|
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: 1025.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 74 GQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIR 153
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 154 MKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE 233
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 234 ALETLKNEREQKNNLRKELSQYISLSD----NHISISVEGLKFAED---GSEPNND-DKMNGHLHG--PLGKLNGDYRAP 303
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDfdyvSHLSISLDGLKFSEDegaGTEPNNDgEAMDGGENGggGLKNSGLDNRTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 304 TARKGESLHP----VSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMR 379
Cdd:pfam09730 241 TPRKSEVFPPapslVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 380 GLQNSKELKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKI 459
Cdd:pfam09730 321 GLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 460 QMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYR 539
Cdd:pfam09730 401 QDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 540 QSRVTRSGslKGPDDPRGLLSPRLSRRGVsspvesrTSSEPVSKENteTSKEPSPTKTPTISPvitappsspvldTSDIR 619
Cdd:pfam09730 481 EGAGARAR--KSHQEPRGLRSPRLLTRGL-------FMGEVGTADT--TSNSPSPCSSCPGSP------------TSDFR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 620 KEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANK 699
Cdd:pfam09730 538 REPMNIYNLVAIIRDQIKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANK 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 700 QTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTL 779
Cdd:pfam09730 618 QTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSL 697
|
730 740
....*....|....*....|
gi 1958770458 780 LRMAIQQKLALTQRLEDLEF 799
Cdd:pfam09730 698 LRMAIQQKLALTQRLEDLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-254 |
9.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 3 AEEALKTVDHYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLKEAFGQsfsihr 81
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELE-AELEELEAELAELEAELeELRLELEELELELEEAQAEEYELLAELAR------ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 kvAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 377 --AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|...
gi 1958770458 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 |
2.08e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 12 HYKTEIERLTKELTETThEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLKEAFGQSFSIHRKVAEDgETR 90
Cdd:TIGR02168 674 ERRREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 91 EETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQ 170
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 171 DYTELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:TIGR02168 832 RIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
....
gi 1958770458 251 ELSQ 254
Cdd:TIGR02168 909 KRSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-814 |
8.72e-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: 59.69 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 105 YLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKEnnEMVELQRI---------RMKDEIREYKFREARLLQDYTEL 175
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE--EIEELQKElyalaneisRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 176 EEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEiaehQLEEALETLKNEREQKNNLRKELSQY 255
Cdd:TIGR02168 322 EAQ---LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 256 ISLSDNHISISVEGLKFAEDgsepnnddkmnghlhgplgklngdyraptaRKGESLHPVSDLFSELNISEIQKLKQQLIQ 335
Cdd:TIGR02168 395 IASLNNEIERLEARLERLED------------------------------RRERLQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 336 VEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSkelkaeldCEKGRNSAEEAHDYEVDInglei 415
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS--------LERLQENLEGFSEGVKAL----- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 416 leCKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKtkyeskIQMY-----DEQVTNLEKTSKESGEKMAHMEKELQKM 490
Cdd:TIGR02168 512 --LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR------LQAVvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKG 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 491 TGIANENHNTLNT------AQDELVTFSEEL-----AQLYHHVCLCNNETPNRVMLDYYRQSR--------VTRSGSLKG 551
Cdd:TIGR02168 584 TEIQGNDREILKNiegflgVAKDLVKFDPKLrkalsYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlVRPGGVITG 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 552 PDDPR--GLLSPRLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSP---VLDTSDIRKEPMNIY 626
Cdd:TIGR02168 664 GSAKTnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 627 NLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVAL 706
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 707 ANLKNkYENEKAMVTETMTKLRNELKALKEDAATFSSLRAmfatrcdEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQ 786
Cdd:TIGR02168 824 ERLES-LERRIAATERRLEDLEEQIEELSEDIESLAAEIE-------ELEELIEELESELEALLNERASLEEALALLRSE 895
|
730 740
....*....|....*....|....*...
gi 1958770458 787 KLALTQRLEDLEFDHEQSRRSKGKLGKS 814
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-255 |
4.85e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 3 AEEALKTVDHYKTEIERLTKELTETTH--EKIQAAEYGLvvLEEKLTLKQQYDELEAEYDGLKQELEQLKEAFGQSfsih 80
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELelEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEELEEELAEL---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 81 RKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQEL--KENNEMVELQRI-RMKDE 157
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleALRAAAELAAQLeELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 158 IREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALET 237
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|....*...
gi 1958770458 238 LKNEREQKNNLRKELSQY 255
Cdd:COG1196 489 AAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-456 |
4.89e-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: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 107 NKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLV 186
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 187 STLKQNQVEYEGLKHEIKRFEEEtvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQyislsdnhISIS 266
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--------LNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 267 VEGLKFAEDGSEPNNDDKmnghlhgplGKLNGDYRAPTARKGESLHPVSDLFSELNI------SEIQKLKQQLIQVEREK 340
Cdd:TIGR02168 819 AANLRERLESLERRIAAT---------ERRLEDLEEQIEELSEDIESLAAEIEELEElieeleSELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 341 AILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNskELKAELDCEKGRNSAEEAHDYEVDINGLEILECKY 420
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958770458 421 RVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYE 456
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-254 |
5.10e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 41 VLEEkltLKQQYDELEAE------YDGLKQELEQLKeafGQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQN 114
Cdd:COG1196 194 ILGE---LERQLEPLERQaekaerYRELKEELKELE---AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 115 ELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQK----LVSTLK 190
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958770458 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 |
9.88e-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: 56.23 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 14 KTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQ------QYDELEAEYDGLKQELEQLKEAFGQSF----SIHRKV 83
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaierQLASLEEELEKLTEEISELEKRLEEIEqlleELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 84 AEDGETREETLLQESASKEAYYLN---KILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 161 YKFREARLLQdytELEEENITLQKLVSTLKQNQVEYEGLKHE----------------------------IKRFEEETVL 212
Cdd:TIGR02169 362 LKEELEDLRA---ELEEVDKEFAETRDELKDYREKLEKLKREinelkreldrlqeelqrlseeladlnaaIAGIEAKINE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958770458 213 LNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQY 255
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-518 |
1.53e-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: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 1 MAAEEALKTVDHYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLK---EAFGQS 76
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEELKeelESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 77 FSIHRKVAEDGETREETL---LQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIR 153
Cdd:TIGR02168 360 LEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 154 MkdeireykfrearllqdytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLE- 232
Cdd:TIGR02168 440 A-------------------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEn 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 233 -----EALETLKNEREQKNNLRKELSQYIS------------LSDNHISISVEGLKFAEDGSE----------------- 278
Cdd:TIGR02168 501 legfsEGVKALLKNQSGLSGILGVLSELISvdegyeaaieaaLGGRLQAVVVENLNAAKKAIAflkqnelgrvtflplds 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 279 ------PNNDDKMNGHLHGPLGKLNG-DYRAPTARKGES-----LHPVSDLFSELNI----------------------- 323
Cdd:TIGR02168 581 ikgteiQGNDREILKNIEGFLGVAKDlVKFDPKLRKALSyllggVLVVDDLDNALELakklrpgyrivtldgdlvrpggv 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 324 ---------SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKELKAELDCE 394
Cdd:TIGR02168 661 itggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 395 KGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSK 474
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1958770458 475 ESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-803 |
6.42e-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: 53.44 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 4 EEALKTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLKEAFGQSFSiHRKV 83
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-LNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 84 AEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREykf 163
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 164 rearllqdytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNERE 243
Cdd:pfam02463 315 ----------KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 244 QKNNLRKELSQYISLSDNHISISVEGLKFAEDgsepNNDDKMNGHLHGPLGKLngdyrapTARKGESLHPVSDLFSELNI 323
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQ----LEDLLKEEKKEELEILE-------EEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 324 SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKG-ALTEQHERVHRLTEHVNAMRGLQNSKELKAELDCEKGRNSAEE 402
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 403 AHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKmah 482
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK--- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 483 meKELQKMTGIANENHNTLNTAQDELVTFSeelaqlyhhvclcnnETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSP- 561
Cdd:pfam02463 611 --ATLEADEDDKRAKVVEGILKDTELTKLK---------------ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTk 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 562 -RLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRD------ 634
Cdd:pfam02463 674 eLLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEeeeeee 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 635 --QIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNK 712
Cdd:pfam02463 754 ksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 713 YENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRqlaaaeDEKKTLNTLLRMAIQQKLALTQ 792
Cdd:pfam02463 834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK------DELESKEEKEKEEKKELEEESQ 907
|
810
....*....|.
gi 1958770458 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 |
1.66e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 4 EEALKTVDHYKTEIERLTKELTETtHEKIQAAEYGLVVLEEKLTLKQQ-YDELEAEYDGLKQELEQLKEAfgqsfsihRK 82
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQEL-EEKLEELRLEVSELEEEIEELQKeLYALANEISRLEQQKQILRER--------LA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 83 VAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYK 162
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 163 FREARLLQDYTELEEENITLQKLVSTLKQNQ--VEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 241 EREQKNNLRKELSQYISLSDNHISISVEGLKFAEDGSEP-NNDDKMNGHlHGPLGKL----NGDYRAPTARKGESL-HPV 314
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALlKNQSGLSGI-LGVLSELisvdEGYEAAIEAALGGRLqAVV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 315 SD--------------------LFSELNI---SEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRL 371
Cdd:TIGR02168 552 VEnlnaakkaiaflkqnelgrvTFLPLDSikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 372 TEhVNAMRGLQNSKELKAELDCEK--------GRNSAEEAHDYEVDInglEILECKYRVAVTE--VIDLKAEIKALKEK- 440
Cdd:TIGR02168 632 DN-ALELAKKLRPGYRIVTLDGDLvrpggvitGGSAKTNSSILERRR---EIEELEEKIEELEekIAELEKALAELRKEl 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 441 --YNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02168 708 eeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 519 yhhvclcnnetpNRVMLDYYRQSRVTRSGSLKgpddprglLSPRLSR-RGVSSPVESRTSSEPVSKENTETSKEPSPTKT 597
Cdd:TIGR02168 788 ------------EAQIEQLKEELKALREALDE--------LRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 598 PTISPVITAppSSPVLDTSDIRKEPmniynlnaiIRDQIKHLQKAVDrslQLSRQRAAARELAPMIDKDKEALMEEILKL 677
Cdd:TIGR02168 848 EELSEDIES--LAAEIEELEELIEE---------LESELEALLNERA---SLEEALALLRSELEELSEELRELESKRSEL 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 678 KSLLSTKREQIATLRAVLkankQTAEVALANLKnkyenekamvtetmTKLRNELKALKEDAATFSSLRamfatrcdeyVT 757
Cdd:TIGR02168 914 RRELEELREKLAQLELRL----EGLEVRIDNLQ--------------ERLSEEYSLTLEEAEALENKI----------ED 965
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1958770458 758 QLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-518 |
7.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 2 AAEEALKTVDHYKTEIERLTKEL--TETTHEKIQAAEYGLV-VLEEKLTLKQQYDELEAEYDGLKQELEQLKEafgqsfs 78
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 79 iHRKVAEDGETREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELqRIRMKDEI 158
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE----KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 159 REYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETL 238
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 239 KNEREQKNNLRKELSQYISlsdnhisisveglkfaEDGSEPNNDDKMNGHLHGPLGKLNG-DYRAPTARKGESLHPVSDL 317
Cdd:PRK03918 390 EKELEELEKAKEEIEEEIS----------------KITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 318 FSE--LNISEIQKLKQQLIQVEREkaiLLANLQESQTQLehtkgaltEQHERVHRLTEHVNAMRGLQNSKElkaELDCEK 395
Cdd:PRK03918 454 LEEytAELKRIEKELKEIEEKERK---LRKELRELEKVL--------KKESELIKLKELAEQLKELEEKLK---KYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 396 GRNSAEEahdyevdingleileckYRVAVTEVIDLKAEIKALKEKYNKsVENYTEEKTKYESKIQMYDEQVTNLEKTSKE 475
Cdd:PRK03918 520 LEKKAEE-----------------YEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1958770458 476 SG-EKMAHMEKELQKMTGIANEnHNTLNTAQDELVTFSEELAQL 518
Cdd:PRK03918 582 LGfESVEELEERLKELEPFYNE-YLELKDAEKELEREEKELKKL 624
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-220 |
1.61e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 4 EEALKTVDHYKTEIERLTKELTETThEKIQA--AEYGLVVLEEKLT--------LKQQYDELEAEYDGLKQELEQLKEAF 73
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAE-AALEEfrQKNGLVDLSEEAKlllqqlseLESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 74 GQSFSIHRKVAEDGETREetllqesaskeayYLNKILEMQNELKQSRAVVTN----VQAENERLSAVVQELKENNEMVel 149
Cdd:COG3206 250 GSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSARYTPnhpdVIALRAQIAALRAQLQQEAQRI-- 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958770458 150 qRIRMKDEIREYKFREARLLQDYTELEEEnitlqklVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3206 315 -LASLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-514 |
1.89e-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: 48.58 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 18 ERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQL----KEAFGQSFSIHRKVA----EDGET 89
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfEEASGKKIYEHDSMStmhfRSLGS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 90 REETLLQESASKEAYYLNKILEMQNELKQSRAVVTN-----VQAENERLSAVVQEL---------KENNEMVELQRIRMK 155
Cdd:pfam15921 221 AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHeveitglteKASSARSQANSIQSQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 156 DEIREYKFRE--ARLLQDYTELEEeniTLQKLVSTLKQNQVEYEglkHEIKRFEEETVLLNSQLEDAIRLKEI------- 226
Cdd:pfam15921 301 LEIIQEQARNqnSMYMRQLSDLES---TVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTEARTERDQfsqesgn 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 227 AEHQLEEALETLkNEREQKNNLRKELSQYISLSDNHISISVEGLKfaedgSEPNNDDKMNGHLHGPLGKLNGDYRAPTAR 306
Cdd:pfam15921 375 LDDQLQKLLADL-HKREKELSLEKEQNKRLWDRDTGNSITIDHLR-----RELDDRNMEVQRLEALLKAMKSECQGQMER 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 307 -------KGESLHPVSDLFSELN---------ISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVH- 369
Cdd:pfam15921 449 qmaaiqgKNESLEKVSSLTAQLEstkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDl 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 370 RLTEhvnaMRGLQNSKE--LKAELDCEKGRNSAEEaHDYEVDI------NGLEILECKYRVAVTEVIDlKAEIKALKEKY 441
Cdd:pfam15921 529 KLQE----LQHLKNEGDhlRNVQTECEALKLQMAE-KDKVIEIlrqqieNMTQLVGQHGRTAGAMQVE-KAQLEKEINDR 602
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958770458 442 NKSVENYTEEKTKYESKIQMYDEQVTNLE----KTSKESGEKMAHMEKELQKMTGIANEnhntLNTAQDELVTFSEE 514
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNE----VKTSRNELNSLSED 675
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-528 |
1.98e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 314 VSDLFSELNiSEIQKLKQQLIQVEREKAIllaNLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQnsKELKAELDC 393
Cdd:TIGR02168 191 LEDILNELE-RQLKSLERQAEKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEEL--EELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 394 EKGRNSAEEAHDYEVDiNGLEILECKYRVAVTEVIDLKAEIKALKEK---YNKSVENYTEEKTKYESKIQMYDEQVTNLE 470
Cdd:TIGR02168 265 LEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958770458 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 ... |
15-489 |
5.37e-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: 47.02 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 15 TEIERLTKELTETTHEKIQAAEYglvvLEEKLTLK-QQYDELEAEYDGLKQELEQLKEAFGQSFSIHRKVAEDGETREET 93
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQ----LEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 94 LLQESASKEAYylnkiLEMQNELKQSRA-VVTNVQAEN---ERLSAVVQELKENNEMvELQRIRMKDEIREYKFREARLL 169
Cdd:pfam05483 326 ICQLTEEKEAQ-----MEELNKAKAAHSfVVTEFEATTcslEELLRTEQQRLEKNED-QLKIITMELQKKSSELEEMTKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 170 QDYTELE-EENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALE-TLKNEREQKNN 247
Cdd:pfam05483 400 KNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 248 LRKELSQYISLSDNHISISVEGLKFAEDGSEpnnddkmnghLHGPLGKLNGDYRAPTARKGESLHPVSDL-FSELNI-SE 325
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASD----------MTLELKKHQEDIINCKKQEERMLKQIENLeEKEMNLrDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 326 IQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAM--RGLQNSKELKAELDCEKGRNSAE-- 401
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKNIEELHQENKALKKKGSAEnk 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 402 EAHDYEVDINGLEIleckyrvavtEVIDLKAEIKALKEKYNKSVE--NYTEEK--TKYESKIQMYDEQVTNLEKTSKESG 477
Cdd:pfam05483 630 QLNAYEIKVNKLEL----------ELASAKQKFEEIIDNYQKEIEdkKISEEKllEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
490
....*....|..
gi 1958770458 478 EKMAHMEKELQK 489
Cdd:pfam05483 700 HKIAEMVALMEK 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-268 |
5.74e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 2 AAEEALKTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEydglKQELEQLKEAFgqsfsihR 81
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEA-------E 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 KVAEDGETREETLLQESASKEAyylnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAiRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 426 --LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEAD 502
|
250 260
....*....|....*....|....*..
gi 1958770458 242 REQKNNLRKELSQYISLSDNHISISVE 268
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-490 |
7.20e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 325 EIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKELKAELDCEKGRNSAEEAH 404
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHME 484
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
....*.
gi 1958770458 485 KELQKM 490
Cdd:TIGR02168 400 NEIERL 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-191 |
7.49e-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: 45.91 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 4 EEALKTVDHYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQEL-EQLKEAFGQSFSIHR 81
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALA-RRIRALEQELAALEAELaELEKEIAELRAELEAQKEELaELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 KVAEDGETREEtllqesASKEAYYLNKILE-MQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:COG4942 123 ALLLSPEDFLD------AVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|.
gi 1958770458 161 YKFREARLLQDYTELEEENITLQKLVSTLKQ 191
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-254 |
7.62e-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: 46.60 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 43 EEKLTLKQQYDELEAEYDGLKQELEQLKEAFGQSFS----IHRKVAEDGETREETLLQESASKEayylnKILEMQNELKQ 118
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdASRKIGEIEKEIEQLEQEEEKLKE-----RLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 119 SRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFR----------------EARLLQDYTELEEENITL 182
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelskleeevsriEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958770458 183 QKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLED---AIRLKEIAEHQLEEALETLKNEREqknNLRKELSQ 254
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKKERD---ELEAQLRE 900
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-265 |
8.59e-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: 46.60 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 2 AAEEALKTVDHYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLKEAFGQSFsih 80
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIEnVKSELKELEARIEELEEDLHKLEEALNDLE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 81 rkvAEDGETREETLLQESASKEAYyLNKILEMQNELKQSravVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:TIGR02169 786 ---ARLSHSRIPEIQAELSKLEEE-VSRIEARLREIEQK---LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 161 YKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKN 240
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLES----------RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
250 260
....*....|....*....|....*
gi 1958770458 241 EREQKNNLRKELSQYISLSDNHISI 265
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSL 953
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1-241 |
2.23e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 1 MAAeeALKTVDHYKTEIERLTKELTEtthekiqaaeyglvvleekltlkqQYDELEAEYDGLKqeleqlkeafGQSF-SI 79
Cdd:COG2433 338 LAA--ALKAYDAYKNKFERVEKKVPP------------------------DVDRDEVKARVIR----------GLSIeEA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 80 HRKVAEDGETREETLLQESASKEAyylNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR 159
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 160 eykfREARLLQDYTELEEENITLQKLVSTLKQNQVEyegLKHEIKRFEEETVLLNSqlEDAIRLKEIAEHqLEEALETLK 239
Cdd:COG2433 459 ----REIRKDREISRLDREIERLERELEEERERIEE---LKRKLERLKELWKLEHS--GELVPVKVVEKF-TKEAIRRLE 528
|
..
gi 1958770458 240 NE 241
Cdd:COG2433 529 EE 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-151 |
2.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 4 EEALKTVDHYKTEIERLTKELTETTHE--KIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLKEAFGQSFSIHR 81
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958770458 82 KVAEDGETREETLLQESASKEA---YYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQR 151
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
88-254 |
2.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 88 ETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLsavvQELKENNEMVELQRIRMKDEIREYKFREA- 166
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 167 -RLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIR-LKEIAEHQLEEALETLKNEREQ 244
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQR 207
|
170
....*....|
gi 1958770458 245 KNNLRKELSQ 254
Cdd:COG4717 208 LAELEEELEE 217
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
48-390 |
8.57e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.79 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 48 LKQQYDELE---AEYDGLKQELEQlkeAFGQSFSihrKVAEDGETREETLLQESASKEAYYlNKILEMQNELKQSRAVVT 124
Cdd:pfam03528 6 LQQRVAELEkenAEFYRLKQQLEA---EFNQKRA---KFKELYLAKEEDLKRQNAVLQEAQ-VELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 125 NVQA-----ENERLSAVVQELKENNEMVELQRIRMKDEIREY----------------KFRE------ARLLQDYTELEE 177
Cdd:pfam03528 79 NIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKETVREYevqfhrrleqeraqwnQYREsaereiADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 178 EnitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA-IRLKEIAEHQLEEaletLKNEREQKNNLRKELSQYI 256
Cdd:pfam03528 159 E----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAeDKIKELEASKMKE----LNHYLEAEKSCRTDLEMYV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 257 SLSDNHISISVEglkfaedgsepnNDDKMNGHLHGPLGKLNGDYRAPTARKgESLHPVSDLFSE---LNISEIQKLK--- 330
Cdd:pfam03528 231 AVLNTQKSVLQE------------DAEKLRKELHEVCHLLEQERQQHNQLK-HTWQKANDQFLEsqrLLMRDMQRMEsvl 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958770458 331 --QQLIQVEREKaillANLQESQTQLEHTKGALTEQHERVHRLTEH-VNAMRGLQNSKELKAE 390
Cdd:pfam03528 298 tsEQLRQVEEIK----KKDQEEHKRARTHKEKETLKSDREHTVSIHaVFSPAGVETSAPLSNV 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-257 |
1.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 50 QQYDELEAEYDGLKQELEQLKEAFGQSFSIHRKVAEDGETREETLLQESAskeayylnKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------RIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 130 NERLSAVVQELKEN--NEMVELQRIRMKDEIR--------EYKFREARLLQDYTELEEENI-TLQKLVSTLKQNQVEYEG 198
Cdd:COG4942 92 IAELRAELEAQKEElaELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958770458 199 LKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYIS 257
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-798 |
1.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 633 RDQIKHLQKAVD--RSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLK 710
Cdd:COG4913 268 RERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 711 NKYENEKAMVTETMTKLRNELKALK----EDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNtllrmaiQQ 786
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-------RE 420
|
170
....*....|..
gi 1958770458 787 KLALTQRLEDLE 798
Cdd:COG4913 421 LRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-238 |
1.50e-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: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 16 EIERLTKELtetthekiQAAEYGLVVLEEkltLKQQYDELEAEYDGLKQELEQLKEAFGQsFSIHRKVAEDGETREETLL 95
Cdd:COG4913 669 EIAELEAEL--------ERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRL 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 96 QESASKEAYYLNKILEMQNELKQSRAVVTNVQaenERLSAVVQELKE--NNEMVELQRIrMKDEIREYKFREARL---LQ 170
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELR---ENLEERIDALRArlNRAEEELERA-MRAFNREWPAETADLdadLE 812
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958770458 171 DYTELEEEnitLQKLVStlkQNQVEYEG-LKHEIKRFEEETVL-LNSQLEDAIRlkEIAE--HQLEEALETL 238
Cdd:COG4913 813 SLPEYLAL---LDRLEE---DGLPEYEErFKELLNENSIEFVAdLLSKLRRAIR--EIKEriDPLNDSLKRI 876
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-265 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 48 LKQQYDELEAEYDGLKQELEQLKEAFGQSFSIHRKVAEDGETREETLlQESASKEAYYLNKILEMQNELKQsravvtnvq 127
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKE--------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 128 aENERLSAVVQELKENNEmvELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEY----------- 196
Cdd:TIGR04523 536 -KESKISDLEDELNKDDF--ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLikeieekekki 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958770458 197 EGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYISLSDNHISI 265
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1-207 |
1.90e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 1 MAAEEALKTVDHYKTEIERLTKELTETTHEK----IQAAEYGLVVLEEKLT-LKQQYDELEAEYDGLKQELEQLK----- 70
Cdd:PRK05771 53 TKLSEALDKLRSYLPKLNPLREEKKKVSVKSleelIKDVEEELEKIEKEIKeLEEEISELENEIKELEQEIERLEpwgnf 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 71 ----EAFGQSFSIHRKVAEDGETREETLLQESASKEAYYLnkilemqNELKQSRAVVtnVQAENERLSAVVQELKENN-E 145
Cdd:PRK05771 133 dldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYI-------STDKGYVYVV--VVVLKELSDEVEEELKKLGfE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958770458 146 MVELQRIRM-KDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYegLKHEIKRFE 207
Cdd:PRK05771 204 RLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY--LEIELERAE 264
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-253 |
2.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 8 KTVDHYKTEIERLTKELTETTHEKIQAAEY---GLVVLEEKLTLKQQYDELEAEYDGL---KQELEQLKEAFGQSFSIHR 81
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLretIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 KVAEDGETREETLLQESAskeayylnkilemqnelkQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREY 161
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG------------------LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 162 KFREARLLQDYTELEEENITLQklvSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:PRK02224 348 REDADDLEERAEELREEAAELE---SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250
....*....|..
gi 1958770458 242 REQKNNLRKELS 253
Cdd:PRK02224 425 REREAELEATLR 436
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3-197 |
2.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 3 AEEALKTVDHYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLKEAFGQSFsihR 81
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-DALQAELEELNEEYNELQAELeALQAEIDKLQAEIAEAEAEIEERREELGERA---R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 KVAEDGETR---EETLLQESAS---KEAYYLNKILEMQNE-LKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRM 154
Cdd:COG3883 94 ALYRSGGSVsylDVLLGSESFSdflDRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958770458 155 KDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYE 197
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
632-797 |
2.11e-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: 41.97 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 632 IRDQIKHLQKAvdrsLQLSRQRAAARELAPmIDKDKEALMEEILKLKSLLSTKREQIATLR-AVLKANKQTAEV-----A 705
Cdd:TIGR02168 218 LKAELRELELA----LLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRlEVSELEEEIEELqkelyA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 706 LANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQ 785
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170
....*....|..
gi 1958770458 786 QKLALTQRLEDL 797
Cdd:TIGR02168 373 RLEELEEQLETL 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-771 |
2.31e-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: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 632 IRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVAL-ANLK 710
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLE 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958770458 711 NKYENE--KAMVTETMTKLRNELKALKEDAA-TFSSLRAMFATRCDEYVTQLDEMQRQLAAAED 771
Cdd:COG4913 753 ERFAAAlgDAVERELRENLEERIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPE 816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
13-252 |
2.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 13 YKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtlkqqydELEAEYDGLKQELEQLKEAFGQSFSIHRKVAEDGETREE 92
Cdd:PRK03918 457 YTAELKRIEKELKEIE-EKERKLRKELRELEKVL-------KKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 93 TLLQESA--SKEAYYLNKILEMQNELKQSRAVVTN-VQAENERLSAVVQELKEN-------------------NEMVELQ 150
Cdd:PRK03918 529 KLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesveeleerlkelepfyNEYLELK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 151 RI--RMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQ-----NQVEYEGLKHEIKRFEEETVLLNSQLEDAIRL 223
Cdd:PRK03918 609 DAekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
250 260
....*....|....*....|....*....
gi 1958770458 224 KEiaehQLEEALETLKNEREQKNNLRKEL 252
Cdd:PRK03918 689 RE----EIKKTLEKLKEELEEREKAKKEL 713
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-256 |
2.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 104 YYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIR----EYKFREARLLQDYTELEEEN 179
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958770458 180 ITLQKLVSTLKQNQVEYEGLKHEIKRFEEE-TVLLNSQLEdaiRLKEIAEHQLEEALETLKNEREQKnnLRKELSQYI 256
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQ---ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-234 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 108 KILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEmvELQRIRMKDE----IREYKFREARLLQDYTELEEENITLQ 183
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958770458 184 KLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEA 234
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-225 |
2.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 16 EIERLTKELTETTHEKIQAAEyglvvlEEKLTLKQQYDELEAEYDGLKQELEQLKEAFGQSF--------------SIHR 81
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKA------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAelekkldeleeelaELLK 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 KVAEDGETREETLLQESASKEAYYlNKILEMQN----------ELKQSRAVVTNVQAENERLSAVVQELKenNEMVELQR 151
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFY-NEYLELKDaekelereekELKKLEEELDKAFEELAETEKRLEELR--KELEELEK 654
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958770458 152 IRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKE 225
Cdd:PRK03918 655 KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-228 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 2 AAEEALKTVdhyKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDGLKQELEQLKEAFGQsfsIH 80
Cdd:COG4942 24 EAEAELEQL---QQEIAELEKELAALK-KEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAE---LR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 81 RKVAEDGETREETLLQESASKEAYYLnKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIRE 160
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958770458 161 YKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGlkhEIKRFEEETVLLNSQLEDAIRLKEIAE 228
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-244 |
2.67e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 13 YKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtLKQQYDELEAEYDGLKqelEQLKEAFGQSFSIHRKVaEDGETREE 92
Cdd:TIGR02169 756 VKSELKELEARIEELE-EDLHKLEEALNDLEARL-SHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL-NRLTLEKE 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 93 TLLQESASKEAYYL---NKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLL 169
Cdd:TIGR02169 830 YLEKEIQELQEQRIdlkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 170 QDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNS------QLEDAIR------LKEIAEHQ------- 230
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEEIRalepvnMLAIQEYEevlkrld 989
|
250
....*....|....*
gi 1958770458 231 -LEEALETLKNEREQ 244
Cdd:TIGR02169 990 eLKEKRAKLEEERKA 1004
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-492 |
2.81e-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: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 325 EIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERvhrLTEHVNAMRGLQNSKELKAELDCEKGRNSAEEAH 404
Cdd:COG4942 63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHME 484
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
....*...
gi 1958770458 485 KELQKMTG 492
Cdd:COG4942 220 QEAEELEA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-254 |
2.82e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 47 TLKQQYDELEAEYDGLKQELEQLKEAFGQSfsiHRKVAE--------DGETREETLLQESASKEAyylnKILEMQNELKQ 118
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA---EAALEEfrqknglvDLSEEAKLLLQQLSELES----QLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 119 SRAVVTNVQAENERLSAVVQELKENNEMVELqrirmKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNqveyeg 198
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958770458 199 LKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG3206 307 LQQEAQR-------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-518 |
3.16e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 11 DHYKTEIERLTKELTETTHEKIQaaeyglvvleekltLKQQYDELEAEYDGLKQELEQLKEAFGQSFSIH--RKVAEDGE 88
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDK--------------LTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEKL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 89 TREETLLQESASKEAYYLNKI----LEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFR 164
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLseelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 165 EARLLQDYTELEEENITLQKLVSTLKQNQVEYE--------------GLKHEIKRFEEETVLlnsQLEDAI--RLKEIA- 227
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkasiqgvhGTVAQLGSVGERYAT---AIEVAAgnRLNNVVv 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 228 --EHQLEEALETLKNEREQK------NNLRKELSQY-ISLSDNHISISVEGLKFaEDGSEP------------NNDDK-- 284
Cdd:TIGR02169 555 edDAVAKEAIELLKRRKAGRatflplNKMRDERRDLsILSEDGVIGFAVDLVEF-DPKYEPafkyvfgdtlvvEDIEAar 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 285 ----------MNGHLHGPLGKLNGDYRAPT-----------------ARKGESLHPVSDLFSELN--------------- 322
Cdd:TIGR02169 634 rlmgkyrmvtLEGELFEKSGAMTGGSRAPRggilfsrsepaelqrlrERLEGLKRELSSLQSELRrienrldelsqelsd 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 323 ----ISEIQKLKQQLIQVEREKAILLANLQESQTQLE-----------HTKGALTEQHERVHRLTEHVN------AMRGL 381
Cdd:TIGR02169 714 asrkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeienvkselkELEARIEELEEDLHKLEEALNdlearlSHSRI 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 382 QNSKELKAELDCEKGRNSAeEAHDYEVDINGL----EILECKYRVAVTEVIDLKAEIKALKEKY---NKSVENYTEEKTK 454
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEA-RLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIenlNGKKEELEEELEE 872
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958770458 455 YESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-255 |
3.98e-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: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 43 EEKL-TLKQQYDELEAEYDGLKQELEQLKEAfgqsfsihrkvaedgetreetllQESASKEAYYLNKILEMQNELKQSRA 121
Cdd:COG4913 609 RAKLaALEAELAELEEELAEAEERLEALEAE-----------------------LDALQERREALQRLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 122 VvtnvQAENERLSAVVQELKENNemvelqrirmkDEIREYKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKH 201
Cdd:COG4913 666 A----EREIAELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKG----------EIGRLEK 720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958770458 202 EIKRFEEETVLLNSQLEDAIRLKEIAEHQ-LEEALETL---KNEREQKNNLRKELSQY 255
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAAlgdAVERELRENLEERIDAL 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
668-806 |
4.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 668 EALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEvALANLKNKYENEK--AMVTETMTKLRNELKALKEDAAtfsslr 745
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIdvASAEREIAELEAELERLDASSD------ 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958770458 746 amfatrcdeyvtQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRR 806
Cdd:COG4913 686 ------------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1-260 |
4.95e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 1 MAAEEALKTVDHYKTEIERLTK-ELTETTHEKIQAaeyglvVLEEKLTLKQQYDELEAEYDGLKQELEQ----LKEAFGQ 75
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNKqKLLEAEDKLVQQ------DLEQTLALLDKIDRQKEETEQLKQQLAQapakLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 76 SFSIHRKVAEDGETREETL-LQESASKEAYYLNKILEMQNELKQ--SRAVVTNVQAEN---------ERLSAVVQELKEN 143
Cdd:PRK11281 103 LEALKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEynSQLVSLQTQPERaqaalyansQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 144 NEMVELQRIRMKDEIR-EYKFREARLLQDYTELeEENITLQklvsTLKQNQVEYegLKHEIKRFEEETVLlnsqLEDAI- 221
Cdd:PRK11281 183 KVGGKALRPSQRVLLQaEQALLNAQNDLQRKSL-EGNTQLQ----DLLQKQRDY--LTARIQRLEHQLQL----LQEAIn 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958770458 222 --RLKEiAEHQLEEALETLKNEREQKNNL-RKELSQYISLSD 260
Cdd:PRK11281 252 skRLTL-SEKTVQEAQSQDEAARIQANPLvAQELEINLQLSQ 292
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
132-469 |
5.62e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 132 RLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKH--EIKRFEEE 209
Cdd:PLN02939 29 RRLAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNraSMQRDEAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 210 TVLLNSQLEDAIRLKEIAEHQLEEALETLKNEreQKNNLRKELSQYISLSD-NHI---------SISVEGLKFAEDGSEP 279
Cdd:PLN02939 109 AAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLNQARLQALEDlEKIltekealqgKINILEMRLSETDARI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 280 NNDDKMNGH---LHGPLGKLNGDYRAPTARKGESLHPVS---DLFSELNIS---EIQKLKQQLIQV----------EREK 340
Cdd:PLN02939 187 KLAAQEKIHveiLEEQLEKLRNELLIRGATEGLCVHSLSkelDVLKEENMLlkdDIQFLKAELIEVaeteervfklEKER 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 341 AILLANLQESQTQLEHTKG-----------ALTEQHERVH----RLTEHV-NAMRGLQNSKELKAELDceKGRNSAEEAH 404
Cdd:PLN02939 267 SLLDASLRELESKFIVAQEdvsklsplqydCWWEKVENLQdlldRATNQVeKAALVLDQNQDLRDKVD--KLEASLKEAN 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958770458 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTE--EKTKYESKIQMYDEQVTNL 469
Cdd:PLN02939 345 VSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDtlSKLKEESKKRSLEHPADDM 411
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
105-440 |
6.94e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 105 YLNKILEMQNELKQSRAVVTNVQAENERLSAV-VQELKENNEMVELQRIRMKDEIR-EYKFREARLLQDYTELEEENITL 182
Cdd:COG5022 815 YLACIIKLQKTIKREKKLRETEEVEFSLKAEVlIQKFGRSLKAKKRFSLLKKETIYlQSAQRVELAERQLQELKIDVKSI 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 183 QKLvsTLKQNQVEYEGLkhEIKRFEEETVLLNSQledaIRLKEIAEhqleeaLETLKNEREQKNNLRKELSQYislsdnh 262
Cdd:COG5022 895 SSL--KLVNLELESEII--ELKKSLSSDLIENLE----FKTELIAR------LKKLLNNIDLEEGPSIEYVKL------- 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 263 isisveglkfaedgSEPNNDDKMNGHLHGPLGKLNGDYRAPTARKGESLHPvsdlfselnISEIQKLKQQLiqveREKAI 342
Cdd:COG5022 954 --------------PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA---------NSELKNFKKEL----AELSK 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 343 LLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKELKAELDCEKGRNSAeEAHDYEVDI-NGLEILECKYR 421
Cdd:COG5022 1007 QYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQA-RYKALKLRReNSLLDDKQLYQ 1085
|
330
....*....|....*....
gi 1958770458 422 VAVTEVIDLKAEIKALKEK 440
Cdd:COG5022 1086 LESTENLLKTINVKDLEVT 1104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-489 |
7.05e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 131 ERLSAVVQELKENnemveLQRIRmkdeireykfREARLLQDYTELEEENITLQKLVSTLKqnqveYEGLKHEIKRFEEET 210
Cdd:COG1196 189 ERLEDILGELERQ-----LEPLE----------RQAEKAERYRELKEELKELEAELLLLK-----LRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 211 VLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYISlsdnHISISVEGLKFAEDGSEPNNDDKmnghlh 290
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA----ELARLEQDIARLEERRRELEERL------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 291 gplgklngdyraptarkgeslhpvsdlfsELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHR 370
Cdd:COG1196 319 -----------------------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 371 LTEHVNAMRGLQNSKELKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTE 450
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958770458 451 EKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQK 489
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
632-813 |
7.24e-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: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 632 IRDQIKHLQKAVDRSLQlsRQRAAARELApMIDKDKEALMEEILKLKSLLSTKREQIAT-LRAVLKANKQTAEVALANLK 710
Cdd:COG4942 53 LLKQLAALERRIAALAR--RIRALEQELA-ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 711 NKYENEK--AMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQ---LAAAEDEKKTLNTLLRmaiQ 785
Cdd:COG4942 130 DFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraaLEALKAERQKLLARLE---K 206
|
170 180
....*....|....*....|....*...
gi 1958770458 786 QKLALTQRLEDLEFDHEQSRRSKGKLGK 813
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-227 |
7.53e-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: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 2 AAEEALKTVDHYKTEIERLTKELTETTHEKIQAAEYGLvvLEEKLTLKQQYDELEAEYDGLKQELEQLKEAfgqsfsihr 81
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERLEARLDALREELDELEAQ--------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 82 kVAEDGETREETLLQESASKEAyylnkilemqnELKQSRAVVTNVQaenERLSAVVQELKENNEMVELQRIRMKDEIREY 161
Cdd:COG4913 332 -IRGNGGDRLEQLEREIERLER-----------ELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958770458 162 KFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIA 227
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEA---EIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-251 |
9.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 4 EEALKTVDHYKTEIERLTKELTETTHEK------IQAAEYGLVVLEEKL---------------TLKQQYDELEAEYDGL 62
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREReelaeeVRDLRERLEELEEERddllaeaglddadaeAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 63 KQELEQLK---EAFGQSFSIHRKVAEDGETREETL----------LQESASKEAYYLNKILEMQNELKQSRAVVTNVQAE 129
Cdd:PRK02224 327 RDRLEECRvaaQAHNEEAESLREDADDLEERAEELreeaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770458 130 NERLSAVVQELKENNEMVELQRIRMKDEIREYK--FREARLLQDY-------TELEEENItlqklVSTLKQNQVEYEGLK 200
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARerVEEAEALLEAgkcpecgQPVEGSPH-----VETIEEDRERVEELE 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958770458 201 HEIKRFEEETVLLNSQLEDAIRLKEiaehqLEEALETLKNEREQKNNLRKE 251
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVE-----AEDRIERLEERREDLEELIAE 527
|
|
| |
