegpldvrLRKLAEEKDELLSQIRKLKLQ 562
Cdd:TIGR04523 269 LSEKQKELEQNNK---KIKELEKQLNQLKSE-----ISDLNNQKEQDW-----------NKELKSELKNQEKKLEEIQNQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 563 LEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQrdanRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEK 642
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQ----RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 672063398 643 IEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 689
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
379-684 |
9.63e-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: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 379 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKT 458
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 459 IGALEKQkehIACLRNERDVLREELADLQQTVKTAEKHGLVIIPESTPNGDVNHEpvvgaitaVSQEAAQVLESAGEGPL 538
Cdd:pfam05483 452 IHDLEIQ---LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE--------LTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 539 DVRLRKLAEEKdeLLSQIRKLK---LQLEEERQKCSRNDGMSGDLAGL------QNGSDLQFIEMQRDANRQISEYkfKL 609
Cdd:pfam05483 521 DIINCKKQEER--MLKQIENLEekeMNLRDELESVREEFIQKGDEVKCkldkseENARSIEYEVLKKEKQMKILEN--KC 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 610 SKAEQDIATLEQSISRL--EGQVLRYKTAAENAE---------KIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKR 678
Cdd:pfam05483 597 NNLKKQIENKNKNIEELhqENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
....*.
gi 672063398 679 LEKMKA 684
Cdd:pfam05483 677 VEKAKA 682
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
327-683 |
1.30e-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: 45.49 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 327 HDVEgryMQGLKELKESL-SEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKH 405
Cdd:pfam15921 276 HEVE---ITGLTEKASSArSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 406 MCSvlqhkmDELKEGLRQRDELIEENQRLQqkvDTMTKEVFDLQEtllwKDKTIgALEKQKEHIACLRNER-----DVLR 480
Cdd:pfam15921 353 LAN------SELTEARTERDQFSQESGNLD---DQLQKLLADLHK----REKEL-SLEKEQNKRLWDRDTGnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 481 EELADLQQTVKTAEKHGLVIIPESTPNGDVNHEPVVG---AITAVSQEAAQvLESAGEgpldvRLRKLAEE----KDELL 553
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGkneSLEKVSSLTAQ-LESTKE-----MLRKVVEEltakKMTLE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 554 SQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ---------RDANRQISEYKFKLSKAEQDIATLEQSI- 623
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIe 572
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672063398 624 --SRLEGQVLRyKTAAENAEKIEDELKAEKRKLQ-RELRTAQD----KIEEMEMTNSHLakRLEKMK 683
Cdd:pfam15921 573 nmTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQEFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
337-681 |
1.93e-04 |
|
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: 44.50 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 337 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvlqhkmDE 416
Cdd:pfam07888 89 LRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK----------ER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 417 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkdktigalEKQKEHIACLRNERDVLREELADLQQTVKTAEKH 496
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF----------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 497 glviipestpngDVNHEPVVGAIT------AVSQEAAQVLESAGEGPLDVRLRKLAE------EKDELLSQIRKLKLQLE 564
Cdd:pfam07888 229 ------------EAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQAElhqarlQAAQLTLQLADASLALR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 565 EERQKcsrndgMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDiatleqsiSRLEGQVLRYKTAAE------ 638
Cdd:pfam07888 297 EGRAR------WAQERETLQ-----QSAEADKDRIEKLSAELQRLEERLQE--------ERMEREKLEVELGREkdcnrv 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 672063398 639 ---NAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 681
Cdd:pfam07888 358 qlsESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
388-683 |
2.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 388 EFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLqetllwkDKTIGALEKQKE 467
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-------EELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 468 HIACLRNERDVLREELADLQQTVKTAEKHGLVIipestpngdvnhEPVVGAITAVSQEAAqvlesagegpldvRLRKLAE 547
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEEL------------EEKVKELKELKEKAE-------------EYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 548 EKDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDIATLE------Q 621
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEE----------INGIE-----ERIKELEEKEERLEELKKKLKELEKRLEELEerhelyE 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672063398 622 SISRLEGQVLRYKT--AAENAEKIEDELK-AEKRK--LQRELRTAQDKIEEMEMTNSHLAKRLEKMK 683
Cdd:PRK03918 366 EAKAKKEELERLKKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
315-686 |
2.80e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 315 ELRDIYDLKDQIHDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 390
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 391 RENEEKSKELERQKHMCSVLQHKMDELKEGLRQ----RDELIEENQrlQQKVDTMTKEVFDLQETLLWKDKTIGALEKQK 466
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 467 EHI-ACLRNERDVLREElaDLQQTVKTAEKHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEG-PLDVRLRK 544
Cdd:PRK03918 483 RELeKVLKKESELIKLK--ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeELKKKLAE 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 545 LAEEKDELLSQIRKLKLQLEEERQKCSrnDGMSGDLAGLQNGSDlQFIEMqRDANRQISEYKFKLSKAEQDIATLEQSIS 624
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFESV--EELEERLKELEPFYN-EYLEL-KDAEKELEREEKELKKLEEELDKAFEELA 636
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672063398 625 RLEGQVLRYKTAAENAEKIEDE-----LKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANR 686
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
321-684 |
3.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 321 DLKDQIHDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 391
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 392 ENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQEtllwkdkTIGALEKQKEHIAC 471
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 472 LRNERDVLREELADLQQTVKTAEKhGLVIIPE----STPNGDVNHEPVVGAITAVSQEAAQVLEsagegpldvRLRKLAE 547
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEE-AKAKKEElerlKKRLTGLTPEKLEKELEELEKAKEEIEE---------EISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 548 EKDELLSQIRKLKL---QLEEERQKCSrndgmsgdlaglQNGSDLQfiemQRDANRQISEYKFKLSKAEQDIATLEQSIS 624
Cdd:PRK03918 413 RIGELKKEIKELKKaieELKKAKGKCP------------VCGRELT----EEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672063398 625 RL-------------EGQVLRYKTAAENAEKIEDELKA----EKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 684
Cdd:PRK03918 477 KLrkelrelekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
538-692 |
4.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 538 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQkcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFklskAEQDIA 617
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQE--------------------------RREALQRLAEYSW----DEIDVA 664
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672063398 618 TLEQSISRLEGQvlryKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 692
Cdd:COG4913 665 SAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-569 |
4.88e-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: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 310 DTSLSELRD-IYDLKDQIHDVEGRYMqglkELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 388
Cdd:COG1196 266 EAELEELRLeLEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 389 fyrENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEH 468
Cdd:COG1196 342 ---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 469 iacLRNERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAEE 548
Cdd:COG1196 419 ---LEEELEELEEALAELEEEEEEEEE----------------------ALEEAAEEEAELEEEEEA--LLELLAELLEE 471
|
250 260
....*....|....*....|.
gi 672063398 549 KDELLSQIRKLKLQLEEERQK 569
Cdd:COG1196 472 AALLEAALAELLEELAEAAAR 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
316-683 |
5.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 316 LRDIYDLKDQIHDVEGRyMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyRENEE 395
Cdd:PRK03918 206 LREINEISSELPELREE-LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 396 KSKELERQKHMCSVLQHKMDELKEGLRqrdELIEENQRLQQKVDTMTKEVFDLQEtllwKDKTIGALEKQKEHIACLRNE 475
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYEEYLDELR---EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 476 RDVLREELADLQQTVKTAEKHglviipeSTPNGDVNHEPVVGAITAVSQEAAQVLEsagegpldvRLRKLAEEKDELLSQ 555
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERL-------KKRLTGLTPEKLEKELEELEKAKEEIEE---------EISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 556 IRKLKL---QLEEERQKCSrndgmsgdlaglQNGSDLQfiemQRDANRQISEYKFKLSKAEQDIATLEQSISRL------ 626
Cdd:PRK03918 421 IKELKKaieELKKAKGKCP------------VCGRELT----EEHRKELLEEYTAELKRIEKELKEIEEKERKLrkelre 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 627 -------EGQVLRYKTAAE------------NAEKIE------DELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 681
Cdd:PRK03918 485 lekvlkkESELIKLKELAEqlkeleeklkkyNLEELEkkaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
..
gi 672063398 682 MK 683
Cdd:PRK03918 565 LD 566
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
335-569 |
6.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 335 QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL---- 410
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 411 --QHKMDELKEGLRQRD--ELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEHIACLRNERDVLREELADL 486
Cdd:COG4942 114 yrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 487 QQTVKTaekhglviipestpngdvnhepvvgAITAVSQEAAQvlesagegpLDVRLRKLAEEKDELLSQIRKLKLQLEEE 566
Cdd:COG4942 194 KAERQK-------------------------LLARLEKELAE---------LAAELAELQQEAEELEALIARLEAEAAAA 239
|
...
gi 672063398 567 RQK 569
Cdd:COG4942 240 AER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-537 |
6.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 318 DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 394
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 395 EKSKE----------------LERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETllwKDKT 458
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672063398 459 IGALEKQKEHIACLRNERDVLREELADLQQTVKTAEKHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGP 537
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
472-668 |
6.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 472 LRNERDVLREELADLQQTVKTAE--------KHGLVIIPESTpngdvnhEPVVGAITAVSQE--AAQVLESAGEGPLDVR 541
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEaaleefrqKNGLVDLSEEA-------KLLLQQLSELESQlaEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 542 LRKLAEEKD------------ELLSQIRKLKLQLEEERQKCSRNDgmsgdlaglqngSDLQFIEMQRDANRQI--SEYKF 607
Cdd:COG3206 246 RAQLGSGPDalpellqspviqQLRAQLAELEAELAELSARYTPNH------------PDVIALRAQIAALRAQlqQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672063398 608 KLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaekRKLQRELRTAQDKIEEM 668
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARELYESL 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
317-539 |
7.93e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 317 RDIYDLKDQIHDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 393
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 394 EEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE-NQRL------QQKVDTMTKEVFDLQETLLWKDKTIGA-LEKQ 465
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADlNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAAdLSKY 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 466 KEHIACLRNERDVLREELADLQQTVKTAEKHGLVIIPESTPNGDV------NHEPVVGAIT---AVSQEAAQVLESAGEG 536
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVeevlkaSIQGVHGTVAqlgSVGERYATAIEVAAGN 547
|
...
gi 672063398 537 PLD 539
Cdd:TIGR02169 548 RLN 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
546-692 |
9.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 546 AEEKDELLSQIRKLKLQLEEERQKCSRNDGmsgdlagLQNGSDLQFIEMQRDANRQiseykfKLSKAEQDIATLEQSISR 625
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA------ELEELRAELARLEAELER 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672063398 626 LEGQvlryktaaenaekiEDELKAEKRKLQRELRTAQ-DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 692
Cdd:COG4913 314 LEAR--------------LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
313-692 |
9.45e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 313 LSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLkdvieeqeeqMAEFYR 391
Cdd:pfam15921 319 LSDLEStVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL----------LADLHK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 392 ENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEV-FDLQETLLWKDKTIGALEKQKEHIA 470
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESLEKVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 471 CLRNERDVLREELADLQQTVKTAEkhglviipestpngdvNHEPVVGAITAVSQEAAQVLESAG------EGPLDVRLRK 544
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLE----------------SSERTVSDLTASLQEKERAIEATNaeitklRSRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 545 LAEEKDE------LLSQIRKLKLQLEEE-------RQKCSRND---GMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFK 608
Cdd:pfam15921 533 LQHLKNEgdhlrnVQTECEALKLQMAEKdkvieilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 609 LSKAEQDIATLEQSISRLEGQVLR---------------------------------------YKTAAENAEKIEDELKA 649
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKlvnagserlravkdikqerdqllnevktsrnelnslsedYEVLKRNFRNKSEEMET 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 672063398 650 EKRKLQRELRTAQDKIEE-------MEMTNSHLAKRLEKMKANRTALLAQ 692
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQtrntlksMEGSDGHAMKVAMGMQKQITAKRGQ 742
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
312-491 |
1.03e-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: 42.31 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 312 SLSELRD-IYDLKDQIHDVEGRYMQGLKELKESLSEVE------EKYKKamvSNAQLDNEKNNLIYQVDTLKDVIEEQEE 384
Cdd:TIGR04523 336 IISQLNEqISQLKKELTNSESENSEKQRELEEKQNEIEklkkenQSYKQ---EIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 385 QMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE----NQRLQQKVDTMTKEVFDLQETLLWKDKTig 460
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntRESLETQLKVLSRSINKIKQNLEQKQKE-- 490
|
170 180 190
....*....|....*....|....*....|.
gi 672063398 461 aLEKQKEHIACLRNERDVLREELADLQQTVK 491
Cdd:TIGR04523 491 -LKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
318-659 |
1.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 318 DIYDLKDQIHDVEGRymqgLKELKESLSEVEE--KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEE 395
Cdd:PRK03918 260 KIRELEERIEELKKE----IEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 396 KSKELERQKHMCSVLQHKMDELKEglrqRDELIEENQRLQQKVDTMTKEVFDLQETLLwkDKTIGALEKQKEHIaclRNE 475
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKL--EKELEELEKAKEEI---EEE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 476 RDVLREELADLQQTVKTAEKhglVIIPESTPNGDVnhePVVGAITAVSQEAAQVLESAGE-GPLDVRLRKLAEEKDELLS 554
Cdd:PRK03918 407 ISKITARIGELKKEIKELKK---AIEELKKAKGKC---PVCGRELTEEHRKELLEEYTAElKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 555 QIRKLKLQLEEERqKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGqvlrYK 634
Cdd:PRK03918 481 ELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LK 555
|
330 340
....*....|....*....|....*
gi 672063398 635 TAAENAEKIEDELKAEKRKLQRELR 659
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELE 580
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-689 |
1.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 340 LKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM---------AEFYRENEEKSKELERQKHmcSVL 410
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREER--DEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 411 QHKMDELKEGLRQRDELIEENQRLQQ--KVDTMTKEVFDlqetllwkDKTIGALEKQKEHIACLRNERDVLREELADLQQ 488
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEagKCPECGQPVEG--------SPHVETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 489 TVKTAEKhgLVIIPESTPNGDVNHEPVVGAIT-------------AVSQEAAQVLESAGEGPLDvRLRKLAEEKDELLSQ 555
Cdd:PRK02224 497 RLERAED--LVEAEDRIERLEERREDLEELIAerretieekreraEELRERAAELEAEAEEKRE-AAAEAEEEAEEAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 556 IRKLKLQLEEERQKCSRNDGMSGDLAGLQN-GSDLQFIEMQRDA-NRQISEYKFKLSKAEQDIATLEQSI--SRLEGQVL 631
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLAAIADaEDEIERLREKREAlAELNDERRERLAEKRERKRELEAEFdeARIEEARE 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672063398 632 RYKTAAENAEKIE---DELKAEKRKLQRELRTAQDKIEEMEmtnsHLAKRLEKMKANRTAL 689
Cdd:PRK02224 654 DKERAEEYLEQVEeklDELREERDDLQAEIGAVENELEELE----ELRERREALENRVEAL 710
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
541-686 |
1.21e-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: 41.06 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 541 RLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 613
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672063398 614 QDIATLEQSISRLEGQVlryKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEmemtnsHLAKRLEKMKANR 686
Cdd:COG1579 124 EELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
596-684 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 596 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaekRKLQRELRTAQDKIEEMEMTNSHL 675
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491
|
....*....
gi 672063398 676 AKRLEKMKA 684
Cdd:COG2433 492 KRKLERLKE 500
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
361-657 |
1.48e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 361 LDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSkelerqkhmcsvlqhkmdelkeglrqrDELIEENQRLQQKVDT 440
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---------------------------DELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 441 MTKEVFDLQETllwkdktigaLEKQKEHIACLRNERDVLREELADLQQTVKTAEKHGlvIIPESTpngdvnhepvvgait 520
Cdd:PHA02562 239 LTDELLNLVMD----------IEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG--VCPTCT--------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 521 avsqeaaQVLESAGEgpldvRLRKLAEEKDELLSQIRKLKLQLEEERQKCSrndgmsgdlaglqngsdlQFIEMQR---D 597
Cdd:PHA02562 292 -------QQISEGPD-----RITKIKDKLKELQHSLEKLDTAIDELEEIMD------------------EFNEQSKkllE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 598 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRE 657
Cdd:PHA02562 342 LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
325-680 |
1.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 325 QIHDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 403
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 404 khmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQkehiacLRNERDVLREEL 483
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ------LQDTQELLQEET 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 484 -ADLQQTVKT----AEKHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGpldvrLRKLAEEKDELLSQIRK 558
Cdd:pfam01576 482 rQKLNLSTRLrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-----LEALEEGKKRLQRELEA 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 559 LKLQLEEERQKCSRNDGMSGDLAGlqngsDLQFIEMQRDANRQI-SEYKFKLSKAEQDIATlEQSISrlegqvLRYKTAA 637
Cdd:pfam01576 557 LTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQLvSNLEKKQKKFDQMLAE-EKAIS------ARYAEER 624
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 672063398 638 ENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLE 680
Cdd:pfam01576 625 DRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
313-540 |
2.18e-03 |
|
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: 40.99 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 313 LSELR-DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSN------------AQLDNEKNNLIYQVDTL---- 375
Cdd:pfam06160 181 LEKLEeETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalehlnvdkeiQQLEEQLEENLALLENLelde 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 376 -KDVIEEQEEQMAEFYR--ENEEKSKE--LERQKHMCSVLQHKMDELKEGL------------------------RQRDE 426
Cdd:pfam06160 261 aEEALEEIEERIDQLYDllEKEVDAKKyvEKNLPEIEDYLEHAEEQNKELKeelervqqsytlnenelervrgleKQLEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 427 LIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQ----KEHIACLRNERDVLREELADLQQTV----KTAEKHGL 498
Cdd:pfam06160 341 LEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEqeefKESLQSLRKDELEAREKLDEFKLELreikRLVEKSNL 420
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 672063398 499 VIIPEStpngdvnhepVVGAITAVSQEAAQVLESAGEGPLDV 540
Cdd:pfam06160 421 PGLPES----------YLDYFFDVSDEIEDLADELNEVPLNM 452
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
338-688 |
2.29e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 338 KELKESLSEVEEKYKKAMVSNAQLDNEKNNLIY-QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 416
Cdd:pfam02463 215 LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 417 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEHIACLRNERDVLREELADLQQTVKTAEKh 496
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 497 glviipestpngdvnhepvvgaitavSQEAAQVLESAGEGPLDVRLRKLAEEKDELLSQIrklKLQLEEERQKcsrndgm 576
Cdd:pfam02463 374 --------------------------ELLAKKKLESERLSSAAKLKEEELELKSEEEKEA---QLLLELARQL------- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 577 sGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQR 656
Cdd:pfam02463 418 -EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
330 340 350
....*....|....*....|....*....|..
gi 672063398 657 ELRTAQDKIEEMEMTNSHLAKRLEKMKANRTA 688
Cdd:pfam02463 497 ERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-619 |
2.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 410 LQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQ--ETLLWKDKTIGALEKQkehIACLRNERDVLRE---ELA 484
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAERE---IAELEAELERLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 485 DLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQvlesagegpLDVRLRKLAEEKDELLSQIRKLKLQLE 564
Cdd:COG4913 689 ALEEQLEELEA----------------------ELEELEEELDE---------LKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 672063398 565 EERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATL 619
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-569 |
2.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 332 RYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNL--IYQVDTLKDVIEEQEEQMAEFYREN-EEKSKELERQKHMCS 408
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 409 VLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWK--------DKTIGALEK---------------- 464
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPfyneylelkdaekele 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 465 -QKEHIACLRNERDVLREELADLQQTVKTAEKHglviIPESTPNGDV-NHEPVVGAITAVSQEAAQVLEsagegpldvRL 542
Cdd:PRK03918 616 rEEKELKKLEEELDKAFEELAETEKRLEELRKE----LEELEKKYSEeEYEELREEYLELSRELAGLRA---------EL 682
|
250 260
....*....|....*....|....*..
gi 672063398 543 RKLAEEKDELLSQIRKLKLQLEEERQK 569
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
519-693 |
3.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 519 ITAVSQEAAQVLESAGEgpLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCS-------RNDGMSGDLAGLQNGSDLQ- 590
Cdd:COG3883 39 LDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 591 FIE-------MQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQD 663
Cdd:COG3883 117 FLDrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|
gi 672063398 664 KIEEMEMTNSHLAKRLEKMKANRTALLAQQ 693
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
598-693 |
3.49e-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: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 598 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAK 677
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 672063398 678 RLEKMKAnrtaLLAQQ 693
Cdd:COG4942 98 ELEAQKE----ELAEL 109
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
337-689 |
3.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 337 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 416
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 417 LKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIG----ALEKQKEHIACLRNERDVLREELADLQQTVKT 492
Cdd:PRK02224 361 LRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDELREREAELEATLRT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 493 AEKhglviipestpngdvnhepvvgaitavSQEAAQVLESAGEGP---LDVRLRKLAEEKDELLSQIRKLKLQLEEERQK 569
Cdd:PRK02224 438 ARE---------------------------RVEEAEALLEAGKCPecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 570 CSRNDgmsgdlaglqngSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKA 649
Cdd:PRK02224 491 VEEVE------------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 672063398 650 EKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 689
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL 598
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
598-667 |
4.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 598 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEE 667
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
334-689 |
4.91e-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: 40.42 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 334 MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN--NLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQ 411
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERELSKAEKNSLteTLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 412 HKMDE----LKEGLRQRDELIEE------NQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEHIaclRNERDVLRE 481
Cdd:TIGR00606 543 DKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI---NNELESKEE 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 482 ELADLQQTV-----KTAEKHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVL-ESAGEGPLDVRLRKLAEEKDELLSQ 555
Cdd:TIGR00606 620 QLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQSCCPVCQRVFQTEAELQEFISD 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 556 IR--------KLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAEQ------- 614
Cdd:TIGR00606 700 LQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNRDIQRLKNDIEEQETllgtimp 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 615 ----------DIATLEQSISRLEGQVLRYKTAAENAEKIE-----DELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRL 679
Cdd:TIGR00606 780 eeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
410
....*....|
gi 672063398 680 EKMKANRTAL 689
Cdd:TIGR00606 860 QHLKSKTNEL 869
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
374-496 |
6.14e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 374 TLKDVIEEQEEQMAEFYRENEEKSKELERqkhmcsvlqhkmdelkeglRQRDELIEENQRLQQKVDTMTKEVFDLQETLL 453
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEE-------------------RELTEEEEEIRRLEEQVERLEAEVEELEAELE 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 672063398 454 WKDKTIGALEK-----QKEHIACLRNERDV--LREELADLQQTVKTAEKH 496
Cdd:COG2433 438 EKDERIERLERelseaRSEERREIRKDREIsrLDREIERLERELEEERER 487
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
541-693 |
6.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 541 RLRKLAEEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAglQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDIATL 619
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELE--QARSELEQLEEElEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672063398 620 EQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 693
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-658 |
6.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 337 LKELKESLSEVEekykkamvsnAQLDNEKnnliyqvDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 416
Cdd:COG1196 255 LEELEAELAELE----------AELEELR-------LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 417 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQEtllwkdktigALEKQKEHIACLRNERDVLREELADLQQTVKTAEKH 496
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEE----------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 497 glviipestpngdvnhepvvgaitAVSQEAAQVLESAGEGPLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRndgm 576
Cdd:COG1196 388 ------------------------LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 577 SGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQR 656
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
..
gi 672063398 657 EL 658
Cdd:COG1196 520 RG 521
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
337-689 |
7.17e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 337 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH---K 413
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 414 MDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDlqetllwKDKTIGALEKQKEHIACLRNERDVLREELADLQ--QTVK 491
Cdd:pfam15921 550 CEALKLQMAEKDKVIE---ILRQQIENMTQLVGQ-------HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKdkKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 492 TAEKHGLVIIPESTPNGDVNH-EPVVGAITAVSQEAAQVLESAGEG---------PLDVRLRKLAEEKDELLSQIRKLKL 561
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAgSERLRAVKDIKQERDQLLNEVKTSrnelnslseDYEVLKRNFRNKSEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 562 QLEEERQKC--SRNDGMSgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISrlegqvlryktaaeN 639
Cdd:pfam15921 700 QLKSAQSELeqTRNTLKS------MEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------------N 759
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 672063398 640 AEKIEDELKAEKRKLQRELRT-AQDKIE---EMEMTNSHLAKRLEKMKANRTAL 689
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQERRLKEKVANMEVAL 813
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
313-445 |
7.55e-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: 38.75 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 313 LSELRDIYD-LKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 386
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 387 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQR-DELIEENQRLQQKVDTMTKEV 445
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
314-451 |
9.53e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672063398 314 SELRDIYDLKDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEF---- 389
Cdd:TIGR04523 381 SYKQEIKNLESQINDLE----SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKelii 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672063398 390 -----YREN-EEKSKELERQ-KHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQET 451
Cdd:TIGR04523 457 knldnTRESlETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| |
