|
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: 1037.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 74 GQSFSIHRKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIR 153
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 154 MKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE 233
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 234 ALETLKNEREQKNNLRKELSQYISLND----NHISISVDGLKFAED---GSEPNND-DKMNGHIHG--PLVKLNGDYRTP 303
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDfdyvSHLSISLDGLKFSEDegaGTEPNNDgEAMDGGENGggGLKNSGLDNRTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 304 TLRKGESLNP----VSDLFSELNISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMR 379
Cdd:pfam09730 241 TPRKSEVFPPapslVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 380 GLQSSKELKAELDGEKGRDSGEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKI 459
Cdd:pfam09730 321 GLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 460 QMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYR 539
Cdd:pfam09730 401 QDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 540 QSRVTRSGslKGPDDPRGLLSPRLARRGVsspvetrTSSEPVAKESTeaSKEPSPTKTPTISPvitappsspvldTSDIR 619
Cdd:pfam09730 481 EGAGARAR--KSHQEPRGLRSPRLLTRGL-------FMGEVGTADTT--SNSPSPCSSCPGSP------------TSDFR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 620 KEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANK 699
Cdd:pfam09730 538 REPMNIYNLVAIIRDQIKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANK 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 700 QTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTL 779
Cdd:pfam09730 618 QTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSL 697
|
730 740
....*....|....*....|
gi 51039802 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 |
5.00e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 12 HYKTEIERLTKELTETThEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDgETR 90
Cdd:TIGR02168 674 ERRREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 91 EETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQ 170
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 171 DYTELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:TIGR02168 832 RIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
....
gi 51039802 251 ELSQ 254
Cdd:TIGR02168 909 KRSE 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-254 |
8.90e-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: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 3 AEEVLQTVDHYKTEIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLKEAFGQsfsihr 81
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELE-AELEELEAELAELEAELeELRLELEELELELEEAQAEEYELLAELAR------ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 82 kvAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREy 161
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 377 --AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|...
gi 51039802 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 |
8.98e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 43 EEKLTLKQQYDELE-----AEYDSLKQELEQLKEAFgqsfsihrKVAEDGETREETLLQESaskeayylgkilemQNELK 117
Cdd:TIGR02168 213 ERYKELKAELRELElallvLRLEELREELEELQEEL--------KEAEEELEELTAELQEL--------------EEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 118 QSRAVVTNVQAENERLTAVVQDLKEnnemvELQRIRMkdEIREYKFREARLLQDYTELEEEnitLQKLVSTLKQNQVEYE 197
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALAN-----EISRLEQ--QKQILRERLANLERQLEELEAQ---LEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 198 GLKHEIKRFEEETVLLNSQLEDAIRLKEiaehQLEEALETLKNEREQKNNLRKELSQYISLNDNHISISVDGLKFAEDgs 277
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED-- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 278 epnnddkmnghihgplvklngdyrtptlRKGESLNPVSDLFSELNISEIQKLKQQLMQVEREKAILLANLQESQTQLEHT 357
Cdd:TIGR02168 415 ----------------------------RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 358 KGALTEQHERVhrltehVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVDINGLEIleckyrvavTEVIDLKAEIKAL 437
Cdd:TIGR02168 467 REELEEAEQAL------DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL---------SGILGVLSELISV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 438 KEKYNKSVENYTDEKAKY--ESKIQMYDEQVTSLEKttkESGEKMAHMEKELQKMTSIANENHSTLNT------AQDELV 509
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQ---NELGRVTFLPLDSIKGTEIQGNDREILKNiegflgVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 510 TFSEEL-----AQLYHHVCLCNNETPNRVMLDYYRQSR--------VTRSGSLKGPDDPR--GLLSPRLARRGVSSPVET 574
Cdd:TIGR02168 609 KFDPKLrkalsYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlVRPGGVITGGSAKTnsSILERRREIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 575 RTSSEPVAKESTEASKEPSPTKTPTISPVITAPPSSP---VLDTSDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSR 651
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 652 QRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNkYENEKAMVTETMTKLRNEL 731
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 732 KALKEDAATFSSLRAmfatrcdEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 848 EELSEDIESLAAEIE-------ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
...
gi 51039802 812 GKS 814
Cdd:TIGR02168 921 REK 923
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
11-803 |
4.89e-09 |
|
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: 60.37 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 11 DHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSiHRKVAEDGETR 90
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-LNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 91 EETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREykfrearllq 170
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE---------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 171 dytELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRK 250
Cdd:pfam02463 315 ---KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 251 ELSQYISLNDNHISISVDGLKFAEDgsepNNDDKMNGHIHGPLVKLngdyrtpTLRKGESLNPVSDLFSELNISEIQKLK 330
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQ----LEDLLKEEKKEELEILE-------EEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 331 QQLMQVEREKAILLANLQESQTQLEHTKG-ALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVD 409
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 410 INGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKmahmeKELQK 489
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK-----ATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 490 MTSIANENHSTLNTAQDELVTFSeelaqlyhhvclcnnETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSPRlaRRGVS 569
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLK---------------ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK--ELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 570 SPVETRTSSEPVAKESTEASKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRDQI------------K 637
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIdeeeeeeeksrlK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 638 HLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNKYENEK 717
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 718 AMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRqlaaaeDEKKTLNTLLRMAIQQKLALTQRLEDL 797
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK------DELESKEEKEKEEKKELEEESQKLNLL 912
|
....*.
gi 51039802 798 EFDHEQ 803
Cdd:pfam02463 913 EEKENE 918
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-255 |
5.98e-09 |
|
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: 60.08 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDhyKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQ------QYDELEAEYDSLKQELEQLKEAFGQSF 77
Cdd:TIGR02169 194 DEKRQQLE--RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaierQLASLEEELEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 78 ----SIHRKVAEDGETREETL---LQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQ 150
Cdd:TIGR02169 272 qlleELNKKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 151 RIRMKDEIREYKFREARLLQdytELEEENITLQKLVSTLKQNQVEYEGLKHE---------------------------- 202
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRA---ELEEVDKEFAETRDELKDYREKLEKLKREinelkreldrlqeelqrlseeladlnaa 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 51039802 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 |
9.81e-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: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 60 DSLKQELEQLKEaFGQSFSIhrkVAEDGE--TREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVV 137
Cdd:TIGR02168 629 DDLDNALELAKK-LRPGYRI---VTLDGDlvRPGGVITGGSAKTNS----SILERRREIEELEEKIEELEEKIAELEKAL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 138 QDLKENNEmvelqriRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQL 217
Cdd:TIGR02168 701 AELRKELE-------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE---RIAQLSKELTELEAEIEELEERL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 218 EDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSqyiSLNDNH--ISISVDGLKFAEDGSEPNNDD--KMNGHIHGPL 293
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALD---ELRAELtlLNEEAANLRERLESLERRIAAteRRLEDLEEQI 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 294 VKLNGDyrtptlrkGESLNP-VSDLFSELN--ISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHR 370
Cdd:TIGR02168 848 EELSED--------IESLAAeIEELEELIEelESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 371 LTEHVNAMR-GLQsskELKAELDGEKGRDSGEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYT 449
Cdd:TIGR02168 920 LREKLAQLElRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
410 420
....*....|....*....|..
gi 51039802 450 DEKAKYESKIQMYDEQVTSLEK 471
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKET 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-518 |
1.35e-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: 58.91 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 1 MAAEEVLQTVDHYKTEIERLTKELtETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLK---EAFGQS 76
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEELKeelESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 77 FSIHRKVAEDGETREETL---LQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIR 153
Cdd:TIGR02168 360 LEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 154 MK---------DEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEET-----VLLNSQ--- 216
Cdd:TIGR02168 440 AEleeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvkaLLKNQSgls 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 217 -----LEDAIRLKEIAEHQLEEAL-------------------ETLK----------------------NEREQKNNLRK 250
Cdd:TIGR02168 520 gilgvLSELISVDEGYEAAIEAALggrlqavvvenlnaakkaiAFLKqnelgrvtflpldsikgteiqgNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 251 ELSQYISLNDNHISISV------DGLKFAEDGSEPNNDDKMNGHiHGPLVKLNGDyrtpTLRKGESLNPVSDLFsELNI- 323
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKalsyllGGVLVVDDLDNALELAKKLRP-GYRIVTLDGD----LVRPGGVITGGSAKT-NSSIl 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 324 ---SEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSG 400
Cdd:TIGR02168 674 errREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 401 EEAHDYEVDING----LEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKY----------ESKIQMYDEQV 466
Cdd:TIGR02168 754 KELTELEAEIEEleerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlRERLESLERRI 833
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 51039802 467 TSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-811 |
2.76e-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: 58.14 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 13 YKTEIERLTKELTETTHEkIQAAEYGLVVLEEKLT--------LKQQYDELEAEYDSLKQELEQLkEAFGQSFSIHRKVA 84
Cdd:TIGR02168 237 LREELEELQEELKEAEEE-LEELTAELQELEEKLEelrlevseLEEEIEELQKELYALANEISRL-EQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 85 EDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFR 164
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 165 EARLLQDYTELEEENITLQKLVSTLKQNQ---------VEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEAL 235
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIeellkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 236 ETLKNEREQKNNLRKELSQYISLNDNHISISvDGLKFAEdgsepNNDDKMNGhIHGPLVKL---NGDYRTP---TLRKG- 308
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFS-EGVKALL-----KNQSGLSG-ILGVLSELisvDEGYEAAieaALGGRl 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 309 -----ESLNPVSDLFSELNISEIQKLKQQLMQVEREKAILlANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRG--- 380
Cdd:TIGR02168 548 qavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ-GNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvl 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 381 --------LQSSKELKAE-----LDGEK--------GRDSGEEAHDYEVDInglEILECKYRVAVTE--VIDLKAEIKAL 437
Cdd:TIGR02168 627 vvddldnaLELAKKLRPGyrivtLDGDLvrpggvitGGSAKTNSSILERRR---EIEELEEKIEELEekIAELEKALAEL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 438 KEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESG---EKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEE 514
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 515 LAQLyhhvclcnnetpNRVMLDYYRQSRVTRSGSLKgpddprglLSPRLAR-RGVSSPVETRTSSEPVAKESTEASKEPS 593
Cdd:TIGR02168 784 IEEL------------EAQIEQLKEELKALREALDE--------LRAELTLlNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 594 PTKTPTISPVITAppSSPVLDTSDIRKEPmniynlnaiIRDQIKHLQKAVDrslQLSRQRAAARELAPMIDKDKEALMEE 673
Cdd:TIGR02168 844 EEQIEELSEDIES--LAAEIEELEELIEE---------LESELEALLNERA---SLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 674 ILKLKSLLSTKREQIATLRAVLkankQTAEVALANLKnkyenekamvtetmTKLRNELKALKEDAATFSSLRamfatrcd 753
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRL----EGLEVRIDNLQ--------------ERLSEEYSLTLEEAEALENKI-------- 963
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 51039802 754 eyVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKL 811
Cdd:TIGR02168 964 --EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-254 |
3.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 41 VLEEkltLKQQYDELEAE------YDSLKQELEQLKeafGQSFSIHRKVAEDGETREETLLQESASKEAYYLGKILEMQN 114
Cdd:COG1196 194 ILGE---LERQLEPLERQaekaerYRELKEELKELE---AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 115 ELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQK----LVSTLK 190
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51039802 191 QNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-254 |
8.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 2 AAEEVLQTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEafgqsfsihr 81
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 82 kvaedgetREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREY 161
Cdd:COG1196 338 --------ELEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 162 KFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250
....*....|...
gi 51039802 242 REQKNNLRKELSQ 254
Cdd:COG1196 486 LAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-255 |
1.25e-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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 3 AEEVLQTVDHYKTEIERLTKELTETTH--EKIQAAEYGLvvLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSfsih 80
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELelEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEELEEELAEL---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 81 RKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDL--KENNEMVELQRI-RMKDE 157
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleALRAAAELAAQLeELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 158 IREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALET 237
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|....*...
gi 51039802 238 LKNEREQKNNLRKELSQY 255
Cdd:COG1196 489 AAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
309-528 |
4.28e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 309 ESLNPVSDLFSELNiSEIQKLKQQLMQVEREKAIllaNLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQssKELK 388
Cdd:TIGR02168 186 ENLDRLEDILNELE-RQLKSLERQAEKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEEL--EELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 389 AELDGEKGRDSGEEAHDYEVDiNGLEILECKYRVAVTEVIDLKAEIKALKEK---YNKSVENYTDEKAKYESKIQMYDEQ 465
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51039802 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 |
1.25e-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: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELTETTHE------KIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLKEafgqS 76
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEElesleaELEELEAELEELESRLeELEEQLETLRSKVAQLELQIASLNN----E 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 77 FSIHRKVAEDGETREETLLQE-SASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMK 155
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 156 DEIREYKFReARLLQDyteLEEENITLQKLVSTLKQNQVEYEGLKH---EIKRFEE------ETVL---LNSQL-EDAIR 222
Cdd:TIGR02168 482 RELAQLQAR-LDSLER---LQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEgyeaaiEAALggrLQAVVvENLNA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 223 LKEIAEHQLEEALETL--------------KNEREQKNNLRKELSQYISLNDNHISISV------DGLKFAEDGSEPNND 282
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllGGVLVVDDLDNALEL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 283 DKMNGHiHGPLVKLNGDyrtpTLRKGESLNPVSDLFsELNI----SEIQKLKQQLMQVEREKAILLANLQESQTQLEHTK 358
Cdd:TIGR02168 638 AKKLRP-GYRIVTLDGD----LVRPGGVITGGSAKT-NSSIlerrREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 359 GALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVDINGL---------EILECKY-RVAVTEVI 428
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELeerleeaeeELAEAEAeIEELEAQI 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 429 D---------------LKAEIKALKEKYNKSVENYTDEKAKYESKIQMYD----------EQVTSLEKTTKESGEKMAHM 483
Cdd:TIGR02168 792 EqlkeelkalrealdeLRAELTLLNEEAANLRERLESLERRIAATERRLEdleeqieelsEDIESLAAEIEELEELIEEL 871
|
570 580 590
....*....|....*....|....*....|....*....
gi 51039802 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 |
1.96e-06 |
|
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: 52.03 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 15 TEIERLTKELTETTHEKIQAAEYglvvLEEKLTLK-QQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREET 93
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQ----LEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 94 LLQESASKEAYylgkiLEMQNELKQSRA-VVTNVQAEN---ERLTAVVQDLKENNEMvELQRIRMKDEIREYKFREARLL 169
Cdd:pfam05483 326 ICQLTEEKEAQ-----MEELNKAKAAHSfVVTEFEATTcslEELLRTEQQRLEKNED-QLKIITMELQKKSSELEEMTKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 170 QDYTELE-EENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALE-TLKNEREQKNN 247
Cdd:pfam05483 400 KNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhYLKEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 248 LRKELSQYISLNDNHISISVDGLKFAEDGSepnnDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPvsdlfSELNI-SEI 326
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEAS----DMTLELKKHQEDIINCKKQEERMLKQIENLEE-----KEMNLrDEL 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 327 QKLKQQLMQVEREkaiLLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSK-----ELKAELDGEKGRDSGE 401
Cdd:pfam05483 551 ESVREEFIQKGDE---VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknieELHQENKALKKKGSAE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 402 --EAHDYEVDINGLEILECKYRVAVTEVID-LKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVtslEKTTKESGE 478
Cdd:pfam05483 628 nkQLNAYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAE 704
|
490 500
....*....|....*....|...
gi 51039802 479 KMAHMEKELQKMTSIANENHSTL 501
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSEL 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-518 |
5.22e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 2 AAEEVLQTVDHYKTEIERLTKEL--TETTHEKIQAAEYGLV-VLEEKLTLKQQYDELEAEYDSLKQELEQLKEafgqsfs 78
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIkrTENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 79 iHRKVAEDGETREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELqRIRMKDEI 158
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE----KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 159 REYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRL----KEIAEHQLEEA 234
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELerlkKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 235 LETLKNEREQKNNLRKELSQYISLNDNHISIS------VDGLKFAED-----GSEPNNDDKMN--GHIHGPLVKLNGDYR 301
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIkelkkaIEELKKAKGkcpvcGRELTEEHRKEllEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 302 TPTLRKGESLNPVSDLFSEL-NISEIQKLKQQLMQV----EREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVN 376
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLkKESELIKLKELAEQLkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 377 AMRGLQSSKEL-----------KAELDGEKGRDSGEEAHDYEVDINGLEILECKY---RVAVTEVIDLKAEIKALKEKYN 442
Cdd:PRK03918 550 KLEELKKKLAElekkldeleeeLAELLKELEELGFESVEELEERLKELEPFYNEYlelKDAEKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51039802 443 KSVENYTDEKAKYESKIQMYDE-QVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQL 518
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-254 |
1.91e-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: 48.91 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 43 EEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFS----IHRKVAEDGETREETLLQESASKEayylgKILEMQNELKQ 118
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdASRKIGEIEKEIEQLEQEEEKLKE-----RLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 119 SRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFR----------------EARLLQDYTELEEENITL 182
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelskleeevsriEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51039802 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 |
1.96e-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: 48.91 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 14 KTEIERLTKELT---ETTHEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQELEQLKEAFgqsfsihRKVAEDGET 89
Cdd:TIGR02169 697 LRRIENRLDELSqelSDASRKIGEIEKEIEQLEQEEeKLKERLEELEEDLSSLEQEIENVKSEL-------KELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 90 REETLLQESASKEAYY-----------LGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEI 158
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEarlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 159 REykfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETvllnSQLEDAIRLKEIAEHQLEEALETL 238
Cdd:TIGR02169 850 KS---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL----RELERKIEELEAQIEKKRKRLSEL 922
|
250
....*....|....*..
gi 51039802 239 KnerEQKNNLRKELSQY 255
Cdd:TIGR02169 923 K---AKLEALEEELSEI 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-254 |
2.05e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 2 AAEEVLQTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEydslKQELEQLKEAFGQSFSIHR 81
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 82 KVAEDGETREETLLQESASKEAyylgKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKEnnemvelQRIRMKDEIREy 161
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLE-------RLERLEEELEE- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 162 kfREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAiRLKEIAEHQLEEALETLKNE 241
Cdd:COG1196 426 --LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEAD 502
|
250
....*....|...
gi 51039802 242 REQKNNLRKELSQ 254
Cdd:COG1196 503 YEGFLEGVKAALL 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-191 |
4.10e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 16 EIERLTKELTETThEKIQAAEYGLVVLEEKL-TLKQQYDELEAEYDSLKQEL-EQLKEAFGQSFSIHRKVAEDGETREEt 93
Cdd:COG4942 56 QLAALERRIAALA-RRIRALEQELAALEAELaELEKEIAELRAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLD- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 94 llqesASKEAYYLGKILE-MQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDY 172
Cdd:COG4942 134 -----AVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170
....*....|....*....
gi 51039802 173 TELEEENITLQKLVSTLKQ 191
Cdd:COG4942 209 AELAAELAELQQEAEELEA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-220 |
8.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELTETThEKIQA--AEYGLVVLEEKLT--------LKQQYDELEAEYDSLKQELEQLKEAF 73
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAE-AALEEfrQKNGLVDLSEEAKlllqqlseLESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 74 GQSFSIHRKVAEDGETREetllqesaskeayYLGKILEMQNELKQSRAVVTN----VQAENERLTAVVQDLKEnnemvEL 149
Cdd:COG3206 250 GSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSARYTPnhpdVIALRAQIAALRAQLQQ-----EA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51039802 150 QRIR--MKDEIREYKFREARLLQDYTELEEEnitlqklVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3206 312 QRILasLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-151 |
1.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELTETTHE--KIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHR 81
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51039802 82 KVAEDGETREETLLQESASKEA---YYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQR 151
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
49-515 |
1.43e-04 |
|
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: 45.78 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 49 KQQYDELEAEYDSLKQELEQLKEafgqsfsIHRKVAEDgETREETLLQESASKEAYYLGKILEMQNELKQsravvtnvqa 128
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKK-------NIDKFLTE-IKKKEKELEKLNNKYNDLKKQKEELENELNL---------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 129 enerLTAVVQDLKENNEMVELQRIRMK---DEIREYKFREARLLQDYTELEEENITLQKlvsTLKQNQVEYEGLKHEIKR 205
Cdd:TIGR04523 178 ----LEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKD---NIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 206 FEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQyisLNDNHISISVDGLKfaedgSEPNNDDKM 285
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD---LNNQKEQDWNKELK-----SELKNQEKK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 286 NGHIHGPLVKLNgdyrtptlrkgeslnpvsDLFSELNiSEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQH 365
Cdd:TIGR04523 323 LEEIQNQISQNN------------------KIISQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 366 ERVHRLTEHVNAMRG-LQSSKELKAELDG-----EKGRDSGEEAHD---YEVDINGLEILECKYRVAVTEVI-------- 428
Cdd:TIGR04523 384 QEIKNLESQINDLESkIQNQEKLNQQKDEqikklQQEKELLEKEIErlkETIIKNNSEIKDLTNQDSVKELIiknldntr 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 429 -DLKAEIKALKEKYNK---SVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTA 504
Cdd:TIGR04523 464 eSLETQLKVLSRSINKikqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
490
....*....|.
gi 51039802 505 QDELVTFSEEL 515
Cdd:TIGR04523 544 EDELNKDDFEL 554
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
88-254 |
1.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 88 ETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLtavvQDLKENNEMVELQRIRMKDEIREYKFREA- 166
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 167 -RLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIR-LKEIAEHQLEEALETLKNEREQ 244
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQR 207
|
170
....*....|
gi 51039802 245 KNNLRKELSQ 254
Cdd:COG4717 208 LAELEEELEE 217
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
48-390 |
2.16e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.10 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 48 LKQQYDELE---AEYDSLKQELEQlkeAFGQSfsiHRKVAEDGETREETLLQESASKEAYYLgKILEMQNELKQSRAVVT 124
Cdd:pfam03528 6 LQQRVAELEkenAEFYRLKQQLEA---EFNQK---RAKFKELYLAKEEDLKRQNAVLQEAQV-ELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 125 NVQA-----ENERLTAVVQDLKENNEMVELQRIRMKDEIREY----------------KFRE------ARLLQDYTELEE 177
Cdd:pfam03528 79 NIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKETVREYevqfhrrleqeraqwnQYREsaereiADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 178 EnitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDA-IRLKEIAEHQLEEaletLKNEREQKNNLRKELSQYI 256
Cdd:pfam03528 159 E----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAeDKIKELEASKMKE----LNHYLEAEKSCRTDLEMYV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 257 SLNDNHISIsvdglkFAEDGsepnndDKMNGHIHGPLVKLNGDYRTPTLRKgESLNPVSDLFSE---LNISEIQKLK--- 330
Cdd:pfam03528 231 AVLNTQKSV------LQEDA------EKLRKELHEVCHLLEQERQQHNQLK-HTWQKANDQFLEsqrLLMRDMQRMEsvl 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51039802 331 --QQLMQVEREKaillANLQESQTQLEHTKGALTEQHERVHRLTEH-VNAMRGLQSSKELKAE 390
Cdd:pfam03528 298 tsEQLRQVEEIK----KKDQEEHKRARTHKEKETLKSDREHTVSIHaVFSPAGVETSAPLSNV 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-234 |
2.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 102 EAYYLG-----KILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEmvELQRIRMKDE----IREYKFREARLLQDY 172
Cdd:COG4913 600 SRYVLGfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWdeidVASAEREIAELEAEL 677
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51039802 173 TELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEA 234
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-253 |
2.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 13 YKTEIERLTKELTETTHEKIQAAEY---GLVVLEEKLTLKQQYDELEAEYDSL---KQELEQLKEAFGQSFSIHRKVAED 86
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLretIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 87 GETREETLLQE----SASKEAYYL------GKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEmvelqrirmkd 156
Cdd:PRK02224 291 LEEERDDLLAEagldDADAEAVEArreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE----------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 157 EIREykfrEARllqdytELEEEnitLQKLVSTLKQNQVEYEGLKHEIKRFEEetvllnsQLEDAIRLKEIAEHQLEEALE 236
Cdd:PRK02224 360 ELRE----EAA------ELESE---LEEAREAVEDRREEIEELEEEIEELRE-------RFGDAPVDLGNAEDFLEELRE 419
|
250
....*....|....*..
gi 51039802 237 TLKNEREQKNNLRKELS 253
Cdd:PRK02224 420 ERDELREREAELEATLR 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-261 |
2.97e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 13 YKTEIERLTKELTETThEKIQAAEYGLVVLEEKLtLKQQYDELEAEYDSLKqelEQLKEAFGQSFSIHRKVaEDGETREE 92
Cdd:TIGR02169 756 VKSELKELEARIEELE-EDLHKLEEALNDLEARL-SHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL-NRLTLEKE 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 93 TLLQESASKEAYYL---GKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLL 169
Cdd:TIGR02169 830 YLEKEIQELQEQRIdlkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 170 QDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNS------QLEDAIR------LKEIAEHQ------- 230
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEEIRalepvnMLAIQEYEevlkrld 989
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 51039802 231 -LEEALETLKNER-------EQKNNLRKE--LSQYISLNDN 261
Cdd:TIGR02169 990 eLKEKRAKLEEERkaileriEEYEKKKREvfMEAFEAINEN 1030
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-225 |
3.66e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELtetthEKIQAAEYGLVVLEEKLtlkqqyDELEAEYDSLKQELEQLkeAFGQSFSIHRKV 83
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKEL-----EKLEELKKKLAELEKKL------DELEEELAELLKELEEL--GFESVEELEERL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 84 AEDGETREETLLQESASKEAYYLGKILE-MQNELKQSRAVVTNVQAENERLTavvqdlkenNEMVELQRIRMKDEIREYK 162
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKkLEEELDKAFEELAETEKRLEELR---------KELEELEKKYSEEEYEELR 665
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51039802 163 FREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKE 225
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE 728
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
50-469 |
4.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 50 QQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEdGETREETLLQESASKEAyyLGKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 130 NERLTAVVQDLKEnnemVELQRIRMKDEIREYKFREARLLQDYTELEEENI-----TLQKLVSTLKQNQVEYEGLKHEIK 204
Cdd:COG4717 148 LEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELqdlaeELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 205 RFEEETVLLNSQLEDAIRLKEIAEHQ----LEEALETLKNEREQKNNLRKELSQYISLNdnhISISVDGLKFAEDGSEPN 280
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGVLFLV---LGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 281 NDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPVSDLFSELNISEIQKLKQQLMQVER-EKAILLANLQESQTQLEHTKG 359
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 360 ALTE--------QHERVHRLTEHVNAMRG--LQSSKELKAELDGEKGRDSGEEAHDYEVDingLEILECKYRVAVTEVID 429
Cdd:COG4717 381 VEDEeelraaleQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEE---LEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 51039802 430 LKAEIKALKEkyNKSVENYTDEKAKYESKIQMYDEQVTSL 469
Cdd:COG4717 458 LEAELEQLEE--DGELAELLQELEELKAELRELAEEWAAL 495
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1-250 |
5.36e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 1 MAAEEVLQTVDHYKTEIERLTKELTETTHEK----IQAAEYGLVVLEEKLT-LKQQYDELEAEYDSLKQELEQLkEAFGq 75
Cdd:PRK05771 53 TKLSEALDKLRSYLPKLNPLREEKKKVSVKSleelIKDVEEELEKIEKEIKeLEEEISELENEIKELEQEIERL-EPWG- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 76 SFSIhrkvaedgetrEETLLQESASKEAYyLGKILEMQNELKQSRAVVTNVQAENE---RLTAVVQDLKENNEMVElqri 152
Cdd:PRK05771 131 NFDL-----------DLSLLLGFKYVSVF-VGTVPEDKLEELKLESDVENVEYISTdkgYVYVVVVVLKELSDEVE---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 153 rmkDEIREYKFREARLlqdyteleEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRlkeiaehQLE 232
Cdd:PRK05771 195 ---EELKKLGFERLEL--------EEEGTPSELIREIKE---ELEEIEKERESLLEELKELAKKYLEELL-------ALY 253
|
250
....*....|....*...
gi 51039802 233 EALETLKNEREQKNNLRK 250
Cdd:PRK05771 254 EYLEIELERAEALSKFLK 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-238 |
6.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 2 AAEEVLQTVDHYKTEIERLTKELTETThEKIQAAEYGLVVLEEkltLKQQYDELEAEYDSLKQELEQLKEAFGQsFSIHR 81
Cdd:COG4913 648 EALQRLAEYSWDEIDVASAEREIAELE-AELERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGR-LEKEL 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 82 KVAEDGETREETLLQESASKEA----YYLGKILEMQNELKQSRAVVTNVQAENERLTAvvqdlKENNEMVELQRIrMKDE 157
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARlelrALLEERFAAALGDAVERELRENLEERIDALRA-----RLNRAEEELERA-MRAF 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 158 IREYKFREARL---LQDYTELEEEnitLQKLVStlkQNQVEYEG-LKHEIKRFEEETVL-LNSQLEDAIRlkEIAE--HQ 230
Cdd:COG4913 797 NREWPAETADLdadLESLPEYLAL---LDRLEE---DGLPEYEErFKELLNENSIEFVAdLLSKLRRAIR--EIKEriDP 868
|
....*...
gi 51039802 231 LEEALETL 238
Cdd:COG4913 869 LNDSLKRI 876
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-807 |
7.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 633 RDQIKHLQKAVD--RSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLK 710
Cdd:COG4913 268 RERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 711 NKYENEKAMVTETMTKLRNELKALK----EDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNtllrmaiQQ 786
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-------RE 420
|
170 180
....*....|....*....|.
gi 51039802 787 KLALTQRLEDLEfdheqSRRS 807
Cdd:COG4913 421 LRELEAEIASLE-----RRKS 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-518 |
7.12e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 2 AAEEVLQTV---DHYKTEIERLTKELTETTHEKIQaaeyglvvleekltLKQQYDELEAEYDSLKQELEQLKEAFGQSFS 78
Cdd:TIGR02169 320 AEERLAKLEaeiDKLLAEIEELEREIEEERKRRDK--------------LTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 79 IH--RKVAEDGETREETLLQESASKEAYYL----GKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRI 152
Cdd:TIGR02169 386 ELkdYREKLEKLKREINELKRELDRLQEELqrlsEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 153 RMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYE--------------GLKHEIKRFEEETVLlnsQLE 218
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkasiqgvhGTVAQLGSVGERYAT---AIE 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 219 DAI--RLKEIA---EHQLEEALETLKNEREQK------NNLRKELSQY-ISLNDNHISISVDGLKFaEDGSEP------- 279
Cdd:TIGR02169 543 VAAgnRLNNVVvedDAVAKEAIELLKRRKAGRatflplNKMRDERRDLsILSEDGVIGFAVDLVEF-DPKYEPafkyvfg 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 280 -----NNDDKMNGHIHG-PLVKLNGDYRTPT--------LRKGESLNPVSD--------------------LFSELN--- 322
Cdd:TIGR02169 622 dtlvvEDIEAARRLMGKyRMVTLEGELFEKSgamtggsrAPRGGILFSRSEpaelqrlrerleglkrelssLQSELRrie 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 323 ----------------ISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGA----LTEQHERVHRLTEHVNAMRglQ 382
Cdd:TIGR02169 702 nrldelsqelsdasrkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseLKELEARIEELEEDLHKLE--E 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 383 SSKELKAELDGEKGRDSGEEAH--------------DYEVDINGL----EILECKYRVAVTEVIDLKAEIKALKEKY--- 441
Cdd:TIGR02169 780 ALNDLEARLSHSRIPEIQAELSkleeevsriearlrEIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIenl 859
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51039802 442 NKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQL 518
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
14-275 |
7.31e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 14 KTEIERLTKELT-ETTHEKIQAAEYGLVVLEEKLT----LKQQYDELEAEYDSLKQELEQlkeafgqSFSIHRKVAEDGE 88
Cdd:COG5022 858 KKRFSLLKKETIyLQSAQRVELAERQLQELKIDVKsissLKLVNLELESEIIELKKSLSS-------DLIENLEFKTELI 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 89 TREETLLQESASKEayylGKILEMQnelkqSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKfreaRL 168
Cdd:COG5022 931 ARLKKLLNNIDLEE----GPSIEYV-----KLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK----NF 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 169 LQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQ--LEDAIRLKEIAEHQLEEALETLKNEREQKN 246
Cdd:COG5022 998 KKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRENSL 1077
|
250 260
....*....|....*....|....*....
gi 51039802 247 NLRKELSQYISLNDNHISISVDGLKFAED 275
Cdd:COG5022 1078 LDDKQLYQLESTENLLKTINVKDLEVTNR 1106
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-271 |
7.33e-04 |
|
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: 43.47 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 48 LKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLlQESASKEAYYLGKILEMQNELKQsravvtnvq 127
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKE--------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 128 aENERLTAVVQDLKENNEmvELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEY----------- 196
Cdd:TIGR04523 536 -KESKISDLEDELNKDDF--ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLikeieekekki 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51039802 197 EGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYISLNDNHISISVDGLK 271
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLK 687
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-257 |
8.09e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 50 QQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLLQESAskeayylgKILEMQNELKQSRAVVTNVQAE 129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------RIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 130 NERLTAVVQDLKEN--NEMVELQRIRMKDEIR--------EYKFREARLLQDYTELEEENI-TLQKLVSTLKQNQVEYEG 198
Cdd:COG4942 92 IAELRAELEAQKEElaELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 51039802 199 LKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYIS 257
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-262 |
9.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 43 EEKL-TLKQQYDELEAEYDSLKQELEQLKEAfgqsfsihrkvaedgetreetllQESASKEAYYLGKILEMQNELKQSRA 121
Cdd:COG4913 609 RAKLaALEAELAELEEELAEAEERLEALEAE-----------------------LDALQERREALQRLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 122 VvtnvQAENERLTAVVQDLKENNemvelqrirmkDEIREYKFREARLLQDYTELEEENITLQKlvstlkqnqvEYEGLKH 201
Cdd:COG4913 666 A----EREIAELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKG----------EIGRLEK 720
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51039802 202 EIKRFEEETVLLNSQLEDAIRLKEIAEHQ-LEEALETL---KNEREQKNNLRKELSQYISLNDNH 262
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAAlgdAVERELRENLEERIDALRARLNRA 785
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-255 |
1.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 16 EIERLTKELTETTHEKIQAAEyglvvlEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLL 95
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKA------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 96 Q---------ESASKEAYYLGKILEMQNELKQSRavvTNVQAENERLTAVVQDLKENNEMVElqriRMKDEIREYKFREA 166
Cdd:PRK03918 578 EleelgfesvEELEERLKELEPFYNEYLELKDAE---KELEREEKELKKLEEELDKAFEELA----ETEKRLEELRKELE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 167 RLLQDYTELEEENItlqklvstlkqnQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEE------ALETLKN 240
Cdd:PRK03918 651 ELEKKYSEEEYEEL------------REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEErekakkELEKLEK 718
|
250
....*....|....*
gi 51039802 241 EREQKNNLRKELSQY 255
Cdd:PRK03918 719 ALERVEELREKVKKY 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-771 |
1.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 632 IRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVAL-ANLK 710
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLE 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51039802 711 NKYENE--KAMVTETMTKLRNELKALKEDAA-TFSSLRAMFATRCDEYVTQLDEMQRQLAAAED 771
Cdd:COG4913 753 ERFAAAlgDAVERELRENLEERIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPE 816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-496 |
1.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELT---------ETTHEKIQAAEYGLVVLE-EKLTLKQQYDELEAEYDSLKQELEQLKEAF 73
Cdd:PRK03918 203 EEVLREINEISSELPELREELEklekevkelEELKEEIEELEKELESLEgSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 74 GQSFSIHRKVAE----------------DGETREETLLQESASKEAYyLGKILEMQNELKQSRAVVTNVQAENERLTAVV 137
Cdd:PRK03918 283 KELKELKEKAEEyiklsefyeeyldelrEIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKELEKRLEELEERH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 138 QDLKENNE-MVELQRIR----------MKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLK------ 200
Cdd:PRK03918 362 ELYEEAKAkKEELERLKkrltgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 201 -HEIKRFEEETVLLNSQLEDAIRLKEIAEhqLEEALETLKNEREQKNNLRKELSQYISLNDnhisiSVDGLKFAEDgsep 279
Cdd:PRK03918 442 gRELTEEHRKELLEEYTAELKRIEKELKE--IEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEE---- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 280 nnddKMNGHIHGPLVKLNGDYRTPTLRKGESLNPVSDLFSELN-----ISEIQKLKQQLMQVEREKAILLANLQE----S 350
Cdd:PRK03918 511 ----KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleelKKKLAELEKKLDELEEELAELLKELEElgfeS 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 351 QTQLEHTKGALTEQHERVHRLtehvnamrgLQSSKELKAELdgEKGRDSGEEAHDYEVDINGLEileckyrvavTEVIDL 430
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLEL---------KDAEKELEREE--KELKKLEEELDKAFEELAETE----------KRLEEL 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51039802 431 KAEIKALKEKYN-KSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANE 496
Cdd:PRK03918 646 RKELEELEKKYSeEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
17-220 |
2.07e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 17 IERLTKELTETTHEKIQAAEYG--LVVLEEKL-TLK---QQYDELEAEYDSLKQELEQLKE-AFGQSFSIHRKVAEDGET 89
Cdd:COG3096 895 LEELREELDAAQEAQAFIQQHGkaLAQLEPLVaVLQsdpEQFEQLQADYLQAKEQQRRLKQqIFALSEVVQRRPHFSYED 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 90 REETLLQESASKEAYYlGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKEN----NEMV-ELQRiRMKD-EIREYKF 163
Cdd:COG3096 975 AVGLLGENSDLNEKLR-ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSrdakQQTLqELEQ-ELEElGVQADAE 1052
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51039802 164 REARLLQDYTELEEE-NITLQKLVSTLKQNQV---EYEGLKHEIKRFEEETVLLNSQLEDA 220
Cdd:COG3096 1053 AEERARIRRDELHEElSQNRSRRSQLEKQLTRceaEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
632-826 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 632 IRDQIKHLQKAVDRSLQlsRQRAAARELApMIDKDKEALMEEILKLKSLLSTKREQIAT-LRAVLKANKQTAEVALANLK 710
Cdd:COG4942 53 LLKQLAALERRIAALAR--RIRALEQELA-ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 711 NKYENEK--AMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQ---LAAAEDEKKTLNTLLRmaiQ 785
Cdd:COG4942 130 DFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraaLEALKAERQKLLARLE---K 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 51039802 786 QKLALTQRLEDLEFDHEQSRRSKGKLGKSKIGSPKVSGEAS 826
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-492 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 325 EIQKLKQQLMQVEREkailLANLQESQTQLEhtkgalTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAH 404
Cdd:COG4942 70 RIRALEQELAALEAE----LAELEKEIAELR------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 405 DYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHME 484
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
....*...
gi 51039802 485 KELQKMTS 492
Cdd:COG4942 220 QEAEELEA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-254 |
2.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 47 TLKQQYDELEAEYDSLKQELEQLKEAFGQSfsiHRKVAE--------DGETREETLLQESASKEAyylgKILEMQNELKQ 118
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA---EAALEEfrqknglvDLSEEAKLLLQQLSELES----QLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 119 SRAVVTNVQAENERLTAVVQDLKENNEMVELqrirmKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNqveyeg 198
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 51039802 199 LKHEIKRfeeetvlLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG3206 307 LQQEAQR-------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
668-806 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 668 EALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEvALANLKNKYENEK--AMVTETMTKLRNELKALKEDAAtfsslr 745
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIdvASAEREIAELEAELERLDASSD------ 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51039802 746 amfatrcdeyvtQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRR 806
Cdd:COG4913 686 ------------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-203 |
2.69e-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: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELtetthEKIQAAEYGLVvlEEKLTLKQQYDELEAEYDSLKQELEQLKEafgqSFSIHRKV 83
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEEL-----EELEAALRDLE--SRLGDLKKERDELEAQLRELERKIEELEA----QIEKKRKR 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 84 AEDGETREETLLQESASkeayyLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNemvelqrirMKdEIREYKF 163
Cdd:TIGR02169 919 LSELKAKLEALEEELSE-----IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVN---------ML-AIQEYEE 983
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 51039802 164 REARLLqdytELEEENITLQKLVSTLKQNQVEYEGLKHEI 203
Cdd:TIGR02169 984 VLKRLD----ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
111-779 |
2.71e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 111 EMQNELKQSRAVVTNVQAENERLTavvQDLKENNEMVelqrIRMKDEIREykfrearLLQDYTELEEENITLQKLVSTLK 190
Cdd:TIGR01612 541 EIEAGLKESYELAKNWKKLIHEIK---KELEEENEDS----IHLEKEIKD-------LFDKYLEIDDEIIYINKLKLELK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 191 Q------NQVEYEGLKHEIKRFEEETvllNSQLEDairLKEIAEHQLEEALE-------TLKNEREQ-----KNNLRKEL 252
Cdd:TIGR01612 607 EkiknisDKNEYIKKAIDLKKIIENN---NAYIDE---LAKISPYQVPEHLKnkdkiysTIKSELSKiyeddIDALYNEL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 253 SQYISLNDnhISISVDGLKFAEDGSEPNNDDKMNGHIHGPLVKLNgdYRTPTLRKGESLNPVSDL----FSELNiSEIQK 328
Cdd:TIGR01612 681 SSIVKENA--IDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELH--LSNIENKKNELLDIIVEIkkhiHGEIN-KDLNK 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 329 LKQQLMQVEREKAILLANLQESQTQLEHTKGALTEqhervhrLTEHVNAMRGLQSSKELKAELDGEKGRD-----SGEEA 403
Cdd:TIGR01612 756 ILEDFKNKEKELSNKINDYAKEKDELNKYKSKISE-------IKNHYNDQINIDNIKDEDAKQNYDKSKEyiktiSIKED 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 404 HDYEVdINGLEILECKYRVAVTEVIDLK--------AEIKALKEKYNKSVENYTDEK-AKYESKIQ----MYDEQVTSLE 470
Cdd:TIGR01612 829 EIFKI-INEMKFMKDDFLNKVDKFINFEnnckekidSEHEQFAELTNKIKAEISDDKlNDYEKKFNdsksLINEINKSIE 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 471 -------------------KTTKESGEKMAHMEKEL-----QKMTSIANEN---HSTLNTAQDELVTFSEELAQLYHHVC 523
Cdd:TIGR01612 908 eeyqnintlkkvdeyikicENTKESIEKFHNKQNILkeilnKNIDTIKESNlieKSYKDKFDNTLIDKINELDKAFKDAS 987
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 524 LCNNETPNRVMLDYYRQSRvTRSGSLKGpddprGLLSPRLArrgvsspvETRTSSEPVAKESTEASKEPSP------TKT 597
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLK-ANLGKNKE-----NMLYHQFD--------EKEKATNDIEQKIEDANKNIPNieiaihTSI 1053
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 598 PTISPVITAPPSSPV--LDTSDIRKEPMNIYNLNAiIRDQIKHL-------QKAVDRSLQLSRQRAAARELAPMIDKDKE 668
Cdd:TIGR01612 1054 YNIIDEIEKEIGKNIelLNKEILEEAEINITNFNE-IKEKLKHYnfddfgkEENIKYADEINKIKDDIKNLDQKIDHHIK 1132
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 669 ALMEEILKLKSLLSTKREQIATL-----RAVLKANKQTAEVALANLKNKYENEKaMVTETMTKLRNELKALKEDAATF-- 741
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLedvadKAISNDDPEEIEKKIENIVTKIDKKK-NIYDEIKKLLNEIAEIEKDKTSLee 1211
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51039802 742 ---------SSLRAMFATRCDE--------------YVTQLDEMQRQLAAAEDE-------KKTLNTL 779
Cdd:TIGR01612 1212 vkginlsygKNLGKLFLEKIDEekkksehmikameaYIEDLDEIKEKSPEIENEmgiemdiKAEMETF 1279
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9-252 |
2.94e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 9 TVDHYKTEIERLTKELT--ETTHEKiqaaeyglvvLEEKLTLKQQYDELEAEYDSLKQEleqlKEAFGQSFSIHRKVAED 86
Cdd:PRK02224 469 TIEEDRERVEELEAELEdlEEEVEE----------VEERLERAEDLVEAEDRIERLEER----REDLEELIAERRETIEE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 87 GETREETLLQESASKEAyylgkilEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVE-LQRIR-MKDEIREYKFR 164
Cdd:PRK02224 535 KRERAEELRERAAELEA-------EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEsLERIRtLLAAIADAEDE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 165 EARL---LQDYTELEEE--------NITLQKLVSTLKQNQVEyeGLKHEIKRFEEETVllnsQLEDAIRLKEIAEHQLEE 233
Cdd:PRK02224 608 IERLrekREALAELNDErrerlaekRERKRELEAEFDEARIE--EAREDKERAEEYLE----QVEEKLDELREERDDLQA 681
|
250
....*....|....*....
gi 51039802 234 ALETLKNEREQKNNLRKEL 252
Cdd:PRK02224 682 EIGAVENELEELEELRERR 700
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
105-440 |
3.08e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 105 YLGKILEMQNELKQSRAVVTNVQAE-NERLTAVVQDLKENNEMVELQRIRMKDEIR-EYKFREARLLQDYTELEEENITL 182
Cdd:COG5022 815 YLACIIKLQKTIKREKKLRETEEVEfSLKAEVLIQKFGRSLKAKKRFSLLKKETIYlQSAQRVELAERQLQELKIDVKSI 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 183 QKLvsTLKQNQVEYEGLkhEIKRFEEETVLLNSQledaIRLKEIAEhqleeaLETLKNEREQKNNLRKELSQYislndnh 262
Cdd:COG5022 895 SSL--KLVNLELESEII--ELKKSLSSDLIENLE----FKTELIAR------LKKLLNNIDLEEGPSIEYVKL------- 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 263 isisvdglkfaedgSEPNNDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPvsdlfselnISEIQKLKQQLmqveREKAI 342
Cdd:COG5022 954 --------------PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA---------NSELKNFKKEL----AELSK 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 343 LLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSKELKAELDgEKGRDSGEEAHDYEVDI-NGLEILECKYR 421
Cdd:COG5022 1007 QYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLL-LENNQLQARYKALKLRReNSLLDDKQLYQ 1085
|
330
....*....|....*....
gi 51039802 422 VAVTEVIDLKAEIKALKEK 440
Cdd:COG5022 1086 LESTENLLKTINVKDLEVT 1104
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-256 |
4.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 104 YYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIR----EYKFREARLLQDYTELEEEN 179
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51039802 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 |
4.64e-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: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 41 VLEEKltlkqqydELEAEYDSLKQELEQLKEAfgqsfsihRKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSR 120
Cdd:COG4913 217 MLEEP--------DTFEAADALVEHFDDLERA--------HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 121 AVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDY--------TELEEENITLQKLVSTLKQN 192
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 193 QVEYEGL--------KHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQ 254
Cdd:COG4913 361 RARLEALlaalglplPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-227 |
4.68e-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: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 2 AAEEVLQTVDHYK--TEIERLTKELTETThekiqaaeyglvvlEEKLTLKQQYDELEAEYDSLKQELEQLKEAfgqsfsi 79
Cdd:COG4913 273 ELEYLRAALRLWFaqRRLELLEAELEELR--------------AELARLEAELERLEARLDALREELDELEAQ------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 80 hrkVAEDGETREETLLQESASKEAyylgkilemqnELKQSRAVVTNVQaenERLTAVVQDLKENNEMVELQRIRMKDEIR 159
Cdd:COG4913 332 ---IRGNGGDRLEQLEREIERLER-----------ELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51039802 160 EYKFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIA 227
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA---EIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
13-496 |
5.02e-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: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 13 YKTEIERLTKELTeTTHEKIQAAEYGLVVLEEKltlKQQYDELEAEYDSLKQELEQLKEAFGQ-SFSIHRKVAEDGETRE 91
Cdd:TIGR04523 178 LEKEKLNIQKNID-KIKNKLLKLELLLSNLKKK---IQKNKSLESQISELKKQNNQLKDNIEKkQQEINEKTTEISNTQT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 92 EtlLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLkeNNEMVELQRIRMKDEIREykfREARLLQD 171
Cdd:TIGR04523 254 Q--LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL--NNQKEQDWNKELKSELKN---QEKKLEEI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 172 YTELEEENITLQKLVSTLKQnqveyegLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKE 251
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQ-------LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 252 LSQYISLNDNhISISVDGLKfaedgSEPNNDDKMNGHIHGPLVKLNGdyrtpTLRKGESLNPVSDL-FSELNISeIQKLK 330
Cdd:TIGR04523 400 IQNQEKLNQQ-KDEQIKKLQ-----QEKELLEKEIERLKETIIKNNS-----EIKDLTNQDSVKELiIKNLDNT-RESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 331 QQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSKELKAE-LDGEKGRDSgEEAHDYEVD 409
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEkLESEKKEKE-SKISDLEDE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 410 INGLEiLECKYRVAVTEVIDLKAEIKALKEKYNKS----------VENYTDEKAKYESKIQMYDEQVTSLEK---TTKES 476
Cdd:TIGR04523 547 LNKDD-FELKKENLEKEIDEKNKEIEELKQTQKSLkkkqeekqelIDQKEKEKKDLIKEIEEKEKKISSLEKeleKAKKE 625
|
490 500
....*....|....*....|
gi 51039802 477 GEKMAHMEKELQKMTSIANE 496
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQ 645
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
4-244 |
5.44e-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: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 4 EEVLQTVDHYKTEIERLTKELTETTHEKIQAAE------------YGLVVLEEKLTLKQQYDELEAEYDSLKQEleqlkE 71
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeqlqllnklLPQANLLADETLADRLEELREELDAAQEA-----Q 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 72 AFGQSfsiHRKVAEDGETREETLLQESASKEayylgkilEMQNELKQSRAVVTNVQAENERLTAVVQD------------ 139
Cdd:COG3096 910 AFIQQ---HGKALAQLEPLVAVLQSDPEQFE--------QLQADYLQAKEQQRRLKQQIFALSEVVQRrphfsyedavgl 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 140 LKENNEMVElqRIRMKDEIREYKFREAR--LLQDYTELEEENITLQKLVSTLkqnQVEYEGLKHEIKRFEEETVLLNSQL 217
Cdd:COG3096 979 LGENSDLNE--KLRARLEQAEEARREAReqLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEELGVQADAEA 1053
|
250 260
....*....|....*....|....*..
gi 51039802 218 EDAIRlkeIAEHQLEEALETLKNEREQ 244
Cdd:COG3096 1054 EERAR---IRRDELHEELSQNRSRRSQ 1077
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
14-513 |
6.26e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 14 KTEIERLTKELT---ETTHEKIQAAEYGLVVLEEKLTlkqqyDELEAEYDSLKQELEQLKEAFGQSfsihrKVAEDGET- 89
Cdd:pfam12128 389 NRDIAGIKDKLAkirEARDRQLAVAEDDLQALESELR-----EQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATa 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 90 REETLLQESASKEAyylgkILEMQNELKQSRAVVTNVQAE-----------NERL---TAVVQDLKENNEMVELQRIRMK 155
Cdd:pfam12128 459 TPELLLQLENFDER-----IERAREEQEAANAEVERLQSElrqarkrrdqaSEALrqaSRRLEERQSALDELELQLFPQA 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 156 DEIREYKFREARLLQDYTE--LEEENITLQKLVSTLKQNQVEYE----GLKHEIKRFEEETVLlnsQLEDAIRLKeiaeh 229
Cdd:pfam12128 534 GTLLHFLRKEAPDWEQSIGkvISPELLHRTDLDPEVWDGSVGGElnlyGVKLDLKRIDVPEWA---ASEEELRER----- 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 230 qLEEALETLKNEREQKNNLRKELSQyislndnhISISVD----GLKFAEDGSEPNNDDkmnghihgpLVKLNGDYRTPTL 305
Cdd:pfam12128 606 -LDKAEEALQSAREKQAAAEEQLVQ--------ANGELEkasrEETFARTALKNARLD---------LRRLFDEKQSEKD 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 306 RKGESLNpvsdlfselniSEIQKLKQQLMQVEREKAillANLQESQTQLEHTKGALTEqhervHRlTEHVNAMRGLQSSK 385
Cdd:pfam12128 668 KKNKALA-----------ERKDSANERLNSLEAQLK---QLDKKHQAWLEEQKEQKRE-----AR-TEKQAYWQVVEGAL 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 386 ELK-AELDGEK-GRDSGEEAH------DYEVDINGLEILECKyrvavteVIDLKAEIKAL-------------------- 437
Cdd:pfam12128 728 DAQlALLKAAIaARRSGAKAElkaletWYKRDLASLGVDPDV-------IAKLKREIRTLerkieriavrrqevlryfdw 800
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51039802 438 -KEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSE 513
Cdd:pfam12128 801 yQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
14-460 |
6.32e-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: 40.39 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 14 KTEIERLTKELTETTHEKIQAAEYglvvLEEKL----TLKQQYDELEAEYDSLKQELEQLKEAFGQSfsIHRKVAEDGET 89
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQ----LSEKQkeleQNNKKIKELEKQLNQLKSEISDLNNQKEQD--WNKELKSELKN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 90 REETLlQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLL 169
Cdd:TIGR04523 319 QEKKL-EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 170 QDYTELEEENitlQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDairLKEiAEHQLEEALETLKNEREQKNNLR 249
Cdd:TIGR04523 398 SKIQNQEKLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD---LTN-QDSVKELIIKNLDNTRESLETQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 250 KELSQYISLNDNHISISVDGLKFAEDGSEPNNDDKMNghihgplvkLNGDYRTPTLRKGESLNPVSDLFSELNI------ 323
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE---------LEEKVKDLTKKISSLKEKIEKLESEKKEkeskis 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 324 ---SEIQKLKQQLMQVEREKAILlaNLQESQTQLEHTKGAL----TEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKG 396
Cdd:TIGR04523 542 dleDELNKDDFELKKENLEKEID--EKNKEIEELKQTQKSLkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51039802 397 RDSGEEAHDYEVDINGleiLECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKIQ 460
Cdd:TIGR04523 620 EKAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-251 |
8.07e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 16 EIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLK---QELEQLKEA-----FGQSF--SIHRKVAE 85
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAgkcpeCGQPVegSPHVETIE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 86 DGETREETLlqesaskeayylgkilemQNELKQSRAVVTNVQAENERLTAVV------QDLKENNEMVELQRIRMKDEIR 159
Cdd:PRK02224 472 EDRERVEEL------------------EAELEDLEEEVEEVEERLERAEDLVeaedriERLEERREDLEELIAERRETIE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 160 EYKFREARLLQDYTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAE--HQLEEALET 237
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEE---EAEEAREEVAELNSKLAELKERIESLERIRTLLAaiADAEDEIER 610
|
250
....*....|....*..
gi 51039802 238 LKNEREQ---KNNLRKE 251
Cdd:PRK02224 611 LREKREAlaeLNDERRE 627
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
15-246 |
8.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 15 TEIERLTKELTETTHEKIQAaeyglvvLEEKLTLKQQYDELEAEYDSLKQELEQLKEafgqsfsihrkvaedgetREETL 94
Cdd:COG3883 16 PQIQAKQKELSELQAELEAA-------QAELDALQAELEELNEEYNELQAELEALQA------------------EIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 95 LQESASKEAyylgKILEMQNELKQsRAVVTNVQAENERLTAVV------QDLKENNEMVELQRIRMKDEIREYKfrearl 168
Cdd:COG3883 71 QAEIAEAEA----EIEERREELGE-RARALYRSGGSVSYLDVLlgsesfSDFLDRLSALSKIADADADLLEELK------ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51039802 169 lQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKN 246
Cdd:COG3883 140 -ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
633-796 |
8.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 633 RDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLST----------KREQIATLRAVLkanKQTA 702
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQL---QQEA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 703 EVALANLKNKYENEKAMVTEtmtkLRNELKALKEDAATFSSLRAmfatrcdeyvtQLDEMQRQLAAAEdekKTLNTLLRM 782
Cdd:COG3206 312 QRILASLEAELEALQAREAS----LQAQLAQLEARLAELPELEA-----------ELRRLEREVEVAR---ELYESLLQR 373
|
170
....*....|....
gi 51039802 783 AIQQKLALTQRLED 796
Cdd:COG3206 374 LEEARLAEALTVGN 387
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
106-158 |
8.83e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 36.78 E-value: 8.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 51039802 106 LGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVElQRIR------MKDEI 158
Cdd:COG2919 28 LLAYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIE-ERAReelgmvKPGET 85
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-243 |
9.28e-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: 40.05 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 16 EIERLTKELtETTHEKIQAAEYGLVVLEEKLT-LKQQYDELEAEYDSLKQELEQLKEAFGQSFsihrkvAEDGETREETL 94
Cdd:TIGR02169 724 EIEQLEQEE-EKLKERLEELEEDLSSLEQEIEnVKSELKELEARIEELEEDLHKLEEALNDLE------ARLSHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51039802 95 LQESASKEAYYL---GKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQD 171
Cdd:TIGR02169 797 QAELSKLEEEVSrieARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51039802 172 YTELEEENITLQKLVSTLKQnqvEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNERE 243
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| |
