|
Name |
Accession |
Description |
Interval |
E-value |
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
74-799 |
0e+00 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 1051.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 74 GQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIR 153
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 154 MKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE 233
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 234 ALETLKNEREQKNNLRKELSQYINLSD----SHISISVDGLKFAED---GSEPNND-DKMNGHIHG--PLGKLNGDYRTP 303
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDfdyvSHLSISLDGLKFSEDegaGTEPNNDgEAMDGGENGggGLKNSGLDNRTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 304 TTRKGESLHP----VSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMR 379
Cdd:pfam09730 241 TPRKSEVFPPapslVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 380 GLQNSKEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKI 459
Cdd:pfam09730 321 GLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 460 QMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYR 539
Cdd:pfam09730 401 QDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 540 QSRVTRSGslKGPDDPRGLLSPRLSRRGVsspvesrTSSEPVSKENteTSKEPSPTKTPTISPvitappsspvldTSDIR 619
Cdd:pfam09730 481 EGAGARAR--KSHQEPRGLRSPRLLTRGL-------FMGEVGTADT--TSNSPSPCSSCPGSP------------TSDFR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 620 KEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANK 699
Cdd:pfam09730 538 REPMNIYNLVAIIRDQIKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANK 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 700 QTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTL 779
Cdd:pfam09730 618 QTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSL 697
|
730 740
....*....|....*....|
gi 1907170352 780 LRMAIQQKLALTQRLEDLEF 799
Cdd:pfam09730 698 LRMAIQQKLALTQRLEDLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-254 |
3.17e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 3 AEEALKTVDQYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLREAFGQsfsihr 81
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELE-AELEELEAELAELEAELeELRLELEELELELEEAQAEEYELLAELAR------ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 82 kvAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 377 --AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|...
gi 1907170352 242 REQKNNLRKELSQ 254
Cdd:COG1196 455 EEEEEALLELLAE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-254 |
8.97e-12 |
|
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: 69.32 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 12 QYKTEIERLTKELTETThEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDgETR 90
Cdd:TIGR02168 674 ERRREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 91 EETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQ 170
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 171 DYTELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:TIGR02168 832 RIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
....
gi 1907170352 251 ELSQ 254
Cdd:TIGR02168 909 KRSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-814 |
1.28e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 48 LKQQYDELEA------EYDGLKQELEQLReafgQSFSIHRKVAEDGEtREETLLQESASKEayylnKILEMQNELKQSRA 121
Cdd:TIGR02168 198 LERQLKSLERqaekaeRYKELKAELRELE----LALLVLRLEELREE-LEELQEELKEAEE-----ELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 122 VVTNVQAENERLSAVVQEL-KENNEMVELQRiRMKDEIREYKFREARLLQDYTELEEEnitLQKLVSTLKQNQVEYEGLK 200
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELqKELYALANEIS-RLEQQKQILRERLANLERQLEELEAQ---LEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 201 HEIKRFEEETVLLNSQLEDAIRLKEiaehQLEEALETLKNEREQKNNLRKELSQYINLSDSHISISVDGLKFAEDgsepn 280
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED----- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 281 nddkmnghihgplgklngdyrtpttRKGESLHPVSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGA 360
Cdd:TIGR02168 415 -------------------------RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 361 LTEQHERVHRLTEHVNAMRGLQNSkeikaeldCEKGRNSAEEAHDYEVDIngleileCKYRVAVTEVIDLKAEIKALKEK 440
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDS--------LERLQENLEGFSEGVKAL-------LKNQSGLSGILGVLSELISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 441 YNKSVENYTEEKtkyeskIQMY-----DEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNT------AQDELV 509
Cdd:TIGR02168 535 YEAAIEAALGGR------LQAVvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNiegflgVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 510 TFSEEL-----AQLYHHVCLCNNETPNRVMLDYYRQSR--------VTRSGSLKGPDDPR--GLLSPRLSRRGVSSPVES 574
Cdd:TIGR02168 609 KFDPKLrkalsYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlVRPGGVITGGSAKTnsSILERRREIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 575 RTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSP---VLDTSDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSR 651
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 652 QRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNkYENEKAMVTETMTKLRNEL 731
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 732 KALKEDAATFSSLRAmfatrcdEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 848 EELSEDIESLAAEIE-------ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
...
gi 1907170352 812 GKS 814
Cdd:TIGR02168 921 REK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-255 |
1.31e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 3 AEEALKTVDQYKTEIERLTKELTETTH--EKIQAAEYGLvvLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSfsih 80
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELelEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEELEEELAEL---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 81 RKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQEL--KENNEMVELQRI-RMKDE 157
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleALRAAAELAAQLeELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 158 IREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALET 237
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|....*...
gi 1907170352 238 LKNEREQKNNLRKELSQY 255
Cdd:COG1196 489 AAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-255 |
1.73e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 14 KTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQ------QYDELEAEYDGLKQELEQLREAFGQSF----SIHRKV 83
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaierQLASLEEELEKLTEEISELEKRLEEIEqlleELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 84 AEDGETREETLLQESASKEAYYLN---KILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 161 YKFREARLLQdytELEEENITLQKLVSTLKQNQVEYEGLKHE----------------------------IKRFEEETVL 212
Cdd:TIGR02169 362 LKEELEDLRA---ELEEVDKEFAETRDELKDYREKLEKLKREinelkreldrlqeelqrlseeladlnaaIAGIEAKINE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907170352 213 LNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQY 255
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-254 |
2.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 41 VLEEkltLKQQYDELEAE------YDGLKQELEQLReafGQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQN 114
Cdd:COG1196 194 ILGE---LERQLEPLERQaekaerYRELKEELKELE---AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 115 ELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQK----LVSTLK 190
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907170352 191 QNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-518 |
5.67e-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: 56.99 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 1 MAAEEALKTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLR---EAFGQS 76
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEELKeelESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 77 FSIHRKVAEDGETREETL---LQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIR 153
Cdd:TIGR02168 360 LEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 154 MkdeireykfrearllqdytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLE- 232
Cdd:TIGR02168 440 A-------------------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEn 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 233 -----EALETLKNEREQKNNLRKELSQYIN------------LSDSHISISVDGLKFAEDGSE----------------- 278
Cdd:TIGR02168 501 legfsEGVKALLKNQSGLSGILGVLSELISvdegyeaaieaaLGGRLQAVVVENLNAAKKAIAflkqnelgrvtflplds 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 279 ------PNNDDKMNGHIHGPLG-------------------------------------KLNGDYRTpTTRKGESLHP-- 313
Cdd:TIGR02168 581 ikgteiQGNDREILKNIEGFLGvakdlvkfdpklrkalsyllggvlvvddldnalelakKLRPGYRI-VTLDGDLVRPgg 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 314 VSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKEIKAELDC 393
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 394 EKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTS 473
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1907170352 474 KESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-456 |
6.61e-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: 56.99 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 107 NKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLV 186
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 187 STLKQNQVEYEGLKHEIKRFEEEtvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQyinlsdshISIS 266
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--------LNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 267 VDGLKFAEDGSEPNNDD--KMNGHIHGPLGKLNGDyrtpttrkGESL-HPVSDLFSELN--ISEIQKLKQQLIQVEREKA 341
Cdd:TIGR02168 819 AANLRERLESLERRIAAteRRLEDLEEQIEELSED--------IESLaAEIEELEELIEelESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 342 ILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNskEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYR 421
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
330 340 350
....*....|....*....|....*....|....*
gi 1907170352 422 VAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYE 456
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-254 |
7.32e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 2 AAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREafgqsfsihr 81
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 82 kvaedgetREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREY 161
Cdd:COG1196 338 --------ELEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 162 KFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250
....*....|...
gi 1907170352 242 REQKNNLRKELSQ 254
Cdd:COG1196 486 LAEAAARLLLLLE 498
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-803 |
2.64e-07 |
|
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: 54.98 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSiHRKV 83
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-LNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 84 AEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREykf 163
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 164 rearllqdytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNERE 243
Cdd:pfam02463 315 ----------KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 244 QKNNLRKELSQYINLSDSHISISVDGLKFAEDgsepNNDDKMNGHIHGPLGKLngdyrtpTTRKGESLHPVSDLFSELNI 323
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQ----LEDLLKEEKKEELEILE-------EEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 324 SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKG-ALTEQHERVHRLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEE 402
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 403 AHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKmah 482
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK--- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 483 meKELQKMTGIANENHNTLNTAQDELVTFSeelaqlyhhvclcnnETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSP- 561
Cdd:pfam02463 611 --ATLEADEDDKRAKVVEGILKDTELTKLK---------------ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTk 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 562 -RLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRD------ 634
Cdd:pfam02463 674 eLLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEeeeeee 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 635 --QIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNK 712
Cdd:pfam02463 754 ksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 713 YENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRqlaaaeDEKKTLNTLLRMAIQQKLALTQ 792
Cdd:pfam02463 834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK------DELESKEEKEKEEKKELEEESQ 907
|
810
....*....|.
gi 1907170352 793 RLEDLEFDHEQ 803
Cdd:pfam02463 908 KLNLLEEKENE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-811 |
2.73e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETtHEKIQAAEYGLVVLEEKLTLKQQ-YDELEAEYDGLKQELEQLREAfgqsfsihRK 82
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQEL-EEKLEELRLEVSELEEEIEELQKeLYALANEISRLEQQKQILRER--------LA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 83 VAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYK 162
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 163 FREARLLQDYTELEEENITLQKLVSTLKQNQ--VEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 241 EREQKNNLRKELSQYINLSDSHISISVDGLKFAEDGSEP-NNDDKMNGhIHGPLGKL----NGDYRTPTTRKGESL-HPV 314
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALlKNQSGLSG-ILGVLSELisvdEGYEAAIEAALGGRLqAVV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 315 SD--------------------LFSELNI---SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRL 371
Cdd:TIGR02168 552 VEnlnaakkaiaflkqnelgrvTFLPLDSikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 372 TEhVNAMRGLQNSKEIKAELDCEK--------GRNSAEEAHDYEVDInglEILECKYRVAVTE--VIDLKAEIKALKEK- 440
Cdd:TIGR02168 632 DN-ALELAKKLRPGYRIVTLDGDLvrpggvitGGSAKTNSSILERRR---EIEELEEKIEELEekIAELEKALAELRKEl 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 441 --YNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02168 708 eeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 519 yhhvclcnnetpNRVMLDYYRQSRVTRSGSLKgpddprglLSPRLSR-RGVSSPVESRTSSEPVSKENTETSKEPSPTKT 597
Cdd:TIGR02168 788 ------------EAQIEQLKEELKALREALDE--------LRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 598 PTISPVITAppSSPVLDTSDIRKEPmniynlnaiIRDQIKHLQKAVDrslQLSRQRAAARELAPMIDKDKEALMEEILKL 677
Cdd:TIGR02168 848 EELSEDIES--LAAEIEELEELIEE---------LESELEALLNERA---SLEEALALLRSELEELSEELRELESKRSEL 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 678 KSLLSTKREQIATLRAVLkankQTAEVALANLKnkyenekamvtetmTKLRNELKALKEDAATFSSLRamfatrcdeyVT 757
Cdd:TIGR02168 914 RRELEELREKLAQLELRL----EGLEVRIDNLQ--------------ERLSEEYSLTLEEAEALENKI----------ED 965
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1907170352 758 QLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-248 |
9.64e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 3 AEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQY--------------DELEAEYDGLKQELEQ 68
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeelkalrealDELRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 69 LREAFGQsfsiHRKVAEDGETREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVE 148
Cdd:TIGR02168 822 LRERLES----LERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 149 LQRIRMKDEIREYKFREARLLQDYTELEEEnitlqklvstLKQNQVEYEGLKHEIKRFEEE-TVLLNSQLEDAIRLKEIA 227
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREK----------LAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKI 963
|
250 260
....*....|....*....|.
gi 1907170352 228 EHQLEEALETLKNEREQKNNL 248
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-241 |
1.10e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 2 AAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHR 81
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 82 KVAEDGETREETLLQESASKEAyYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 447 --AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-------AAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-220 |
4.49e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETThEKIQA--AEYGLVVLEEKLT--------LKQQYDELEAEYDGLKQELEQLREAF 73
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAE-AALEEfrQKNGLVDLSEEAKlllqqlseLESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 74 GQSFSIHRKVAEDGETREetllqesaskeayYLNKILEMQNELKQSRAVVTN----VQAENERLSAVVQELKEnnemvEL 149
Cdd:COG3206 250 GSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSARYTPnhpdVIALRAQIAALRAQLQQ-----EA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907170352 150 QRIR--MKDEIREYKFREARLLQDYTELEEEnitlqklVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3206 312 QRILasLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-514 |
5.77e-06 |
|
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: 50.50 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 18 ERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQL----REAFGQSFSIHRKVA----EDGET 89
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfEEASGKKIYEHDSMStmhfRSLGS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 90 REETLLQESASKEAYYLNKILEMQNELKQSRAVVTN-----VQAENERLSAVVQEL---------KENNEMVELQRIRMK 155
Cdd:pfam15921 221 AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHeveitglteKASSARSQANSIQSQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 156 DEIREYKFRE--ARLLQDYTELEEeniTLQKLVSTLKQNQVEYEglkHEIKRFEEETVLLNSQLEDAIRLKEI------- 226
Cdd:pfam15921 301 LEIIQEQARNqnSMYMRQLSDLES---TVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTEARTERDQfsqesgn 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 227 AEHQLEEALETLkNEREQKNNLRKELSQYINLSDSHISISVDGLKfaedgSEPNNDDKMNGHIHGPLGKLNGDYRTPTTR 306
Cdd:pfam15921 375 LDDQLQKLLADL-HKREKELSLEKEQNKRLWDRDTGNSITIDHLR-----RELDDRNMEVQRLEALLKAMKSECQGQMER 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 307 -------KGESLHPVSDLFSELN---------ISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVH- 369
Cdd:pfam15921 449 qmaaiqgKNESLEKVSSLTAQLEstkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDl 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 370 RLTEHVNAMRGLQNSKEIKAELDCEK----GRNSAEEAHDYEVDiNGLEILECKYRVAVTEVIDlKAEIKALKEKYNKSV 445
Cdd:pfam15921 529 KLQELQHLKNEGDHLRNVQTECEALKlqmaEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVE-KAQLEKEINDRRLEL 606
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907170352 446 ENYTEEKTKYESKIQMYDEQVTNLE----KTSKESGEKMAHMEKELQKMTGIANEnhntLNTAQDELVTFSEE 514
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNE----VKTSRNELNSLSED 675
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-191 |
7.47e-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: 49.38 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQEL-EQLREAFGQSFSIHR 81
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALA-RRIRALEQELAALEAELaELEKEIAELRAELEAQKEELaELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 82 KVAEDGETREEtllqesASKEAYYLNKILE-MQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:COG4942 123 ALLLSPEDFLD------AVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|.
gi 1907170352 161 YKFREARLLQDYTELEEENITLQKLVSTLKQ 191
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-528 |
1.19e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 314 VSDLFSELNiSEIQKLKQQLIQVEREKAIllaNLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQnsKEIKAELDC 393
Cdd:TIGR02168 191 LEDILNELE-RQLKSLERQAEKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEEL--EELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 394 EKGRNSAEEAHDYEVDiNGLEILECKYRVAVTEVIDLKAEIKALKEK---YNKSVENYTEEKTKYESKIQMYDEQVTNLE 470
Cdd:TIGR02168 265 LEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907170352 471 KTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNE 528
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
4-254 |
1.78e-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: 48.56 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTL---KQQYDELEAEYDGLKQELEQLREAfgqsfsiH 80
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIAEELKGKEQELIFLLQA-------R 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 81 RKVAEDGETReetlLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:pfam05483 449 EKEIHDLEIQ----LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 161 YKFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
250
....*....|....
gi 1907170352 241 EREQKNNLRKELSQ 254
Cdd:pfam05483 602 QIENKNKNIEELHQ 615
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-518 |
2.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 2 AAEEALKTVDQYKTEIERLTKEL--TETTHEKIQAAEYGLV-VLEEKLTLKQQYDELEAEYDGLKQELEQLREafgqsfs 78
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 79 iHRKVAEDGETREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELqRIRMKDEI 158
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE----KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 159 REYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETL 238
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 239 KNEREQKNNLRKELSQYINlsdshisisvdglkfaEDGSEPNNDDKMNGHIHGPLGKLNGDYRT-PTTRKGESLHPVSDL 317
Cdd:PRK03918 390 EKELEELEKAKEEIEEEIS----------------KITARIGELKKEIKELKKAIEELKKAKGKcPVCGRELTEEHRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 318 FSE--LNISEIQKLKQQLIQVEREkaiLLANLQESQTQLehtkgaltEQHERVHRLTEHVNAMRGLQNSKEikaELDCEK 395
Cdd:PRK03918 454 LEEytAELKRIEKELKEIEEKERK---LRKELRELEKVL--------KKESELIKLKELAEQLKELEEKLK---KYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 396 GRNSAEEahdyevdingleileckYRVAVTEVIDLKAEIKALKEKYNKsVENYTEEKTKYESKIQMYDEQVTNLEKTSKE 475
Cdd:PRK03918 520 LEKKAEE-----------------YEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907170352 476 SG-EKMAHMEKELQKMTGIANEnHNTLNTAQDELVTFSEELAQL 518
Cdd:PRK03918 582 LGfESVEELEERLKELEPFYNE-YLELKDAEKELEREEKELKKL 624
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-151 |
3.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETTHE--KIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHR 81
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907170352 82 KVAEDGETREETLLQESASKEA---YYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQR 151
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
15-490 |
3.43e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 15 TEIERLTKELTETTHEKIQAAEYglvvLEEKLTLK-QQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREET 93
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQ----LEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 94 LLQESASKEAYylnkiLEMQNELKQSRA-VVTNVQAEN---ERLSAVVQELKENNEMvELQRIRMKDEIREYKFREARLL 169
Cdd:pfam05483 326 ICQLTEEKEAQ-----MEELNKAKAAHSfVVTEFEATTcslEELLRTEQQRLEKNED-QLKIITMELQKKSSELEEMTKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 170 QDYTELE-EENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALE-TLKNEREQKNN 247
Cdd:pfam05483 400 KNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 248 LRKELSQYINLSDSHISISVDGLKFAEDGSE---------------PNNDDKMNGHIHGPLGKLNGDYRTPTTRKGESLH 312
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDmtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 313 PVSDLFSELNISE--IQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKEIKA- 389
Cdd:pfam05483 560 KGDEVKCKLDKSEenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVn 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 390 --ELDCEKGRNSAEEAHD-YEVDINGLEILE-------CKYRVAVTEVIDLKAEI-KALKEKYNKSVENYTEEKTKYESK 458
Cdd:pfam05483 640 klELELASAKQKFEEIIDnYQKEIEDKKISEeklleevEKAKAIADEAVKLQKEIdKRCQHKIAEMVALMEKHKHQYDKI 719
|
490 500 510
....*....|....*....|....*....|..
gi 1907170352 459 IQMYDEQVTNLEKTSKESGEKMAHMEKELQKM 490
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-254 |
3.72e-05 |
|
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: 47.76 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 43 EEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFS----IHRKVAEDGETREETLLQESASKEayylnKILEMQNELKQ 118
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdASRKIGEIEKEIEQLEQEEEKLKE-----RLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 119 SRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFR----------------EARLLQDYTELEEENITL 182
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelskleeevsriEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907170352 183 QKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLED---AIRLKEIAEHQLEEALETLKNEREqknNLRKELSQ 254
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKKERD---ELEAQLRE 900
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3-193 |
4.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 3 AEEALKTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLREAFGQSFsihR 81
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-DALQAELEELNEEYNELQAELeALQAEIDKLQAEIAEAEAEIEERREELGERA---R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 82 KVAEDGETR---EETLLQESAS---KEAYYLNKILEMQN----ELKQSRAVVTNVQAENE----RLSAVVQELKENNEMV 147
Cdd:COG3883 94 ALYRSGGSVsylDVLLGSESFSdflDRLSALSKIADADAdlleELKADKAELEAKKAELEaklaELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907170352 148 ELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQ 193
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-266 |
4.60e-05 |
|
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: 47.37 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 2 AAEEALKTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLREAFGQSFsih 80
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIEnVKSELKELEARIEELEEDLHKLEEALNDLE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 81 rkvAEDGETREETLLQESASKEAYyLNKILEMQNELKQSravVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:TIGR02169 786 ---ARLSHSRIPEIQAELSKLEEE-VSRIEARLREIEQK---LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 161 YKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKHEIKRFEEETvllnSQLEDAIRLKEIAEHQLEEALETLKn 240
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLES----------RLGDLKKERDELEAQL----RELERKIEELEAQIEKKRKRLSELK- 923
|
250 260
....*....|....*....|....*.
gi 1907170352 241 erEQKNNLRKELSQYINLSDSHISIS 266
Cdd:TIGR02169 924 --AKLEALEEELSEIEDPKGEDEEIP 947
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
88-254 |
1.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 88 ETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLsavvQELKENNEMVELQRIRMKDEIREYKFREA- 166
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 167 -RLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIR-LKEIAEHQLEEALETLKNEREQ 244
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQR 207
|
170
....*....|
gi 1907170352 245 KNNLRKELSQ 254
Cdd:COG4717 208 LAELEEELEE 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-252 |
1.98e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 8 KTVDQYKTEIERLTKELTETTHEKIQAAEyglvVLEEKLTLKQQYDELEAEYDGLKQELEQLREafgqsfsihrKVAEDG 87
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERREELETLEAEIEDLRE----------TIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 88 ETREETLLQESASKEAyylnkILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREAR 167
Cdd:PRK02224 272 REREELAEEVRDLRER-----LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 168 LLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNN 247
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
....*
gi 1907170352 248 LRKEL 252
Cdd:PRK02224 424 LRERE 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10-238 |
2.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 10 VDQYKTEIERLTKELtetthekiQAAEYGLVVLEEkltLKQQYDELEAEYDGLKQELEQLREAFGQsFSIHRKVAEDGET 89
Cdd:COG4913 663 VASAEREIAELEAEL--------ERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELD 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 90 REETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQaenERLSAVVQELKE--NNEMVELQRIrMKDEIREYKFREAR 167
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR---ENLEERIDALRArlNRAEEELERA-MRAFNREWPAETAD 806
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907170352 168 L---LQDYTELEEEnitLQKLVStlkQNQVEYEG-LKHEIKRFEEETVL-LNSQLEDAIRlkEIAE--HQLEEALETL 238
Cdd:COG4913 807 LdadLESLPEYLAL---LDRLEE---DGLPEYEErFKELLNENSIEFVAdLLSKLRRAIR--EIKEriDPLNDSLKRI 876
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
48-375 |
3.02e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.33 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 48 LKQQYDELE---AEYDGLKQELEQlreAFGQSfsiHRKVAEDGETREETLLQESASKEAYYlNKILEMQNELKQSRAVVT 124
Cdd:pfam03528 6 LQQRVAELEkenAEFYRLKQQLEA---EFNQK---RAKFKELYLAKEEDLKRQNAVLQEAQ-VELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 125 NVQA-----ENERLSAVVQELKENNEMVELQRIRMKDEIREY----------------KFRE------ARLLQDYTELEE 177
Cdd:pfam03528 79 NIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKETVREYevqfhrrleqeraqwnQYREsaereiADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 178 EnitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA-IRLKEIAEHQLEEaletLKNEREQKNNLRKELSQYI 256
Cdd:pfam03528 159 E----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAeDKIKELEASKMKE----LNHYLEAEKSCRTDLEMYV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 257 NLSDSHISIsvdglkFAEDGsepnndDKMNGHIHGPLGKLNGDyRTPTTRKGESLHPVSDLFSE---LNISEIQKLK--- 330
Cdd:pfam03528 231 AVLNTQKSV------LQEDA------EKLRKELHEVCHLLEQE-RQQHNQLKHTWQKANDQFLEsqrLLMRDMQRMEsvl 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907170352 331 --QQLIQVEREKaillANLQESQTQLEHTKGALTEQHERVHRLTEHV 375
Cdd:pfam03528 298 tsEQLRQVEEIK----KKDQEEHKRARTHKEKETLKSDREHTVSIHA 340
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1-241 |
3.06e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 1 MAAeeALKTVDQYKTEIERLTKELTEtthekiqaaeyglvvleekltlkqQYDELEAEYDGLKqeleqlreafGQSF-SI 79
Cdd:COG2433 338 LAA--ALKAYDAYKNKFERVEKKVPP------------------------DVDRDEVKARVIR----------GLSIeEA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 80 HRKVAEDGETREETLLQESASKEAyylNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR 159
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 160 eykfREARLLQDYTELEEENITLQKLVSTLKQNQVEyegLKHEIKRFEEETVLLNSqlEDAIRLKEIAEHqLEEALETLK 239
Cdd:COG2433 459 ----REIRKDREISRLDREIERLERELEEERERIEE---LKRKLERLKELWKLEHS--GELVPVKVVEKF-TKEAIRRLE 528
|
..
gi 1907170352 240 NE 241
Cdd:COG2433 529 EE 530
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-251 |
4.56e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETTHEK------IQAAEYGLVVLEEKL---------------TLKQQYDELEAEYDGL 62
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREReelaeeVRDLRERLEELEEERddllaeaglddadaeAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 63 KQELEQLR---EAFGQSFSIHRKVAEDGETREETL----------LQESASKEAYYLNKILEMQNELKQSRAVVTNVQAE 129
Cdd:PRK02224 327 RDRLEECRvaaQAHNEEAESLREDADDLEERAEELreeaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 130 NERLSAVVQELKENNEMVELQRIRMKDEIREYK--FREARLLQDY-------TELEEENItlqklVSTLKQNQVEYEGLK 200
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARerVEEAEALLEAgkcpecgQPVEGSPH-----VETIEEDRERVEELE 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907170352 201 HEIKRFEEETVLLNSQLEDAIRLKEiaehqLEEALETLKNEREQKNNLRKE 251
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVE-----AEDRIERLEERREDLEELIAE 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-252 |
5.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtlkqqydELEAEYDGLKQELEQLREAFGQSFSIHRKV 83
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVL-------KKESELIKLKELAEQLKELEEKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 84 AEDGETREETLLQESA--SKEAYYLNKILEMQNELKQSRAVVTN-VQAENERLSAVVQELKEN----------------- 143
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesveeleerlkelep 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 144 --NEMVELQRI--RMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQ-----NQVEYEGLKHEIKRFEEETVLLN 214
Cdd:PRK03918 600 fyNEYLELKDAekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLR 679
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907170352 215 SQLEDAIRLKEiaehQLEEALETLKNEREQKNNLRKEL 252
Cdd:PRK03918 680 AELEELEKRRE----EIKKTLEKLKEELEEREKAKKEL 713
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-244 |
6.31e-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: 43.90 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 13 YKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtLKQQYDELEAEYDGLKQELEQLREafgqsfsihRKVAEDGETREE 92
Cdd:TIGR02169 756 VKSELKELEARIEELE-EDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEA---------RLREIEQKLNRL 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 93 TLLQESASKE--------AYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFR 164
Cdd:TIGR02169 825 TLEKEYLEKEiqelqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 165 EARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNS------QLEDAIR------LKEIAEHQ-- 230
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEEIRalepvnMLAIQEYEev 984
|
250 260
....*....|....*....|
gi 1907170352 231 ------LEEALETLKNEREQ 244
Cdd:TIGR02169 985 lkrldeLKEKRAKLEEERKA 1004
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-518 |
6.31e-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: 43.90 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 11 DQYKTEIERLTKELTETTHEKIQaaeyglvvleekltLKQQYDELEAEYDGLKQELEQLREAFGQSFSIH--RKVAEDGE 88
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDK--------------LTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEKL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 89 TREETLLQESASKEAYYLNKI----LEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFR 164
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLseelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 165 EARLLQDYTELEEENITLQKLVSTLKQNQVEYE--------------GLKHEIKRFEEETVLlnsQLEDAI--RLKEIA- 227
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkasiqgvhGTVAQLGSVGERYAT---AIEVAAgnRLNNVVv 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 228 --EHQLEEALETLKNEREQK------NNLRKELSQY-INLSDSHISISVDGLKFaEDGSEP------------NNDDK-- 284
Cdd:TIGR02169 555 edDAVAKEAIELLKRRKAGRatflplNKMRDERRDLsILSEDGVIGFAVDLVEF-DPKYEPafkyvfgdtlvvEDIEAar 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 285 ----------MNGHIHGPLGKLNGDYRTPTTRKG------ESLHPVSD-----------LFSELN--------------- 322
Cdd:TIGR02169 634 rlmgkyrmvtLEGELFEKSGAMTGGSRAPRGGILfsrsepAELQRLRErleglkrelssLQSELRrienrldelsqelsd 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 323 ----ISEIQK-----------LKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVN------AMRGL 381
Cdd:TIGR02169 714 asrkIGEIEKeieqleqeeekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlSHSRI 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 382 QNSKEIKAELDCEKGRNSAeEAHDYEVDINGL----EILECKYRVAVTEVIDLKAEIKALKEKY---NKSVENYTEEKTK 454
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEA-RLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIenlNGKKEELEEELEE 872
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907170352 455 YESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
10-485 |
7.00e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 10 VDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGET 89
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 90 REE--TLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKEnnemveLQRIRmkDEIREYKFREAR 167
Cdd:PRK01156 279 EERhmKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSV------LQKDY--NDYIKKKSRYDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 168 LLQDYTELEEENITLQKLVStlkqnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEhqleealETLKNEREQknn 247
Cdd:PRK01156 351 LNNQILELEGYEMDYNSYLK-------SIESLKKKIEEYSKNIERMSAFISEILKIQEIDP-------DAIKKELNE--- 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 248 LRKELSQYiNLSDSHISISVDGLKFAEDGSEpNNDDKMNGHIHGPLgklngdyrTPTTRKGESLHPVSDLFSElnisEIQ 327
Cdd:PRK01156 414 INVKLQDI-SSKVSSLNQRIRALRENLDELS-RNMEMLNGQSVCPV--------CGTTLGEEKSNHIINHYNE----KKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 328 KLKQQLIQVEREkailLANLQESQTQLEHTKGALTEqhERVHRLTEHVNAMRGLQNS-KEIKAELDCEKGRNSAEEAHDY 406
Cdd:PRK01156 480 RLEEKIREIEIE----VKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIESARADlEDIKIKINELKDKHDKYEEIKN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 407 EVDINGLEILECKYR-----VAVTEVIDL----------KAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEK 471
Cdd:PRK01156 554 RYKSLKLEDLDSKRTswlnaLAVISLIDIetnrsrsneiKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN 633
|
490
....*....|....
gi 1907170352 472 TSKESGEKMAHMEK 485
Cdd:PRK01156 634 KYNEIQENKILIEK 647
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-490 |
8.93e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 14 KTEIERLTKELTETTHEKIQAAEYgLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREET 93
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 94 LLQESASKE-AYYLNKILEMQNELKQSRAVVTNVqaENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARllqdy 172
Cdd:PRK03918 351 EKRLEELEErHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 173 teleeenitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEhqLEEALETLKNEREQKNNLRKEL 252
Cdd:PRK03918 424 ---------LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKE--IEEKERKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 253 SQYINLSDshisiSVDGLKFAEdgsepnndDKMNGHIHGPLGKLNGDYRTPTTRKGESLHPVSDLFSELNisEIQKLKQQ 332
Cdd:PRK03918 493 SELIKLKE-----LAEQLKELE--------EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE--KLEELKKK 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 333 LIQVEREKAILLANLQESQTQLEHTK-GALTEQHERVHRLTEHVNAMRGLQNS-KEIKAELdcEKGRNSAEEAHDYEVDI 410
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAeKELEREE--KELKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 411 NGLEileckyrvavTEVIDLKAEIKALKEKYN-KSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQK 489
Cdd:PRK03918 636 AETE----------KRLEELRKELEELEKKYSeEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
.
gi 1907170352 490 M 490
Cdd:PRK03918 706 R 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-807 |
9.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 633 RDQIKHLQKAVD--RSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLK 710
Cdd:COG4913 268 RERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 711 NKYENEKAMVTETMTKLRNELKALK----EDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNtllrmaiQQ 786
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-------RE 420
|
170 180
....*....|....*....|.
gi 1907170352 787 KLALTQRLEDLEfdheqSRRS 807
Cdd:COG4913 421 LRELEAEIASLE-----RRKS 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-256 |
1.02e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 50 QQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREETLLQESAskeayylnKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------RIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 130 NERLSAVVQELKEN--NEMVELQRIRMKDEIR--------EYKFREARLLQDYTELEEENI-TLQKLVSTLKQNQVEYEG 198
Cdd:COG4942 92 IAELRAELEAQKEElaELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907170352 199 LKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYI 256
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-257 |
1.28e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 104 YYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR----EYKFREARLLQDYTELEEEN 179
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907170352 180 ITLQKLVSTLKQNQVEYEGLKHEIKRFEEE-TVLLNSQLEdaiRLKEIAEHQLEEALETLKNEREQKnnLRKELSQYIN 257
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQ---ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLIK 176
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
4-244 |
1.39e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELTETTHEKIQAAEYglvvLEEKLTLKQQY---------DELEAEYDGLKQELEQLREAfG 74
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQ----LKEQLQLLNKLlpqanlladETLADRLEELREELDAAQEA-Q 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 75 QSFSIHRKVAEDGETREETLLQESASKEayylnkilEMQNELKQSRAVVTNVQAENERLSAVVQE------------LKE 142
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVLQSDPEQFE--------QLQADYLQAKEQQRRLKQQIFALSEVVQRrphfsyedavglLGE 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 143 NNEMVElqRIRMKDEIREYKFREAR--LLQDYTELEEENITLQKLVSTLkqnQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3096 982 NSDLNE--KLRARLEQAEEARREAReqLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEELGVQADAEAEER 1056
|
250 260
....*....|....*....|....
gi 1907170352 221 IRlkeIAEHQLEEALETLKNEREQ 244
Cdd:COG3096 1057 AR---IRRDELHEELSQNRSRRSQ 1077
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-254 |
1.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 47 TLKQQYDELEAEYDGLKQELEQLREAFGQSfsiHRKVAE--------DGETREETLLQESASKEayylNKILEMQNELKQ 118
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA---EAALEEfrqknglvDLSEEAKLLLQQLSELE----SQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 119 SRAVVTNVQAENERLSAVVQELKENNEMVELqrirmKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNqveyeg 198
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907170352 199 LKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG3206 307 LQQEAQR-------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-225 |
1.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 4 EEALKTVDQYKTEIERLTKELtetthEKIQAAEYGLVVLEEKLtlkqqyDELEAEYDGLKQELEQLreAFGQSFSIHRKV 83
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKEL-----EKLEELKKKLAELEKKL------DELEEELAELLKELEEL--GFESVEELEERL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 84 AEDGETREETLLQESASKEayylnkILEMQNELKQSRAVVTNVQAENERLSAVVQELKenNEMVELQRIRMKDEIREYKF 163
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKE------LEREEKELKKLEEELDKAFEELAETEKRLEELR--KELEELEKKYSEEEYEELRE 666
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907170352 164 REARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKE 225
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE 728
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-271 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 48 LKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREETLlQESASKEAYYLNKILEMQNELKQsravvtnvq 127
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKE--------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 128 aENERLSAVVQELKENNEmvELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEY----------- 196
Cdd:TIGR04523 536 -KESKISDLEDELNKDDF--ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLikeieekekki 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907170352 197 EGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYINLSDSHISISVDGLK 271
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLK 687
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9-252 |
1.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 9 TVDQYKTEIERLTKELT--ETTHEKiqaaeyglvvLEEKLTLKQQYDELEAEYDglkqELEQLREAFGQSFSIHRKVAED 86
Cdd:PRK02224 469 TIEEDRERVEELEAELEdlEEEVEE----------VEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 87 GETREETLLQESASKEAyylnkilEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVE-LQRIR-MKDEIREYKFR 164
Cdd:PRK02224 535 KRERAEELRERAAELEA-------EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEsLERIRtLLAAIADAEDE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 165 EARL---LQDYTELEEE--------NITLQKLVSTLKQNQVEyeGLKHEIKRFEEETVllnsQLEDAIRLKEIAEHQLEE 233
Cdd:PRK02224 608 IERLrekREALAELNDErrerlaekRERKRELEAEFDEARIE--EAREDKERAEEYLE----QVEEKLDELREERDDLQA 681
|
250
....*....|....*....
gi 1907170352 234 ALETLKNEREQKNNLRKEL 252
Cdd:PRK02224 682 EIGAVENELEELEELRERR 700
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1-260 |
1.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 1 MAAEEALKTVDQYKTEIERLTK-ELTETTHEKIQAaeyglvVLEEKLTLKQQYDELEAEYDGLKQELEQ----LREAFGQ 75
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNKqKLLEAEDKLVQQ------DLEQTLALLDKIDRQKEETEQLKQQLAQapakLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 76 SFSIHRKVAEDGETREETL-LQESASKEAYYLNKILEMQNELKQ--SRAVVTNVQAEN---------ERLSAVVQELKEN 143
Cdd:PRK11281 103 LEALKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEynSQLVSLQTQPERaqaalyansQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 144 NEMVELQRIRMKDEIR-EYKFREARLLQDYTELeEENITLQklvsTLKQNQVEYegLKHEIKRFEEETVLlnsqLEDAI- 221
Cdd:PRK11281 183 KVGGKALRPSQRVLLQaEQALLNAQNDLQRKSL-EGNTQLQ----DLLQKQRDY--LTARIQRLEHQLQL----LQEAIn 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907170352 222 --RLKEiAEHQLEEALETLKNEREQKNNL-RKELSQYINLSD 260
Cdd:PRK11281 252 skRLTL-SEKTVQEAQSQDEAARIQANPLvAQELEINLQLSQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-771 |
1.84e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 632 IRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVAL-ANLK 710
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLE 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907170352 711 NKYENE--KAMVTETMTKLRNELKALKEDAA-TFSSLRAMFATRCDEYVTQLDEMQRQLAAAED 771
Cdd:COG4913 753 ERFAAAlgDAVERELRENLEERIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPE 816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-234 |
1.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 108 KILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEmvELQRIRMKDE----IREYKFREARLLQDYTELEEENITLQ 183
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907170352 184 KLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEA 234
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
9-254 |
2.29e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 9 TVDQYKTEIERLTKELTEtthEKIQAaeyglvvlEEKLTLKQQYDELEAEYDGLKQELEQlreafgqSFSIHRKVAEDGE 88
Cdd:COG5022 869 IYLQSAQRVELAERQLQE---LKIDV--------KSISSLKLVNLELESEIIELKKSLSS-------DLIENLEFKTELI 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 89 TREETLLQESASKEAyylnkiLEMQnelKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKfreaRL 168
Cdd:COG5022 931 ARLKKLLNNIDLEEG------PSIE---YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK----NF 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 169 LQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQ--LEDAIRLKEIAEHQLEEALETLKNEREQKN 246
Cdd:COG5022 998 KKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRENSL 1077
|
....*...
gi 1907170352 247 NLRKELSQ 254
Cdd:COG5022 1078 LDDKQLYQ 1085
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-255 |
2.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 43 EEKL-TLKQQYDELEAEYDGLKQELEQLREAfgqsfsihrkvaedgetreetllQESASKEAYYLNKILEMQNELKQSRA 121
Cdd:COG4913 609 RAKLaALEAELAELEEELAEAEERLEALEAE-----------------------LDALQERREALQRLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 122 VvtnvQAENERLSAVVQELKENNemvelqrirmkDEIREYKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKH 201
Cdd:COG4913 666 A----EREIAELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKG----------EIGRLEK 720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907170352 202 EIKRFEEETVLLNSQLEDAIRLKEIAEHQ-LEEALETL---KNEREQKNNLRKELSQY 255
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAAlgdAVERELRENLEERIDAL 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
632-826 |
2.89e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 632 IRDQIKHLQKAVDRSLQlsRQRAAARELApMIDKDKEALMEEILKLKSLLSTKREQIAT-LRAVLKANKQTAEVALANLK 710
Cdd:COG4942 53 LLKQLAALERRIAALAR--RIRALEQELA-ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 711 NKYENEK--AMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQ---LAAAEDEKKTLNTLLRmaiQ 785
Cdd:COG4942 130 DFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraaLEALKAERQKLLARLE---K 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907170352 786 QKLALTQRLEDLEFDHEQSRRSKGKLGKSKIGSPKVSGEAP 826
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-489 |
2.93e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 3 AEEALKTVDQYKTEIERLTKELTETTHEKIQAAEyglvvleekltLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRK 82
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-----------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 83 VAEDGETREET-----LLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDE 157
Cdd:PTZ00121 1355 AADEAEAAEEKaeaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 158 IREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLK--------HEIKRFEEETVLLNSQLEDAIRLKEIAEh 229
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaeeakkaDEAKKKAEEAKKKADEAKKAAEAKKKAD- 1513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 230 QLEEALETLKNEREQKNNLRKELSQyinLSDSHISISVDGLKFAEDGSEPNNDDKMNGHIHGPLGKLNGDYRTPTTRKGE 309
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADE---AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 310 S--LHPVSDLFSELNISEIQKLKQQliQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRL--TEHVNAMRGLQNSK 385
Cdd:PTZ00121 1591 EarIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAK 1668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 386 eiKAELDCEKgrnsAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQ 465
Cdd:PTZ00121 1669 --KAEEDKKK----AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
490 500
....*....|....*....|....*.
gi 1907170352 466 VTNLEKTSKESGE--KMAHMEKELQK 489
Cdd:PTZ00121 1743 KKKAEEAKKDEEEkkKIAHLKKEEEK 1768
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-251 |
3.06e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 2 AAEEALKTVDQYKTEIERLTKELTE-------TTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLK---QELEQLRE 71
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEElrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 72 A-----FGQSF--SIHRKVAEDGETREETLlqesaskeayylnkilemQNELKQSRAVVTNVQAENERLSAVV------Q 138
Cdd:PRK02224 451 AgkcpeCGQPVegSPHVETIEEDRERVEEL------------------EAELEDLEEEVEEVEERLERAEDLVeaedriE 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 139 ELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLE 218
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE---EAEEAREEVAELNSKLAELKERIE 589
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907170352 219 DAIRLKEIAE--HQLEEALETLKNEREQ---KNNLRKE 251
Cdd:PRK02224 590 SLERIRTLLAaiADAEDEIERLREKREAlaeLNDERRE 627
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
668-806 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 668 EALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEvALANLKNKYENEK--AMVTETMTKLRNELKALKEDAAtfsslr 745
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIdvASAEREIAELEAELERLDASSD------ 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907170352 746 amfatrcdeyvtQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRR 806
Cdd:COG4913 686 ------------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-227 |
3.27e-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: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 2 AAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLvvLEEKLTLKQQYDELEAEYDGLKQELEQLREAfgqsfsihr 81
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERLEARLDALREELDELEAQ--------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 82 kVAEDGETREETLLQESASKEAyylnkilemqnELKQSRAVVTNVQaenERLSAVVQELKENNEMVELQRIRMKDEIREY 161
Cdd:COG4913 332 -IRGNGGDRLEQLEREIERLER-----------ELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907170352 162 KFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIA 227
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEA---EIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
130-366 |
3.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 130 NERLSAVVQELKENNeMVELqrIRMKDEIREYKFREARllqdyteleEENITLQKLVSTLKQnQVEYEGLKHEIK---RF 206
Cdd:PRK05771 15 KSYKDEVLEALHELG-VVHI--EDLKEELSNERLRKLR---------SLLTKLSEALDKLRS-YLPKLNPLREEKkkvSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 207 EEETVLLNSQLEDAIRL-KEIAEhqLEEALETLKNEREQKNNLRKELSQYINLS--------DSHISISVDGLKFAEDGS 277
Cdd:PRK05771 82 KSLEELIKDVEEELEKIeKEIKE--LEEEISELENEIKELEQEIERLEPWGNFDldlslllgFKYVSVFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 278 EPNNDDKMNGHIHGPLGklNGDYRTPTTRKgESLHPVSDL-----FSELNISE-------IQKLKQQLIQVEREKAILLA 345
Cdd:PRK05771 160 LKLESDVENVEYISTDK--GYVYVVVVVLK-ELSDEVEEElkklgFERLELEEegtpselIREIKEELEEIEKERESLLE 236
|
250 260
....*....|....*....|.
gi 1907170352 346 NLQESQTQLEHTKGALTEQHE 366
Cdd:PRK05771 237 ELKELAKKYLEELLALYEYLE 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-492 |
3.47e-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: 40.90 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 325 EIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERvhrLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEEAH 404
Cdd:COG4942 63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHME 484
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
....*...
gi 1907170352 485 KELQKMTG 492
Cdd:COG4942 220 QEAEELEA 227
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1-207 |
3.75e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 1 MAAEEALKTVDQYKTEIERLTKELTETTHEK----IQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLR----- 70
Cdd:PRK05771 53 TKLSEALDKLRSYLPKLNPLREEKKKVSVKSleelIKDVEEELEKIEKEIKeLEEEISELENEIKELEQEIERLEpwgnf 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 71 ----EAFGQSFSIHRKVAEDGETREETLLQESASKEAYYLnkilemqNELKQSRAVVtnVQAENERLSAVVQELKENN-E 145
Cdd:PRK05771 133 dldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYI-------STDKGYVYVV--VVVLKELSDEVEEELKKLGfE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907170352 146 MVELQRIRM-KDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYegLKHEIKRFE 207
Cdd:PRK05771 204 RLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY--LEIELERAE 264
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-489 |
4.30e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 131 ERLSAVVQELKENnemveLQRIRmkdeireykfREARLLQDYTELEEENITLQKLVSTLKqnqveYEGLKHEIKRFEEET 210
Cdd:COG1196 189 ERLEDILGELERQ-----LEPLE----------RQAEKAERYRELKEELKELEAELLLLK-----LRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 211 VLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELsqyiNLSDSHISISVDGLKFAEDGSEPNNDDKmnghih 290
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----YELLAELARLEQDIARLEERRRELEERL------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 291 gplgklngdyrtpttrkgeslhpvsdlfsELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHR 370
Cdd:COG1196 319 -----------------------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 371 LTEHVNAMRGLQNSKEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTE 450
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907170352 451 EKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQK 489
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-216 |
4.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 7 LKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKltlKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAED 86
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK---EEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 87 GETREETLLQESASKEayyLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKEnnemvELQRIRMKDEIREYKfREA 166
Cdd:COG4717 125 LQLLPLYQELEALEAE---LAELPERLEELEERLEELRELEEELEELEAELAELQE-----ELEELLEQLSLATEE-ELQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907170352 167 RLLQDYTELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQ 216
Cdd:COG4717 196 DLAEELEELQQR---LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
36-309 |
7.98e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 36 EYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFG---QSFSIHrkVAEDGEtrEETLLQESASKEAYYLNKilem 112
Cdd:PRK10246 609 ERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLtalAGYALT--LPQEDE--EASWLATRQQEAQSWQQR---- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 113 QNELkqsravvTNVQAENERLSAVVQELKENNEMVELQrirmkdeireykfrEARLLQDYTELEEENITLQKLVSTLKQN 192
Cdd:PRK10246 681 QNEL-------TALQNRIQQLTPLLETLPQSDDLPHSE--------------ETVALDNWRQVHEQCLSLHSQLQTLQQQ 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 193 QV-EYEGLKHEIKRFEeeTVLLNSQLED-----AIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYInlsDSHISIS 266
Cdd:PRK10246 740 DVlEAQRLQKAQAQFD--TALQASVFDDqqaflAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQAL---AQHQQHR 814
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907170352 267 VDGLKFAEDGSepnnddkmngHIHGPLGKLNGDYRTPTTRKGE 309
Cdd:PRK10246 815 PDGLDLTVTVE----------QIQQELAQLAQQLRENTTRQGE 847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
41-254 |
9.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 41 VLEEKltlkqqydELEAEYDGLKQELEQLREAfgqsfsihRKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSR 120
Cdd:COG4913 217 MLEEP--------DTFEAADALVEHFDDLERA--------HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 121 AVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDY--------TELEEENITLQKLVSTLKQN 192
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 193 QVEYEGL--------KHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG4913 361 RARLEALlaalglplPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
8-496 |
9.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 8 KTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKLTLKQQ--------YDELEAEYDGLKQELEQLREAFGQSfsI 79
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEI-SNTQTQLNQLKDEQNKIKKQLSEKQKeleqnnkkIKELEKQLNQLKSEISDLNNQKEQD--W 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 80 HRKVAEDGETREETLlQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR 159
Cdd:TIGR04523 309 NKELKSELKNQEKKL-EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 160 EYKFREARLLQDYTELEEENitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDairLKEiAEHQLEEALETLK 239
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD---LTN-QDSVKELIIKNLD 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 240 NEREQKNNLRKELSQYINLSDSHISISVDGLKFAEDGSEPNNDDKMNghihgplgkLNGDYRTPTTRKGESLHPVSDLFS 319
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE---------LEEKVKDLTKKISSLKEKIEKLES 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 320 ELNI---------SEIQKLKQQLIQVEREKAILlaNLQESQTQLEHTKGAL----TEQHERVHRLTEHVNAMRGLQNSKE 386
Cdd:TIGR04523 532 EKKEkeskisdleDELNKDDFELKKENLEKEID--EKNKEIEELKQTQKSLkkkqEEKQELIDQKEKEKKDLIKEIEEKE 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170352 387 IKAELDCEKGRNSAEEAHDYEVDINGleiLECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMydeqv 466
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIEL----- 681
|
490 500 510
....*....|....*....|....*....|
gi 1907170352 467 tnlekTSKESGEKMAHMEKELQKMTGIANE 496
Cdd:TIGR04523 682 -----MKDWLKELSLHYKKYITRMIRIKDL 706
|
|
| |
