|
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: 1019.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 74 GQSFSIHRKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIR 153
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 154 MKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE 233
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 234 ALETLKNEREQKNNLRKELSQYISLND----NHISISVDGLKFAED---GSEPNND-DKMNGHIHG--PLVKLNGDYRTP 303
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDfdyvSHLSISLDGLKFSEDegaGTEPNNDgEAMDGGENGggGLKNSGLDNRTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 304 TLRKGESLNP----VSDLFSELNISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMR 379
Cdd:pfam09730 241 TPRKSEVFPPapslVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 380 GLQSSKELKAELDGEKGRDSGEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKI 459
Cdd:pfam09730 321 GLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 460 QMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYR 539
Cdd:pfam09730 401 QDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 540 QSRVTRSGslKGPDDPRGLLSPRLARRGVsspvetrTSSEPVAKESTeaSKEPSPTKTPTISPvitappsspvldTSDIR 619
Cdd:pfam09730 481 EGAGARAR--KSHQEPRGLRSPRLLTRGL-------FMGEVGTADTT--SNSPSPCSSCPGSP------------TSDFR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 620 KEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANK 699
Cdd:pfam09730 538 REPMNIYNLVAIIRDQIKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANK 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 700 QTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTL 779
Cdd:pfam09730 618 QTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSL 697
|
730 740
....*....|....*....|
gi 1231802437 780 LRMAIQQKLALTQRLEDLEF 799
Cdd:pfam09730 698 LRMAIQQKLALTQRLEDLEF 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-254 |
2.23e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 12 HYKTEIERLTKELTETThEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDgETR 90
Cdd:TIGR02168 674 ERRREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 91 EETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQ 170
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 171 DYTELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:TIGR02168 832 RIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
....
gi 1231802437 251 ELSQ 254
Cdd:TIGR02168 909 KRSE 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-254 |
3.48e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 3 AEEVLQTVDHYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLKEAFGQsfsihr 81
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELE-AELEELEAELAELEAELeELRLELEELELELEEAQAEEYELLAELAR------ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 82 kvAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 377 --AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|...
gi 1231802437 242 REQKNNLRKELSQ 254
Cdd:COG1196 455 EEEEEALLELLAE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-814 |
2.45e-10 |
|
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: 64.69 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 43 EEKLTLKQQYDELE-----AEYDSLKQELEQLKEAFgqsfsihrKVAEDGETREETLLQESaskeayylgkilemQNELK 117
Cdd:TIGR02168 213 ERYKELKAELRELElallvLRLEELREELEELQEEL--------KEAEEELEELTAELQEL--------------EEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 118 QSRAVVTNVQAENERLTAVVQDLKEnnemvELQRIRMkdEIREYKFREARLLQDYTELEEEnitLQKLVSTLKQNQVEYE 197
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALAN-----EISRLEQ--QKQILRERLANLERQLEELEAQ---LEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 198 GLKHEIKRFEEETVLLNSQLEDAIRLKEiaehQLEEALETLKNEREQKNNLRKELSQYISLNDNHISISVDGLKFAEDgs 277
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED-- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 278 epnnddkmnghihgplvklngdyrtptlRKGESLNPVSDLFSELNISEIQKLKQQLMQVEREKAILLANLQESQTQLEHT 357
Cdd:TIGR02168 415 ----------------------------RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 358 KGALTEQHERVhrltehVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVDINGLEIleckyrvavTEVIDLKAEIKAL 437
Cdd:TIGR02168 467 REELEEAEQAL------DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL---------SGILGVLSELISV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 438 KEKYNKSVENYTDEKAKY--ESKIQMYDEQVTSLEKttkESGEKMAHMEKELQKMTSIANENHSTLNT------AQDELV 509
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQ---NELGRVTFLPLDSIKGTEIQGNDREILKNiegflgVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 510 TFSEEL-----AQLYHHVCLCNNETPNRVMLDYYRQSR--------VTRSGSLKGPDDPR--GLLSPRLARRGVSSPVET 574
Cdd:TIGR02168 609 KFDPKLrkalsYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlVRPGGVITGGSAKTnsSILERRREIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 575 RTSSEPVAKESTEASKEPSPTKTPTISPVITAPPSSP---VLDTSDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSR 651
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 652 QRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNkYENEKAMVTETMTKLRNEL 731
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 732 KALKEDAATFSSLRAmfatrcdEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 848 EELSEDIESLAAEIE-------ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
...
gi 1231802437 812 GKS 814
Cdd:TIGR02168 921 REK 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-255 |
3.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 4 EEVLQTVDhyKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQ------QYDELEAEYDSLKQELEQLKEAFGQSF 77
Cdd:TIGR02169 194 DEKRQQLE--RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaierQLASLEEELEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 78 ----SIHRKVAEDGETREETL---LQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQ 150
Cdd:TIGR02169 272 qlleELNKKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 151 RIRMKDEIREYKFREARLLQdytELEEENITLQKLVSTLKQNQVEYEGLKHE---------------------------- 202
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRA---ELEEVDKEFAETRDELKDYREKLEKLKREinelkreldrlqeelqrlseeladlnaa 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1231802437 203 IKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQY 255
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-471 |
7.29e-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: 56.60 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 60 DSLKQELEQLKEaFGQSFSIhrkVAEDGE--TREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVV 137
Cdd:TIGR02168 629 DDLDNALELAKK-LRPGYRI---VTLDGDlvRPGGVITGGSAKTNS----SILERRREIEELEEKIEELEEKIAELEKAL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 138 QDLKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEEtvlLNSQL 217
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEEL 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 218 EDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQyislndnhISISVDGLKFAEDGSEPNNDD--KMNGHIHGPLVK 295
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--------LNEEAANLRERLESLERRIAAteRRLEDLEEQIEE 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 296 LNGDyrtptlrkGESLNP-VSDLFSELN--ISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLT 372
Cdd:TIGR02168 850 LSED--------IESLAAeIEELEELIEelESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 373 EHVNAMRGLQSskELKAELDGEKGRDSGEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEK 452
Cdd:TIGR02168 922 EKLAQLELRLE--GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
410
....*....|....*....
gi 1231802437 453 AKYESKIQMYDEQVTSLEK 471
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKET 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-254 |
1.08e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 41 VLEEkltLKQQYDELEAE------YDSLKQELEQLKeafGQSFSIHRKVAEDGETREETLLQESASKEAYYLGKILEMQN 114
Cdd:COG1196 194 ILGE---LERQLEPLERQaekaerYRELKEELKELE---AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 115 ELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQK----LVSTLK 190
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802437 191 QNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-518 |
2.26e-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: 55.06 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 1 MAAEEVLQTVDHYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLK---EAFGQS 76
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEELKeelESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 77 FSIHRKVAEDGETREETL---LQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIR 153
Cdd:TIGR02168 360 LEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 154 MK---------DEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEET-----VLLN----- 214
Cdd:TIGR02168 440 AEleeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvkaLLKNqsgls 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 215 ---SQLEDAIRLKEIAEHQLEEAL-------------------ETLK----------------------NEREQKNNLRK 250
Cdd:TIGR02168 520 gilGVLSELISVDEGYEAAIEAALggrlqavvvenlnaakkaiAFLKqnelgrvtflpldsikgteiqgNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 251 ELSQYISLNDNHISISV------DGLKFAEDGSEPNNDDKMNGHiHGPLVKLNGDyrtpTLRKGESLNPVSDLFsELNI- 323
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKalsyllGGVLVVDDLDNALELAKKLRP-GYRIVTLDGD----LVRPGGVITGGSAKT-NSSIl 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 324 ---SEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSG 400
Cdd:TIGR02168 674 errREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 401 EEAHDYEVDING----LEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKY----------ESKIQMYDEQV 466
Cdd:TIGR02168 754 KELTELEAEIEEleerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlRERLESLERRI 833
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1231802437 467 TSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-254 |
2.49e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 2 AAEEVLQTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEafgqsfsihr 81
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 82 kvaedgetREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREY 161
Cdd:COG1196 338 --------ELEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 162 KFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250
....*....|...
gi 1231802437 242 REQKNNLRKELSQ 254
Cdd:COG1196 486 LAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-255 |
4.83e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 3 AEEVLQTVDHYKTEIERLTKELTETTH--EKIQAAEYGLvvLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSfsih 80
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELelEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEELEEELAEL---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 81 RKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDL--KENNEMVELQRI-RMKDE 157
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleALRAAAELAAQLeELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 158 IREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALET 237
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|....*...
gi 1231802437 238 LKNEREQKNNLRKELSQY 255
Cdd:COG1196 489 AAARLLLLLEAEADYEGF 506
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
11-803 |
4.93e-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: 53.82 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 11 DHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSiHRKVAEDGETR 90
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-LNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 91 EETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREykfrearllq 170
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE---------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 171 dytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:pfam02463 315 ---KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 251 ELSQYISLNDNHISISVDGLKFAEDgsepNNDDKMNGHIHGPLVKLngdyrtpTLRKGESLNPVSDLFSELNISEIQKLK 330
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQ----LEDLLKEEKKEELEILE-------EEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 331 QQLMQVEREKAILLANLQESQTQLEHTKG-ALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVD 409
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 410 INGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKmahmeKELQK 489
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK-----ATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 490 MTSIANENHSTLNTAQDELVTFSeelaqlyhhvclcnnETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSPRlaRRGVS 569
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLK---------------ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK--ELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 570 SPVETRTSSEPVAKESTEASKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRDQI------------K 637
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIdeeeeeeeksrlK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 638 HLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNKYENEK 717
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 718 AMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRqlaaaeDEKKTLNTLLRMAIQQKLALTQRLEDL 797
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK------DELESKEEKEKEEKKELEEESQKLNLL 912
|
....*.
gi 1231802437 798 EFDHEQ 803
Cdd:pfam02463 913 EEKENE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-811 |
1.10e-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: 52.75 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 13 YKTEIERLTKELTETTHEkIQAAEYGLVVLEEKLT--------LKQQYDELEAEYDSLKQELEQLkEAFGQSFSIHRKVA 84
Cdd:TIGR02168 237 LREELEELQEELKEAEEE-LEELTAELQELEEKLEelrlevseLEEEIEELQKELYALANEISRL-EQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 85 EDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFR 164
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 165 EARLLQDYTELEEENITLQKLVSTLKQNQ--VEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNER 242
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 243 EQKNNLRKELSQYISLNDNHISISVDGLKFAEDGSEP-NNDDKMNGhIHGPLVKL---NGDYRTP---TLRKG------E 309
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALlKNQSGLSG-ILGVLSELisvDEGYEAAieaALGGRlqavvvE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 310 SLNPVSDLFSELNISEIQKLKQQLMQVEREKAILlANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRG--------- 380
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ-GNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvvddld 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 381 --LQSSKELKAE-----LDGEK--------GRDSGEEAHDYEVDInglEILECKYRVAVTE--VIDLKAEIKALKEKYNK 443
Cdd:TIGR02168 633 naLELAKKLRPGyrivtLDGDLvrpggvitGGSAKTNSSILERRR---EIEELEEKIEELEekIAELEKALAELRKELEE 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 444 SVENYTDEKAKYESKIQMYDEQVTSLEKTTKESG---EKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQLyh 520
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-- 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 521 hvclcnNETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSPRLARRGVSSPVETRTSSEPVAKESTEASKEpsptktpti 600
Cdd:TIGR02168 788 ------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE--------- 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 601 spvitappsspvldtsDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSL 680
Cdd:TIGR02168 853 ----------------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 681 LSTKREQIATLRAVLkankQTAEVALANLKnkyenekamvtetmTKLRNELKALKEDAATFSSLRamfatrcdeyVTQLD 760
Cdd:TIGR02168 917 LEELREKLAQLELRL----EGLEVRIDNLQ--------------ERLSEEYSLTLEEAEALENKI----------EDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1231802437 761 EMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
309-528 |
1.46e-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: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 309 ESLNPVSDLFSELNiSEIQKLKQQLMQVEREKAIllaNLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQssKELK 388
Cdd:TIGR02168 186 ENLDRLEDILNELE-RQLKSLERQAEKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEEL--EELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 389 AELDGEKGRDSGEEAHDYEVDiNGLEILECKYRVAVTEVIDLKAEIKALKEK---YNKSVENYTDEKAKYESKIQMYDEQ 465
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802437 466 VTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQLYHHVCLCNNE 528
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-522 |
2.81e-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: 48.13 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 4 EEVLQTVDHYKTEIERLTKELTETTHE------KIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLKEafgqS 76
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEElesleaELEELEAELEELESRLeELEEQLETLRSKVAQLELQIASLNN----E 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 77 FSIHRKVAEDGETREETLLQE-SASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMK 155
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 156 DEIREYKFREARLlqdyTELEEENITLQKLVSTLKQNQVEYEGLKH---EIKRFEE------ETVL---LNSQL-EDAIR 222
Cdd:TIGR02168 482 RELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEgyeaaiEAALggrLQAVVvENLNA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 223 LKEIAEHQLEEALETL--------------KNEREQKNNLRKELSQYISLNDNHISISV------DGLKFAEDGSEPNND 282
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllGGVLVVDDLDNALEL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 283 DKMNGHiHGPLVKLNGDyrtpTLRKGESLNPVSDLFsELNI----SEIQKLKQQLMQVEREKAILLANLQESQTQLEHTK 358
Cdd:TIGR02168 638 AKKLRP-GYRIVTLDGD----LVRPGGVITGGSAKT-NSSIlerrREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 359 GALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVDINGL---------EILECKY-RVAVTEVI 428
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELeerleeaeeELAEAEAeIEELEAQI 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 429 D---------------LKAEIKALKEKYNKSVENYTDEKAKYESKIQMYD----------EQVTSLEKTTKESGEKMAHM 483
Cdd:TIGR02168 792 EqlkeelkalrealdeLRAELTLLNEEAANLRERLESLERRIAATERRLEdleeqieelsEDIESLAAEIEELEELIEEL 871
|
570 580 590
....*....|....*....|....*....|....*....
gi 1231802437 484 EKELQKMTSIANENHSTLNTAQDELVTFSEELAQLYHHV 522
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
15-501 |
4.53e-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: 47.41 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 15 TEIERLTKELTETTHEKIQAAEYglvvLEEKLTLK-QQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREET 93
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQ----LEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 94 LLQESASKEAYylgkiLEMQNELKQSRA-VVTNVQAEN---ERLTAVVQDLKENNEMvELQRIRMKDEIREYKFREARLL 169
Cdd:pfam05483 326 ICQLTEEKEAQ-----MEELNKAKAAHSfVVTEFEATTcslEELLRTEQQRLEKNED-QLKIITMELQKKSSELEEMTKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 170 QDYTELE-EENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALE-TLKNEREQKNN 247
Cdd:pfam05483 400 KNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 248 LRKELSQYISLNDNHISISVDGLKFAEDGSepnnDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPvsdlfSELNI-SEI 326
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEAS----DMTLELKKHQEDIINCKKQEERMLKQIENLEE-----KEMNLrDEL 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 327 QKLKQQLMQVEREkaiLLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSK-----ELKAELDGEKGRDSGE 401
Cdd:pfam05483 551 ESVREEFIQKGDE---VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknieELHQENKALKKKGSAE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 402 --EAHDYEVDINGLEILECKYRVAVTEVID-LKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVtslEKTTKESGE 478
Cdd:pfam05483 628 nkQLNAYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAE 704
|
490 500
....*....|....*....|...
gi 1231802437 479 KMAHMEKELQKMTSIANENHSTL 501
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSEL 727
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-254 |
6.31e-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: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 2 AAEEVLQTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEydslKQELEQLKEAFGQSFSIHR 81
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 82 KVAEDGETREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKEnnemvelQRIRMKDEIREy 161
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLE-------RLERLEEELEE- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAiRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 426 --LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEAD 502
|
250
....*....|...
gi 1231802437 242 REQKNNLRKELSQ 254
Cdd:COG1196 503 YEGFLEGVKAALL 515
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-254 |
7.69e-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: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 43 EEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFS----IHRKVAEDGETREETLLQESASKEayylgKILEMQNELKQ 118
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdASRKIGEIEKEIEQLEQEEEKLKE-----RLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 119 SRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFR----------------EARLLQDYTELEEENITL 182
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelskleeevsriEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802437 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 ... |
14-255 |
7.89e-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: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 14 KTEIERLTKELT---ETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLKEAFgqsfsihRKVAEDGET 89
Cdd:TIGR02169 697 LRRIENRLDELSqelSDASRKIGEIEKEIEQLEQEEeKLKERLEELEEDLSSLEQEIENVKSEL-------KELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 90 REETLLQESASKEAYY-----------LGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEI 158
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEarlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 159 REykfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETvllnSQLEDAIRLKEIAEHQLEEALETL 238
Cdd:TIGR02169 850 KS---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL----RELERKIEELEAQIEKKRKRLSEL 922
|
250
....*....|....*..
gi 1231802437 239 KnerEQKNNLRKELSQY 255
Cdd:TIGR02169 923 K---AKLEALEEELSEI 936
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-191 |
8.68e-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: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 16 EIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQEL-EQLKEAFGQSFSIHRKVAEDGETREEt 93
Cdd:COG4942 56 QLAALERRIAALA-RRIRALEQELAALEAELaELEKEIAELRAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLD- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 94 llqesASKEAYYLGKILE-MQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDY 172
Cdd:COG4942 134 -----AVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170
....*....|....*....
gi 1231802437 173 TELEEENITLQKLVSTLKQ 191
Cdd:COG4942 209 AELAAELAELQQEAEELEA 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-518 |
1.13e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 2 AAEEVLQTVDHYKTEIERLTKEL--TETTHEKIQAAEYGLV-VLEEKLTLKQQYDELEAEYDSLKQELEQLKEafgqsfs 78
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 79 iHRKVAEDGETREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELqRIRMKDEI 158
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE----KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 159 REYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRL----KEIAEHQLEEA 234
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELerlkKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 235 LETLKNEREQKNNLRKELSQYISLNDNHISIS------VDGLKFAED-----GSEPNNDDKMN--GHIHGPLVKLNGDYR 301
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIkelkkaIEELKKAKGkcpvcGRELTEEHRKEllEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 302 TPTLRKGESLNPVSDLFSEL-NISEIQKLKQQLMQV----EREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVN 376
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLkKESELIKLKELAEQLkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 377 AMRGLQSSKEL-----------KAELDGEKGRDSGEEAHDYEVDINGLEILECKY---RVAVTEVIDLKAEIKALKEKYN 442
Cdd:PRK03918 550 KLEELKKKLAElekkldeleeeLAELLKELEELGFESVEELEERLKELEPFYNEYlelKDAEKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802437 443 KSVENYTDEKAKYESKIQMYDE-QVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQL 518
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-220 |
1.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 4 EEVLQTVDHYKTEIERLTKELTETThEKIQA--AEYGLVVLEEKLT--------LKQQYDELEAEYDSLKQELEQLKEAF 73
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAE-AALEEfrQKNGLVDLSEEAKlllqqlseLESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 74 GQSFSIHRKVAEDGETREetllqesaskeayYLGKILEMQNELKQSRAVVTN----VQAENERLTAVVQDLKENNEMVel 149
Cdd:COG3206 250 GSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSARYTPnhpdVIALRAQIAALRAQLQQEAQRI-- 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802437 150 qRIRMKDEIREYKFREARLLQDYTELEEEnitlqklVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3206 315 -LASLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-151 |
4.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 4 EEVLQTVDHYKTEIERLTKELTETTHE--KIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHR 81
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802437 82 KVAEDGETREETLLQESASKEA---YYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQR 151
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-234 |
4.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 102 EAYYLG-----KILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEmvELQRIRMKDE----IREYKFREARLLQDY 172
Cdd:COG4913 600 SRYVLGfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWdeidVASAEREIAELEAEL 677
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802437 173 TELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEA 234
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
88-254 |
7.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 88 ETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLtavvQDLKENNEMVELQRIRMKDEIREYKFREA- 166
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 167 -RLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIR-LKEIAEHQLEEALETLKNEREQ 244
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQR 207
|
170
....*....|
gi 1231802437 245 KNNLRKELSQ 254
Cdd:COG4717 208 LAELEEELEE 217
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1-250 |
8.57e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 1 MAAEEVLQTVDHYKTEIERLTKELTETTHEK----IQAAEYGLVVLEEKLT-LKQQYDELEAEYDSLKQELEQLkEAFGq 75
Cdd:PRK05771 53 TKLSEALDKLRSYLPKLNPLREEKKKVSVKSleelIKDVEEELEKIEKEIKeLEEEISELENEIKELEQEIERL-EPWG- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 76 SFSIhrkvaedgetrEETLLQESASKEAYyLGKILEMQNELKQSRAVVTNVQAENE---RLTAVVQDLKENNEMVElqri 152
Cdd:PRK05771 131 NFDL-----------DLSLLLGFKYVSVF-VGTVPEDKLEELKLESDVENVEYISTdkgYVYVVVVVLKELSDEVE---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 153 rmkDEIREYKFREARLlqdyteleEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRlkeiaehQLE 232
Cdd:PRK05771 195 ---EELKKLGFERLEL--------EEEGTPSELIREIKE---ELEEIEKERESLLEELKELAKKYLEELL-------ALY 253
|
250
....*....|....*...
gi 1231802437 233 EALETLKNEREQKNNLRK 250
Cdd:PRK05771 254 EYLEIELERAEALSKFLK 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-798 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 633 RDQIKHLQKAVD--RSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLK 710
Cdd:COG4913 268 RERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 711 NKYENEKAMVTETMTKLRNELKALK----EDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNtllrmaiQQ 786
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-------RE 420
|
170
....*....|..
gi 1231802437 787 KLALTQRLEDLE 798
Cdd:COG4913 421 LRELEAEIASLE 432
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
14-275 |
1.30e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 14 KTEIERLTKELT-ETTHEKIQAAEYGLVVLEEKLT----LKQQYDELEAEYDSLKQELEQlkeafgqSFSIHRKVAEDGE 88
Cdd:COG5022 858 KKRFSLLKKETIyLQSAQRVELAERQLQELKIDVKsissLKLVNLELESEIIELKKSLSS-------DLIENLEFKTELI 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 89 TREETLLQESASKEayylGKILEMQnelkqSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKfreaRL 168
Cdd:COG5022 931 ARLKKLLNNIDLEE----GPSIEYV-----KLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK----NF 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 169 LQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQ--LEDAIRLKEIAEHQLEEALETLKNEREQKN 246
Cdd:COG5022 998 KKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRENSL 1077
|
250 260
....*....|....*....|....*....
gi 1231802437 247 NLRKELSQYISLNDNHISISVDGLKFAED 275
Cdd:COG5022 1078 LDDKQLYQLESTENLLKTINVKDLEVTNR 1106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-253 |
1.41e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 13 YKTEIERLTKELTETTHEKIQAAEY---GLVVLEEKLTLKQQYDELEAEYDSL---KQELEQLKEAFGQSFSIHRKVAED 86
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLretIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 87 GETREETLLQE----SASKEAYYL------GKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEmvelqrirmkd 156
Cdd:PRK02224 291 LEEERDDLLAEagldDADAEAVEArreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE----------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 157 EIREykfrEARllqdytELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEetvllnsQLEDAIRLKEIAEHQLEEALE 236
Cdd:PRK02224 360 ELRE----EAA------ELESE---LEEAREAVEDRREEIEELEEEIEELRE-------RFGDAPVDLGNAEDFLEELRE 419
|
250
....*....|....*..
gi 1231802437 237 TLKNEREQKNNLRKELS 253
Cdd:PRK02224 420 ERDELREREAELEATLR 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-257 |
1.60e-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: 41.67 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 50 QQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLLQESAskeayylgKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------RIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 130 NERLTAVVQDLKEN--NEMVELQRIRMKDEIR--------EYKFREARLLQDYTELEEENI-TLQKLVSTLKQNQVEYEG 198
Cdd:COG4942 92 IAELRAELEAQKEElaELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802437 199 LKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYIS 257
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-261 |
1.78e-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: 41.98 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 13 YKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtLKQQYDELEAEYDSLKqelEQLKEAFGQSFSIHRKVaEDGETREE 92
Cdd:TIGR02169 756 VKSELKELEARIEELE-EDLHKLEEALNDLEARL-SHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL-NRLTLEKE 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 93 TLLQESASKEAYYL---GKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLL 169
Cdd:TIGR02169 830 YLEKEIQELQEQRIdlkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 170 QDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNS------QLEDAIR------LKEIAEHQ------- 230
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEEIRalepvnMLAIQEYEevlkrld 989
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1231802437 231 -LEEALETLKNER-------EQKNNLRKE--LSQYISLNDN 261
Cdd:TIGR02169 990 eLKEKRAKLEEERkaileriEEYEKKKREvfMEAFEAINEN 1030
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
48-390 |
1.86e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.63 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 48 LKQQYDELE---AEYDSLKQELEQlkeAFGQSFSihrKVAEDGETREETLLQESASKEAYYLgKILEMQNELKQSRAVVT 124
Cdd:pfam03528 6 LQQRVAELEkenAEFYRLKQQLEA---EFNQKRA---KFKELYLAKEEDLKRQNAVLQEAQV-ELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 125 NVQA-----ENERLTAVVQDLKENNEMVELQRIRMKDEIREY----------------KFRE------ARLLQDYTELEE 177
Cdd:pfam03528 79 NIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKETVREYevqfhrrleqeraqwnQYREsaereiADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 178 EnitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA-IRLKEIAEHQLEEaletLKNEREQKNNLRKELSQYI 256
Cdd:pfam03528 159 E----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAeDKIKELEASKMKE----LNHYLEAEKSCRTDLEMYV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 257 SLNDNHISIsvdglkFAEDGsepnndDKMNGHIHGPLVKLNGDYRTPTLRKgESLNPVSDLFSE---LNISEIQKLK--- 330
Cdd:pfam03528 231 AVLNTQKSV------LQEDA------EKLRKELHEVCHLLEQERQQHNQLK-HTWQKANDQFLEsqrLLMRDMQRMEsvl 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802437 331 --QQLMQVEREKaillANLQESQTQLEHTKGALTEQHERVHRLTEH-VNAMRGLQSSKELKAE 390
Cdd:pfam03528 298 tsEQLRQVEEIK----KKDQEEHKRARTHKEKETLKSDREHTVSIHaVFSPAGVETSAPLSNV 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-238 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 2 AAEEVLQTVDHYKTEIERLTKELTETThEKIQAAEYGLVVLEEkltLKQQYDELEAEYDSLKQELEQLKEAFGQsFSIHR 81
Cdd:COG4913 648 EALQRLAEYSWDEIDVASAEREIAELE-AELERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGR-LEKEL 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 82 KVAEDGETREETLLQESASKEA----YYLGKILEMQNELKQSRAVVTNVQAENERLTAvvqdlKENNEMVELQRIrMKDE 157
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARlelrALLEERFAAALGDAVERELRENLEERIDALRA-----RLNRAEEELERA-MRAF 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 158 IREYKFREARL---LQDYTELEEEnitLQKLVStlkQNQVEYEG-LKHEIKRFEEETVL-LNSQLEDAIRlkEIAE--HQ 230
Cdd:COG4913 797 NREWPAETADLdadLESLPEYLAL---LDRLEE---DGLPEYEErFKELLNENSIEFVAdLLSKLRRAIR--EIKEriDP 868
|
....*...
gi 1231802437 231 LEEALETL 238
Cdd:COG4913 869 LNDSLKRI 876
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-225 |
1.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 4 EEVLQTVDHYKTEIERLTKELtetthEKIQAAEYGLVVLEEKLtlkqqyDELEAEYDSLKQELEQLkeAFGQSFSIHRKV 83
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKEL-----EKLEELKKKLAELEKKL------DELEEELAELLKELEEL--GFESVEELEERL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 84 AEDGETREETLLQESASKEAYYLGKILE-MQNELKQSRAVVTNVQAENERLTavvqdlkenNEMVELQRIRMKDEIREYK 162
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKkLEEELDKAFEELAETEKRLEELR---------KELEELEKKYSEEEYEELR 665
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802437 163 FREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKE 225
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE 728
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-262 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 43 EEKL-TLKQQYDELEAEYDSLKQELEQLKEAfgqsfsihrkvaedgetreetllQESASKEAYYLGKILEMQNELKQSRA 121
Cdd:COG4913 609 RAKLaALEAELAELEEELAEAEERLEALEAE-----------------------LDALQERREALQRLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 122 VvtnvQAENERLTAVVQDLKENNemvelqrirmkDEIREYKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKH 201
Cdd:COG4913 666 A----EREIAELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKG----------EIGRLEK 720
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802437 202 EIKRFEEETVLLNSQLEDAIRLKEIAEHQ-LEEALETL---KNEREQKNNLRKELSQYISLNDNH 262
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAAlgdAVERELRENLEERIDALRARLNRA 785
|
|
| 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 1231802437 632 IRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVAL-ANLK 710
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLE 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802437 711 NKYENE--KAMVTETMTKLRNELKALKEDAA-TFSSLRAMFATRCDEYVTQLDEMQRQLAAAED 771
Cdd:COG4913 753 ERFAAAlgDAVERELRENLEERIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPE 816
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-254 |
3.87e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 47 TLKQQYDELEAEYDSLKQELEQLKEAFGQSfsiHRKVAE--------DGETREETLLQESASKEAyylgKILEMQNELKQ 118
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA---EAALEEfrqknglvDLSEEAKLLLQQLSELES----QLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 119 SRAVVTNVQAENERLTAVVQDLKENNEMVELqrirmKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNqveyeg 198
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802437 199 LKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG3206 307 LQQEAQR-------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-492 |
4.23e-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: 40.52 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 325 EIQKLKQQLMQVEREkailLANLQESQTQLEhtkgalTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAH 404
Cdd:COG4942 70 RIRALEQELAALEAE----LAELEKEIAELR------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHME 484
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
....*...
gi 1231802437 485 KELQKMTS 492
Cdd:COG4942 220 QEAEELEA 227
|
|
| 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 1231802437 668 EALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEvALANLKNKYENEK--AMVTETMTKLRNELKALKEDAAtfsslr 745
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIdvASAEREIAELEAELERLDASSD------ 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802437 746 amfatrcdeyvtQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRR 806
Cdd:COG4913 686 ------------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
17-220 |
4.48e-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: 40.71 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 17 IERLTKELTETTHEKIQAAEYG--LVVLEEKL-TLK---QQYDELEAEYDSLKQELEQLKE-AFGQSFSIHRKVAEDGET 89
Cdd:COG3096 895 LEELREELDAAQEAQAFIQQHGkaLAQLEPLVaVLQsdpEQFEQLQADYLQAKEQQRRLKQqIFALSEVVQRRPHFSYED 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 90 REETLLQESASKEAYYlGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKEN----NEMV-ELQRiRMKD-EIREYKF 163
Cdd:COG3096 975 AVGLLGENSDLNEKLR-ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSrdakQQTLqELEQ-ELEElGVQADAE 1052
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802437 164 REARLLQDYTELEEE-NITLQKLVSTLKQNQV---EYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3096 1053 AEERARIRRDELHEElSQNRSRRSQLEKQLTRceaEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-271 |
4.90e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 48 LKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLlQESASKEAYYLGKILEMQNELKQsravvtnvq 127
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKE--------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 128 aENERLTAVVQDLKENNEmvELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEY----------- 196
Cdd:TIGR04523 536 -KESKISDLEDELNKDDF--ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLikeieekekki 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802437 197 EGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYISLNDNHISISVDGLK 271
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLK 687
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
323-518 |
5.26e-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: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 323 ISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGA----LTEQHERVHRLTEHVNAMRglQSSKELKAELDGEKGRD 398
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseLKELEARIEELEEDLHKLE--EALNDLEARLSHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 399 SGEEAH--------------DYEVDINGL----EILECKYRVAVTEVIDLKAEIKALKEKY---NKSVENYTDEKAKYES 457
Cdd:TIGR02169 796 IQAELSkleeevsriearlrEIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIenlNGKKEELEEELEELEA 875
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802437 458 KIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
50-469 |
5.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 50 QQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEdGETREETLLQESASKEAyyLGKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 130 NERLTAVVQDLKEnnemVELQRIRMKDEIREYKFREARLLQDYTELEEENI-----TLQKLVSTLKQNQVEYEGLKHEIK 204
Cdd:COG4717 148 LEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELqdlaeELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 205 RFEEETVLLNSQLEDAIRLKEIAEHQ----LEEALETLKNEREQKNNLRKELSQYISLNdnhISISVDGLKFAEDGSEPN 280
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGVLFLV---LGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 281 NDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPVSDLFSELNISEIQKLKQQLMQVER-EKAILLANLQESQTQLEHTKG 359
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 360 ALTE--------QHERVHRLTEHVNAMRG--LQSSKELKAELDGEKGRDSGEEAHDYEVDingLEILECKYRVAVTEVID 429
Cdd:COG4717 381 VEDEeelraaleQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEE---LEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1231802437 430 LKAEIKALKEkyNKSVENYTDEKAKYESKIQMYDEQVTSL 469
Cdd:COG4717 458 LEAELEQLEE--DGELAELLQELEELKAELRELAEEWAAL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
632-813 |
5.83e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 632 IRDQIKHLQKAVDRSLQlsRQRAAARELApMIDKDKEALMEEILKLKSLLSTKREQIAT-LRAVLKANKQTAEVALANLK 710
Cdd:COG4942 53 LLKQLAALERRIAALAR--RIRALEQELA-ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 711 NKYENEK--AMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQ---LAAAEDEKKTLNTLLRmaiQ 785
Cdd:COG4942 130 DFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraaLEALKAERQKLLARLE---K 206
|
170 180
....*....|....*....|....*...
gi 1231802437 786 QKLALTQRLEDLEFDHEQSRRSKGKLGK 813
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
49-515 |
6.60e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 49 KQQYDELEAEYDSLKQELEQLKEafgqsfsIHRKVAEDgETREETLLQESASKEAYYLGKILEMQNELKQsravvtnvqa 128
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKK-------NIDKFLTE-IKKKEKELEKLNNKYNDLKKQKEELENELNL---------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 129 enerLTAVVQDLKENNEMVELQRIRMK---DEIREYKFREARLLQDYTELEEENITLQKlvsTLKQNQVEYEGLKHEIKR 205
Cdd:TIGR04523 178 ----LEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKD---NIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 206 FEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYISLNDNHISISVDglkfaedgSEPNNDDKM 285
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK--------SELKNQEKK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 286 NGHIHGPLVKLNgdyrtptlrkgeslnpvsDLFSELNiSEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQH 365
Cdd:TIGR04523 323 LEEIQNQISQNN------------------KIISQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 366 ERVHRLTEHVNAMRG-LQSSKELKAELDG-----EKGRDSGEEAHD---YEVDINGLEILECKYRVAVTEVI-------- 428
Cdd:TIGR04523 384 QEIKNLESQINDLESkIQNQEKLNQQKDEqikklQQEKELLEKEIErlkETIIKNNSEIKDLTNQDSVKELIiknldntr 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 429 -DLKAEIKALKEKYNK---SVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTA 504
Cdd:TIGR04523 464 eSLETQLKVLSRSINKikqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
490
....*....|.
gi 1231802437 505 QDELVTFSEEL 515
Cdd:TIGR04523 544 EDELNKDDFEL 554
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
105-440 |
7.18e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 105 YLGKILEMQNELKQSRAVVTNVQAE-NERLTAVVQDLKENNEMVELQRIRMKDEIR-EYKFREARLLQDYTELEEENITL 182
Cdd:COG5022 815 YLACIIKLQKTIKREKKLRETEEVEfSLKAEVLIQKFGRSLKAKKRFSLLKKETIYlQSAQRVELAERQLQELKIDVKSI 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 183 QKLvsTLKQNQVEYEGLkhEIKRFEEETVLLNSQledaIRLKEIAEhqleeaLETLKNEREQKNNLRKELSQYislndnh 262
Cdd:COG5022 895 SSL--KLVNLELESEII--ELKKSLSSDLIENLE----FKTELIAR------LKKLLNNIDLEEGPSIEYVKL------- 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 263 isisvdglkfaedgSEPNNDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPvsdlfselnISEIQKLKQQLmqveREKAI 342
Cdd:COG5022 954 --------------PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA---------NSELKNFKKEL----AELSK 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 343 LLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSKELKAELDgEKGRDSGEEAHDYEVDI-NGLEILECKYR 421
Cdd:COG5022 1007 QYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLL-LENNQLQARYKALKLRReNSLLDDKQLYQ 1085
|
330
....*....|....*....
gi 1231802437 422 VAVTEVIDLKAEIKALKEK 440
Cdd:COG5022 1086 LESTENLLKTINVKDLEVT 1104
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-256 |
7.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 104 YYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIR----EYKFREARLLQDYTELEEEN 179
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802437 180 ITLQKLVSTLKQNQVEYEGLKHEIKRFEEE-TVLLNSQLEdaiRLKEIAEHQLEEALETLKNEREQKnnLRKELSQYI 256
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQ---ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
41-254 |
8.27e-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: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 41 VLEEKltlkqqydELEAEYDSLKQELEQLKEAfgqsfsihRKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSR 120
Cdd:COG4913 217 MLEEP--------DTFEAADALVEHFDDLERA--------HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 121 AVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDY--------TELEEENITLQKLVSTLKQN 192
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 193 QVEYEGL--------KHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG4913 361 RARLEALlaalglplPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-255 |
8.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 16 EIERLTKELTETTHEKIQAAEyglvvlEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLL 95
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKA------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 96 Q---------ESASKEAYYLGKILEMQNELKqsravvtNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREA 166
Cdd:PRK03918 578 EleelgfesvEELEERLKELEPFYNEYLELK-------DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802437 167 RLLQDYTELEEENItlqklvstlkqnQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE------ALETLKN 240
Cdd:PRK03918 651 ELEKKYSEEEYEEL------------REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEErekakkELEKLEK 718
|
250
....*....|....*
gi 1231802437 241 EREQKNNLRKELSQY 255
Cdd:PRK03918 719 ALERVEELREKVKKY 733
|
|
| |
