|
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: 1020.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 74 GQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIR 153
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 154 MKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE 233
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 234 ALETLKNEREQKNNLRKELSQYINLSD----SHISISVDGLKFAED---GSEPNND-DKMNGHIHG--PLGKLNGDYRTP 303
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDfdyvSHLSISLDGLKFSEDegaGTEPNNDgEAMDGGENGggGLKNSGLDNRTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 304 TTRKGESLHP----VSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMR 379
Cdd:pfam09730 241 TPRKSEVFPPapslVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 380 GLQNSKEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKI 459
Cdd:pfam09730 321 GLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 460 QMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYR 539
Cdd:pfam09730 401 QDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 540 QSRVTRSGslKGPDDPRGLLSPRLSRRGVsspvesrTSSEPVSKENteTSKEPSPTKTPTISPvitappsspvldTSDIR 619
Cdd:pfam09730 481 EGAGARAR--KSHQEPRGLRSPRLLTRGL-------FMGEVGTADT--TSNSPSPCSSCPGSP------------TSDFR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 620 KEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANK 699
Cdd:pfam09730 538 REPMNIYNLVAIIRDQIKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANK 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 700 QTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTL 779
Cdd:pfam09730 618 QTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSL 697
|
730 740
....*....|....*....|
gi 568944412 780 LRMAIQQKLALTQRLEDLEF 799
Cdd:pfam09730 698 LRMAIQQKLALTQRLEDLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-254 |
2.51e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 3 AEEALKTVDQYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLREAFGQsfsihr 81
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELE-AELEELEAELAELEAELeELRLELEELELELEEAQAEEYELLAELAR------ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 82 kvAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 377 --AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|...
gi 568944412 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 |
7.58e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 12 QYKTEIERLTKELTETThEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDgETR 90
Cdd:TIGR02168 674 ERRREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 91 EETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQ 170
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 171 DYTELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:TIGR02168 832 RIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
....
gi 568944412 251 ELSQ 254
Cdd:TIGR02168 909 KRSE 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-255 |
9.55e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 3 AEEALKTVDQYKTEIERLTKELTETTH--EKIQAAEYGLvvLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSfsih 80
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELelEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEELEEELAEL---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 81 RKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQEL--KENNEMVELQRI-RMKDE 157
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleALRAAAELAAQLeELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 158 IREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALET 237
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|....*...
gi 568944412 238 LKNEREQKNNLRKELSQY 255
Cdd:COG1196 489 AAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-814 |
1.45e-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: 55.45 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 105 YLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKEnnEMVELQRI---------RMKDEIREYKFREARLLQDYTEL 175
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE--EIEELQKElyalaneisRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 176 EEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEiaehQLEEALETLKNEREQKNNLRKELSQY 255
Cdd:TIGR02168 322 EAQ---LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 256 INLSDSHISISVDGLKFAEDgsepnnddkmnghihgplgklngdyrtpttRKGESLHPVSDLFSELNISEIQKLKQQLIQ 335
Cdd:TIGR02168 395 IASLNNEIERLEARLERLED------------------------------RRERLQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 336 VEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSkeikaeldCEKGRNSAEEAHDYEVDInglei 415
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS--------LERLQENLEGFSEGVKAL----- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 416 leCKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYeskIQMYDEQVTNL--EKTSKESGEKMAHMEKELQKMTGI 493
Cdd:TIGR02168 512 --LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQA---VVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 494 ANENHNTLNT------AQDELVTFSEEL-----AQLYHHVCLCNNETPNRVMLDYYRQSR--------VTRSGSLKGPDD 554
Cdd:TIGR02168 587 QGNDREILKNiegflgVAKDLVKFDPKLrkalsYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlVRPGGVITGGSA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 555 PR--GLLSPRLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSP---VLDTSDIRKEPMNIYNLN 629
Cdd:TIGR02168 667 KTnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 630 AIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANL 709
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 710 KNkYENEKAMVTETMTKLRNELKALKEDAATFSSLRAmfatrcdEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLA 789
Cdd:TIGR02168 827 ES-LERRIAATERRLEDLEEQIEELSEDIESLAAEIE-------ELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740
....*....|....*....|....*
gi 568944412 790 LTQRLEDLEFDHEQSRRSKGKLGKS 814
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-254 |
1.51e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 41 VLEEkltLKQQYDELEAE------YDGLKQELEQLReafGQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQN 114
Cdd:COG1196 194 ILGE---LERQLEPLERQaekaerYRELKEELKELE---AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 115 ELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQK----LVSTLK 190
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568944412 191 QNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-255 |
1.85e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 14 KTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQ------QYDELEAEYDGLKQELEQLREAFGQSF----SIHRKV 83
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaierQLASLEEELEKLTEEISELEKRLEEIEqlleELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 84 AEDGETREETLLQESASKEAYYLN---KILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 161 YKFREARLLQdytELEEENITLQKLVSTLKQNQVEYEGLKHE----------------------------IKRFEEETVL 212
Cdd:TIGR02169 362 LKEELEDLRA---ELEEVDKEFAETRDELKDYREKLEKLKREinelkreldrlqeelqrlseeladlnaaIAGIEAKINE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568944412 213 LNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQY 255
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-254 |
3.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 2 AAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREafgqsfsihr 81
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 82 kvaedgetREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREY 161
Cdd:COG1196 338 --------ELEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 162 KFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250
....*....|...
gi 568944412 242 REQKNNLRKELSQ 254
Cdd:COG1196 486 LAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-456 |
6.68e-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: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 107 NKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLV 186
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 187 STLKQNQVEYEGLKHEIKRFEEEtvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQyinlsdshISIS 266
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--------LNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 267 VDGLKFAEDGSEPNNDD--KMNGHIHGPLGKLNGDyrtpttrkGESL-HPVSDLFSELN--ISEIQKLKQQLIQVEREKA 341
Cdd:TIGR02168 819 AANLRERLESLERRIAAteRRLEDLEEQIEELSED--------IESLaAEIEELEELIEelESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 342 ILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRglQNSKEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYR 421
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLE--LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
330 340 350
....*....|....*....|....*....|....*
gi 568944412 422 VAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYE 456
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-257 |
1.09e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 1 MAAEEALKTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLR---EAFGQS 76
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEELKeelESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 77 FSIHRKVAEDGETREETL---LQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIR 153
Cdd:TIGR02168 360 LEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 154 MkdeireykfrearllqdytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLE- 232
Cdd:TIGR02168 440 A-------------------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEn 500
|
250 260 270
....*....|....*....|....*....|
gi 568944412 233 -----EALETLKNEREQKNNLRKELSQYIN 257
Cdd:TIGR02168 501 legfsEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-241 |
4.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 2 AAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHR 81
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 82 KVAEDGETREETLLQESASKEAyYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 447 --AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-------AAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-248 |
7.79e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 3 AEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQY--------------DELEAEYDGLKQELEQ 68
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeelkalrealDELRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 69 LREAFGQsfsiHRKVAEDGETREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVE 148
Cdd:TIGR02168 822 LRERLES----LERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 149 LQRIRMKDEIREYKFREARLLQDYTELEEEnitlqklvstLKQNQVEYEGLKHEIKRFEEE-TVLLNSQLEDAIRLKEIA 227
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREK----------LAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKI 963
|
250 260
....*....|....*....|.
gi 568944412 228 EHQLEEALETLKNEREQKNNL 248
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKEL 984
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-220 |
1.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETThEKIQA--AEYGLVVLEEKLT--------LKQQYDELEAEYDGLKQELEQLREAF 73
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAE-AALEEfrQKNGLVDLSEEAKlllqqlseLESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 74 GQSFSIHRKVAEDGETREetllqesaskeayYLNKILEMQNELKQSRAVVTN----VQAENERLSAVVQELKENNEMVel 149
Cdd:COG3206 250 GSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSARYTPnhpdVIALRAQIAALRAQLQQEAQRI-- 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568944412 150 qRIRMKDEIREYKFREARLLQDYTELEEEnitlqklVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3206 315 -LASLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-191 |
2.22e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQEL-EQLREAFGQSFSIHR 81
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALA-RRIRALEQELAALEAELaELEKEIAELRAELEAQKEELaELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 82 KVAEDGETREEtllqesASKEAYYLNKILE-MQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:COG4942 123 ALLLSPEDFLD------AVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|.
gi 568944412 161 YKFREARLLQDYTELEEENITLQKLVSTLKQ 191
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-514 |
4.81e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 18 ERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQL----REAFGQSFSIHRKVA----EDGET 89
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfEEASGKKIYEHDSMStmhfRSLGS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 90 REETLLQESASKEAYYLNKILEMQNELKQSRAVVTN-----VQAENERLSAVVQEL---------KENNEMVELQRIRMK 155
Cdd:pfam15921 221 AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHeveitglteKASSARSQANSIQSQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 156 DEIREYKFRE--ARLLQDYTELEEeniTLQKLVSTLKQNQVEYEglkHEIKRFEEETVLLNSQLEDAIRLKEI------- 226
Cdd:pfam15921 301 LEIIQEQARNqnSMYMRQLSDLES---TVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTEARTERDQfsqesgn 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 227 AEHQLEEALETLkNEREQKNNLRKELSQYINLSDSHISISVDGLKfaedgSEPNNDDKMNGHIHGPLGKLNGDYRTPTTR 306
Cdd:pfam15921 375 LDDQLQKLLADL-HKREKELSLEKEQNKRLWDRDTGNSITIDHLR-----RELDDRNMEVQRLEALLKAMKSECQGQMER 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 307 -------KGESLHPVSDLFSELN---------ISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVH- 369
Cdd:pfam15921 449 qmaaiqgKNESLEKVSSLTAQLEstkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDl 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 370 RLTEHVNAMRGLQNSKEIKAELDCEK----GRNSAEEAHDYEVDiNGLEILECKYRVAVTEVIDlKAEIKALKEKYNKSV 445
Cdd:pfam15921 529 KLQELQHLKNEGDHLRNVQTECEALKlqmaEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVE-KAQLEKEINDRRLEL 606
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568944412 446 ENYTEEKTKYESKIQMYDEQVTNLE----KTSKESGEKMAHMEKELQKMTGIANEnhntLNTAQDELVTFSEE 514
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNE----VKTSRNELNSLSED 675
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-811 |
5.45e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETtHEKIQAAEYGLVVLEEKLTLKQQ-YDELEAEYDGLKQELEQLREAfgqsfsihRK 82
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQEL-EEKLEELRLEVSELEEEIEELQKeLYALANEISRLEQQKQILRER--------LA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 83 VAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYK 162
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 163 FREARLLQDYTELEEENITLQKLVSTLKQNQ--VEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 241 EREQKNNLRKELSQYINLSDSHISISVDGLKFAEDGSEPNNDDKMNGHIHGPLGKL----NGDYRTPTTRKGESL-HPVS 315
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdEGYEAAIEAALGGRLqAVVV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 316 D--------------------LFSELNI---SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLT 372
Cdd:TIGR02168 553 EnlnaakkaiaflkqnelgrvTFLPLDSikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLD 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 373 EhVNAMRGLQNSKEIKAELDCEK--------GRNSAEEAHDYEVDInglEILECKYRVAVTE--VIDLKAEIKALKEK-- 440
Cdd:TIGR02168 633 N-ALELAKKLRPGYRIVTLDGDLvrpggvitGGSAKTNSSILERRR---EIEELEEKIEELEekIAELEKALAELRKEle 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 441 -YNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLy 519
Cdd:TIGR02168 709 eLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL- 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 520 hhvclcnnetpNRVMLDYYRQSRVTRSGSLKgpddprglLSPRLSR-RGVSSPVESRTSSEPVSKENTETSKEPSPTKTP 598
Cdd:TIGR02168 788 -----------EAQIEQLKEELKALREALDE--------LRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 599 TISPVITAppSSPVLDTSDIRKEPmniynlnaiIRDQIKHLQKAVDrslQLSRQRAAARELAPMIDKDKEALMEEILKLK 678
Cdd:TIGR02168 849 ELSEDIES--LAAEIEELEELIEE---------LESELEALLNERA---SLEEALALLRSELEELSEELRELESKRSELR 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 679 SLLSTKREQIATLRAVLkankQTAEVALANLKnkyenekamvtetmTKLRNELKALKEDAATFSSLRamfatrcdeyVTQ 758
Cdd:TIGR02168 915 RELEELREKLAQLELRL----EGLEVRIDNLQ--------------ERLSEEYSLTLEEAEALENKI----------EDD 966
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 568944412 759 LDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-528 |
6.51e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 314 VSDLFSELNiSEIQKLKQQLIQVEREKAIllaNLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQnsKEIKAELDC 393
Cdd:TIGR02168 191 LEDILNELE-RQLKSLERQAEKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEEL--EELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 394 EKGRNSAEEAHDYEVDiNGLEILECKYRVAVTEVIDLKAEIKALKEK---YNKSVENYTEEKTKYESKIQMYDEQVTNLE 470
Cdd:TIGR02168 265 LEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568944412 471 KTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNE 528
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-803 |
1.29e-04 |
|
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: 45.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSiHRKV 83
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-LNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 84 AEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREykf 163
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 164 rearllqdytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNERE 243
Cdd:pfam02463 315 ----------KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 244 QKNNLRKELSQYINLSDSHISISVDGLKFAEDgsepNNDDKMNGHIHGPLGKLngdyrtpTTRKGESLHPVSDLFSELNI 323
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQ----LEDLLKEEKKEELEILE-------EEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 324 SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKG-ALTEQHERVHRLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEE 402
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 403 AHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKmah 482
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK--- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 483 meKELQKMTGIANENHNTLNTAQDELVTFSeelaqlyhhvclcnnETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSP- 561
Cdd:pfam02463 611 --ATLEADEDDKRAKVVEGILKDTELTKLK---------------ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTk 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 562 -RLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRD------ 634
Cdd:pfam02463 674 eLLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEeeeeee 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 635 --QIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNK 712
Cdd:pfam02463 754 ksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 713 YENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRqlaaaeDEKKTLNTLLRMAIQQKLALTQ 792
Cdd:pfam02463 834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK------DELESKEEKEKEEKKELEEESQ 907
|
810
....*....|.
gi 568944412 793 RLEDLEFDHEQ 803
Cdd:pfam02463 908 KLNLLEEKENE 918
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-151 |
1.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETTHE--KIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHR 81
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568944412 82 KVAEDGETREETLLQESASKEA---YYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQR 151
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-490 |
2.01e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 325 EIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEEAH 404
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHME 484
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
....*.
gi 568944412 485 KELQKM 490
Cdd:TIGR02168 400 NEIERL 405
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
4-254 |
2.50e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTL---KQQYDELEAEYDGLKQELEQLREAfgqsfsiH 80
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIAEELKGKEQELIFLLQA-------R 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 81 RKVAEDGETReetlLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:pfam05483 449 EKEIHDLEIQ----LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 161 YKFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
250
....*....|....
gi 568944412 241 EREQKNNLRKELSQ 254
Cdd:pfam05483 602 QIENKNKNIEELHQ 615
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-254 |
2.60e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 43 EEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFS----IHRKVAEDGETREETLLQESASKEayylnKILEMQNELKQ 118
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdASRKIGEIEKEIEQLEQEEEKLKE-----RLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 119 SRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFR----------------EARLLQDYTELEEENITL 182
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelskleeevsriEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568944412 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 |
3.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 3 AEEALKTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLREAFGQSFsihR 81
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-DALQAELEELNEEYNELQAELeALQAEIDKLQAEIAEAEAEIEERREELGERA---R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 82 KVAEDGETR---EETLLQESAS---KEAYYLNKILEMQN----ELKQSRAVVTNVQAENE----RLSAVVQELKENNEMV 147
Cdd:COG3883 94 ALYRSGGSVsylDVLLGSESFSdflDRLSALSKIADADAdlleELKADKAELEAKKAELEaklaELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568944412 148 ELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQ 193
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-254 |
4.28e-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: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 2 AAEEALKTVDQYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLREAFGQSFsih 80
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIEnVKSELKELEARIEELEEDLHKLEEALNDLE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 81 rkvAEDGETREETLLQESASKEAYyLNKILEMQNELKQSravVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:TIGR02169 786 ---ARLSHSRIPEIQAELSKLEEE-VSRIEARLREIEQK---LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 161 YKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLES----------RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
250
....*....|....
gi 568944412 241 EREQKNNLRKELSQ 254
Cdd:TIGR02169 929 LEEELSEIEDPKGE 942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
88-254 |
6.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 88 ETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLsavvQELKENNEMVELQRIRMKDEIREYKFREA- 166
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 167 -RLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIR-LKEIAEHQLEEALETLKNEREQ 244
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQR 207
|
170
....*....|
gi 568944412 245 KNNLRKELSQ 254
Cdd:COG4717 208 LAELEEELEE 217
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1-241 |
8.36e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 1 MAAeeALKTVDQYKTEIERLTKELTEtthekiqaaeyglvvleekltlkqQYDELEAEYDGLKqeleqlreafGQSF-SI 79
Cdd:COG2433 338 LAA--ALKAYDAYKNKFERVEKKVPP------------------------DVDRDEVKARVIR----------GLSIeEA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 80 HRKVAEDGETREETLLQESASKEAyylNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR 159
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 160 eykfREARLLQDYTELEEENITLQKLVSTLKQNQVEyegLKHEIKRFEEETVLLNSqlEDAIRLKEIAEHqLEEALETLK 239
Cdd:COG2433 459 ----REIRKDREISRLDREIERLERELEEERERIEE---LKRKLERLKELWKLEHS--GELVPVKVVEKF-TKEAIRRLE 528
|
..
gi 568944412 240 NE 241
Cdd:COG2433 529 EE 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10-238 |
8.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 10 VDQYKTEIERLTKELtetthekiQAAEYGLVVLEEkltLKQQYDELEAEYDGLKQELEQLREAFGQsFSIHRKVAEDGET 89
Cdd:COG4913 663 VASAEREIAELEAEL--------ERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELD 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 90 REETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQaenERLSAVVQELKE--NNEMVELQRIrMKDEIREYKFREAR 167
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR---ENLEERIDALRArlNRAEEELERA-MRAFNREWPAETAD 806
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568944412 168 L---LQDYTELEEEnitLQKLVStlkQNQVEYEG-LKHEIKRFEEETVL-LNSQLEDAIRlkEIAE--HQLEEALETL 238
Cdd:COG4913 807 LdadLESLPEYLAL---LDRLEE---DGLPEYEErFKELLNENSIEFVAdLLSKLRRAIR--EIKEriDPLNDSLKRI 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-252 |
1.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 8 KTVDQYKTEIERLTKELTETTHEKIQAAEyglvVLEEKLTLKQQYDELEAEYDGLKQELEQLREafgqsfsihrKVAEDG 87
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERREELETLEAEIEDLRE----------TIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 88 ETREETLLQESASKEAyylnkILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREAR 167
Cdd:PRK02224 272 REREELAEEVRDLRER-----LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 168 LLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNN 247
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
....*
gi 568944412 248 LRKEL 252
Cdd:PRK02224 424 LRERE 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-798 |
1.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 633 RDQIKHLQKAVD--RSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLK 710
Cdd:COG4913 268 RERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 711 NKYENEKAMVTETMTKLRNELKALK----EDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNtllrmaiQQ 786
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-------RE 420
|
170
....*....|..
gi 568944412 787 KLALTQRLEDLE 798
Cdd:COG4913 421 LRELEAEIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-253 |
2.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 2 AAEEALKTVDQYKTEIERLTKEL--TETTHEKIQAAEYGLV-VLEEKLTLKQQYDELEAEYDGLKQELEQLREafgqsfs 78
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 79 iHRKVAEDGETREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELqRIRMKDEI 158
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE----KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 159 REYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRL----KEIAEHQLEEA 234
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELerlkKRLTGLTPEKL 389
|
250
....*....|....*....
gi 568944412 235 LETLKNEREQKNNLRKELS 253
Cdd:PRK03918 390 EKELEELEKAKEEIEEEIS 408
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1-260 |
2.55e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 1 MAAEEALKTVDQYKTEIERLTK-ELTETTHEKIQAaeyglvVLEEKLTLKQQYDELEAEYDGLKQELEQ----LREAFGQ 75
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNKqKLLEAEDKLVQQ------DLEQTLALLDKIDRQKEETEQLKQQLAQapakLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 76 SFSIHRKVAEDGETREETL-LQESASKEAYYLNKILEMQNELKQ--SRAVVTNVQAEN---------ERLSAVVQELKEN 143
Cdd:PRK11281 103 LEALKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEynSQLVSLQTQPERaqaalyansQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 144 NEMVELQRIRMKDEIR-EYKFREARLLQDYTELeEENITLQklvsTLKQNQVEYegLKHEIKRFEEETVLlnsqLEDAI- 221
Cdd:PRK11281 183 KVGGKALRPSQRVLLQaEQALLNAQNDLQRKSL-EGNTQLQ----DLLQKQRDY--LTARIQRLEHQLQL----LQEAIn 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568944412 222 --RLKEiAEHQLEEALETLKNEREQKNNL-RKELSQYINLSD 260
Cdd:PRK11281 252 skRLTL-SEKTVQEAQSQDEAARIQANPLvAQELEINLQLSQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-256 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 50 QQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREETLLQESAskeayylnKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------RIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 130 NERLSAVVQELKEN--NEMVELQRIRMKDEIR--------EYKFREARLLQDYTELEEENI-TLQKLVSTLKQNQVEYEG 198
Cdd:COG4942 92 IAELRAELEAQKEElaELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568944412 199 LKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYI 256
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-257 |
3.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 104 YYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR----EYKFREARLLQDYTELEEEN 179
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568944412 180 ITLQKLVSTLKQNQVEYEGLKHEIKRFEEE-TVLLNSQLEdaiRLKEIAEHQLEEALETLKNEREQKnnLRKELSQYIN 257
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQ---ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLIK 176
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-254 |
3.31e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 47 TLKQQYDELEAEYDGLKQELEQLREAFGQSfsiHRKVAE--------DGETREETLLQESASKEayylNKILEMQNELKQ 118
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA---EAALEEfrqknglvDLSEEAKLLLQQLSELE----SQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 119 SRAVVTNVQAENERLSAVVQELKENNEMVELqrirmKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNqveyeg 198
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568944412 199 LKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG3206 307 LQQEAQR-------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-771 |
3.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 632 IRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVAL-ANLK 710
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLE 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568944412 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 |
3.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 108 KILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEmvELQRIRMKDE----IREYKFREARLLQDYTELEEENITLQ 183
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568944412 184 KLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEA 234
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
15-490 |
3.82e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 15 TEIERLTKELTETTHEKIQAAEYglvvLEEKLTLK-QQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREET 93
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQ----LEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 94 LLQESASKEAYylnkiLEMQNELKQSRA-VVTNVQAEN---ERLSAVVQELKENNEMvELQRIRMKDEIREYKFREARLL 169
Cdd:pfam05483 326 ICQLTEEKEAQ-----MEELNKAKAAHSfVVTEFEATTcslEELLRTEQQRLEKNED-QLKIITMELQKKSSELEEMTKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 170 QDYTELE-EENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALE-TLKNEREQKNN 247
Cdd:pfam05483 400 KNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 248 LRKELSQYINLSDSHISISVDGLKFAEDGSE---------------PNNDDKMNGHIHGPLGKLNGDYRTPTTRKGESLH 312
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDmtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 313 PVSDLFSELNISE--IQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKEIKA- 389
Cdd:pfam05483 560 KGDEVKCKLDKSEenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVn 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 390 --ELDCEKGRNSAEEAHD-YEVDINGLEILE-------CKYRVAVTEVIDLKAEI-KALKEKYNKSVENYTEEKTKYESK 458
Cdd:pfam05483 640 klELELASAKQKFEEIIDnYQKEIEDKKISEeklleevEKAKAIADEAVKLQKEIdKRCQHKIAEMVALMEKHKHQYDKI 719
|
490 500 510
....*....|....*....|....*....|..
gi 568944412 459 IQMYDEQVTNLEKTSKESGEKMAHMEKELQKM 490
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
4-244 |
3.86e-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: 41.09 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETTHEKIQAAEYglvvLEEKLTLKQQY---------DELEAEYDGLKQELEQLREAfG 74
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQ----LKEQLQLLNKLlpqanlladETLADRLEELREELDAAQEA-Q 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 75 QSFSIHRKVAEDGETREETLLQESASKEayylnkilEMQNELKQSRAVVTNVQAENERLSAVVQE------------LKE 142
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVLQSDPEQFE--------QLQADYLQAKEQQRRLKQQIFALSEVVQRrphfsyedavglLGE 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 143 NNEMVElqRIRMKDEIREYKFREAR--LLQDYTELEEENITLQKLVSTLkqnQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3096 982 NSDLNE--KLRARLEQAEEARREAReqLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEELGVQADAEAEER 1056
|
250 260
....*....|....*....|....
gi 568944412 221 IRlkeIAEHQLEEALETLKNEREQ 244
Cdd:COG3096 1057 AR---IRRDELHEELSQNRSRRSQ 1077
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
5-254 |
4.56e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 5 EALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLK------QQYDELEAEYDGLKQELEQLREafgQSFS 78
Cdd:COG5022 834 ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVElaerqlQELKIDVKSISSLKLVNLELES---EIIE 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 79 IHRKVAEDGETREETLLQESASKEAYYLNKILEMQNELK-QSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDE 157
Cdd:COG5022 911 LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 158 IREYKfreaRLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQ--LEDAIRLKEIAEHQLEEAL 235
Cdd:COG5022 991 NSELK----NFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARY 1066
|
250
....*....|....*....
gi 568944412 236 ETLKNEREQKNNLRKELSQ 254
Cdd:COG5022 1067 KALKLRRENSLLDDKQLYQ 1085
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-251 |
4.71e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 4 EEALKTVDQYKTEIERLTKELTETTHEK------IQAAEYGLVVLEEKL---------------TLKQQYDELEAEYDGL 62
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREReelaeeVRDLRERLEELEEERddllaeaglddadaeAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 63 KQELEQLR---EAFGQSFSIHRKVAEDGETREETL----------LQESASKEAYYLNKILEMQNELKQSRAVVTNVQAE 129
Cdd:PRK02224 327 RDRLEECRvaaQAHNEEAESLREDADDLEERAEELreeaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 130 NERLSAVVQELKENNEMVELQRIRMKDEIREYK--FREARLLQD----------------YTELEEENITLQKLVSTLKQ 191
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARerVEEAEALLEagkcpecgqpvegsphVETIEEDRERVEELEAELED 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 192 NQVEYEGLKHEIKRFeEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKE 251
Cdd:PRK02224 487 LEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
632-797 |
4.94e-03 |
|
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: 40.43 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 632 IRDQIKHLQKAvdrsLQLSRQRAAARELAPmIDKDKEALMEEILKLKSLLSTKREQIATLR-AVLKANKQTAEV-----A 705
Cdd:TIGR02168 218 LKAELRELELA----LLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRlEVSELEEEIEELqkelyA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 706 LANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQ 785
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170
....*....|..
gi 568944412 786 QKLALTQRLEDL 797
Cdd:TIGR02168 373 RLEELEEQLETL 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-244 |
5.15e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 13 YKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREE 92
Cdd:TIGR02169 756 VKSELKELEARIEELE-EDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 93 tLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDY 172
Cdd:TIGR02169 834 -EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 173 TELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNS------QLEDAIR------LKEIAEHQ--------LE 232
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEEIRalepvnMLAIQEYEevlkrldeLK 992
|
250
....*....|..
gi 568944412 233 EALETLKNEREQ 244
Cdd:TIGR02169 993 EKRAKLEEERKA 1004
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-492 |
5.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 325 EIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERvhrLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEEAH 404
Cdd:COG4942 63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHME 484
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
....*...
gi 568944412 485 KELQKMTG 492
Cdd:COG4942 220 QEAEELEA 227
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
48-265 |
6.23e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.09 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 48 LKQQYDELE---AEYDGLKQELEQlreAFGQSfsiHRKVAEDGETREETLLQESASKEAYYlNKILEMQNELKQSRAVVT 124
Cdd:pfam03528 6 LQQRVAELEkenAEFYRLKQQLEA---EFNQK---RAKFKELYLAKEEDLKRQNAVLQEAQ-VELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 125 NVQA-----ENERLSAVVQELKENNEMVELQRIRMKDEIREY----------------KFRE------ARLLQDYTELEE 177
Cdd:pfam03528 79 NIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKETVREYevqfhrrleqeraqwnQYREsaereiADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 178 EnitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA-IRLKEIAEHQLEEaletLKNEREQKNNLRKELSQYI 256
Cdd:pfam03528 159 E----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAeDKIKELEASKMKE----LNHYLEAEKSCRTDLEMYV 230
|
....*....
gi 568944412 257 NLSDSHISI 265
Cdd:pfam03528 231 AVLNTQKSV 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
668-806 |
6.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 668 EALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEvALANLKNKYENEK--AMVTETMTKLRNELKALKEDAAtfsslr 745
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIdvASAEREIAELEAELERLDASSD------ 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568944412 746 amfatrcdeyvtQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRR 806
Cdd:COG4913 686 ------------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-255 |
7.90e-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: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 43 EEKL-TLKQQYDELEAEYDGLKQELEQLREAfgqsfsihrkvaedgetreetllQESASKEAYYLNKILEMQNELKQSRA 121
Cdd:COG4913 609 RAKLaALEAELAELEEELAEAEERLEALEAE-----------------------LDALQERREALQRLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 122 VvtnvQAENERLSAVVQELKENNemvelqrirmkDEIREYKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKH 201
Cdd:COG4913 666 A----EREIAELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKG----------EIGRLEK 720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568944412 202 EIKRFEEETVLLNSQLEDAIRLKEIAEHQ-LEEALETL---KNEREQKNNLRKELSQY 255
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAAlgdAVERELRENLEERIDAL 778
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1-207 |
8.08e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 1 MAAEEALKTVDQYKTEIERLTKELTETTHEK----IQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLR----- 70
Cdd:PRK05771 53 TKLSEALDKLRSYLPKLNPLREEKKKVSVKSleelIKDVEEELEKIEKEIKeLEEEISELENEIKELEQEIERLEpwgnf 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 71 ----EAFGQSFSIHRKVAEDGETREETLLQESASKEAYYLnkilemqNELKQSRAVVtnVQAENERLSAVVQELKENN-E 145
Cdd:PRK05771 133 dldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYI-------STDKGYVYVV--VVVLKELSDEVEEELKKLGfE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568944412 146 MVELQRIRM-KDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYegLKHEIKRFE 207
Cdd:PRK05771 204 RLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY--LEIELERAE 264
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-227 |
8.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 2 AAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLvvLEEKLTLKQQYDELEAEYDGLKQELEQLREAfgqsfsihr 81
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERLEARLDALREELDELEAQ--------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 82 kVAEDGETREETLLQESASKEAyylnkilemqnELKQSRAVVTNVQaenERLSAVVQELKENNEMVELQRIRMKDEIREY 161
Cdd:COG4913 332 -IRGNGGDRLEQLEREIERLER-----------ELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568944412 162 KFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIA 227
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEA---EIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
130-366 |
9.51e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 130 NERLSAVVQELKENNeMVELqrIRMKDEIREYKFREARllqdyteleEENITLQKLVSTLKQnQVEYEGLKHEIK---RF 206
Cdd:PRK05771 15 KSYKDEVLEALHELG-VVHI--EDLKEELSNERLRKLR---------SLLTKLSEALDKLRS-YLPKLNPLREEKkkvSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 207 EEETVLLNSQLEDAIRL-KEIAEhqLEEALETLKNEREQKNNLRKELSQYINLS--------DSHISISVDGLKFAEDGS 277
Cdd:PRK05771 82 KSLEELIKDVEEELEKIeKEIKE--LEEEISELENEIKELEQEIERLEPWGNFDldlslllgFKYVSVFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944412 278 EPNNDDKMNGHIHGPLGklNGDYRTPTTRKgESLHPVSDL-----FSELNISE-------IQKLKQQLIQVEREKAILLA 345
Cdd:PRK05771 160 LKLESDVENVEYISTDK--GYVYVVVVVLK-ELSDEVEEElkklgFERLELEEegtpselIREIKEELEEIEKERESLLE 236
|
250 260
....*....|....*....|.
gi 568944412 346 NLQESQTQLEHTKGALTEQHE 366
Cdd:PRK05771 237 ELKELAKKYLEELLALYEYLE 257
|
|
| |
