|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
585-693 |
1.08e-30 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 116.49 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 585 QLSNSNGHISAHLVNKLSTELKRLEGELSASKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQMQSKL 664
Cdd:pfam12325 1 SVSTSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRY 80
|
90 100
....*....|....*....|....*....
gi 398365551 665 ETSLQLLGEKTEQVEELENDVSDLKEMMH 693
Cdd:pfam12325 81 ETTLELLGEKSEEVEELKADVEDLKEMYR 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-438 |
2.01e-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: 70.86 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 122 VEELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKL-IKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVK 200
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 201 DLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLET-LEKNIKEKDDLITILQQsldnmrtlL 279
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqLEELESKLDELAEELAE--------L 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 280 EKEKSEFQTEKKALQEatvdQVTTLETKLEQLRIELDSSTQNLDAKSNRdfVDDQQSYEEKQHASFQYNR-LKEQLESSK 358
Cdd:TIGR02168 343 EEKLEELKEELESLEA----ELEELEAELEELESRLEELEEQLETLRSK--VAQLELQIASLNNEIERLEaRLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 359 ANWDSIEYALNTKIVNLE-NRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQS 437
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
.
gi 398365551 438 I 438
Cdd:TIGR02168 497 L 497
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
158-231 |
1.26e-09 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 55.01 E-value: 1.26e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365551 158 SSFFKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQ 231
Cdd:pfam12329 1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-692 |
2.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 140 IDDLTNELNR------------------KSQIETTDSSFFKL-IKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVK 200
Cdd:COG1196 191 LEDILGELERqleplerqaekaeryrelKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 201 DLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLE 280
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 281 KEKSEFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLDAKSNrdfvdDQQSYEEKQHASFQYNRLKEQLESSKAN 360
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 361 WDSIEYALNTKIVNLENRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKsslqsisd 440
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-------- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 441 dynllkkkyEIQRSQLEQKENELKPHQENSNEKIIDKIPVELTD----------SLNSMEGNIEDEWTLPQENSMLSLSM 510
Cdd:COG1196 498 ---------EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaayeaaleaALAAALQNIVVEDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 511 SKLGELESDPSLKPIYNESHETICSEESQHFDRKNVDFSIDDIPEEAAALQAIREGESMNSLNNTSIPYRRASV------ 584
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLagrlre 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 585 -----QLSNSNGHISAHLVNKLSTELKRLEGELsasKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQ 659
Cdd:COG1196 649 vtlegEGGSAGGSLTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 398365551 660 MQSKLETSLQLLGEKTEQ------------------VEELENDVSDLKEMM 692
Cdd:COG1196 726 LEEQLEAEREELLEELLEeeelleeealeelpeppdLEELERELERLEREI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-460 |
1.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 121 TVEELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKLIKEKDDLIDQLRKegakLAETELRQSNQIKALRTKVK 200
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEEEINGIEERIK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 201 DLEYEVSELNDSSAQ-------------SVENYNELQSLYHNIQG--------QLAEATNKLKDADKQKESLETLEKNIK 259
Cdd:PRK03918 332 ELEEKEERLEELKKKlkelekrleeleeRHELYEEAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKIT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 260 EK-DDLITILQQSLDNM--------------RTLLEKEKSEFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLDA 324
Cdd:PRK03918 412 ARiGELKKEIKELKKAIeelkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 325 KS----NRDFVDDQQSYEEK---------QHASFQYNRLKEQLESSKANWDSIEYALNtKIVNLENRFESTMKEKNDIEE 391
Cdd:PRK03918 492 ESelikLKELAEQLKELEEKlkkynleelEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 392 KYQTALRSSETLGKQLEKEKENH--------------SKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLE 457
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERlkelepfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
...
gi 398365551 458 QKE 460
Cdd:PRK03918 651 ELE 653
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
246-690 |
1.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 246 KQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKEKS--EFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLd 323
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENieELIKEKEKELEEVLREINEISSELPELREELEKLEKEV- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 324 aksnrdfvddqQSYEEKQHASFQYNRLKEQLESSKAnwdsieyALNTKIVNLENRFESTMKEKNDIEEK----------- 392
Cdd:PRK03918 231 -----------KELEELKEEIEELEKELESLEGSKR-------KLEEKIRELEERIEELKKEIEELEEKvkelkelkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 393 ------------YQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLK---KKYEIQRSQLE 457
Cdd:PRK03918 293 eeyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 458 QKENELKPHQENSNEKIIDKI------PVELTDSLNSMEGNIEDewtLPQENSMLSLSMSKLGELESDPSL--KPIYNES 529
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELeelekaKEEIEEEISKITARIGE---LKKEIKELKKAIEELKKAKGKCPVcgRELTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 530 HETICSEesQHFDRKNVDFSIDDIPEEAAALQA-IREGESMNSLNNTSIPYRRASVQLSNsnghisahlvnkLSTELKRL 608
Cdd:PRK03918 450 RKELLEE--YTAELKRIEKELKEIEEKERKLRKeLRELEKVLKKESELIKLKELAEQLKE------------LEEKLKKY 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 609 EGE-LSASKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQMQSKLETSLQLLGEKT-EQVEELENDVS 686
Cdd:PRK03918 516 NLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
....
gi 398365551 687 DLKE 690
Cdd:PRK03918 596 ELEP 599
|
|
| ClyA_HblB-like |
cd22653 |
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model ... |
214-367 |
5.44e-03 |
|
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model includes Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL (HBL), and is a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). HBL is composed of three distinct protein components, B, L1, and L2, which together possess hemolytic, cytotoxic, dermonecrotic, and vascular permeability activities in B. cereus. Although all three HBL components can individually bind to the membrane, it requires the three components to form a complex to form a pore. Structure of HblB shows an elongated, almost entirely alpha-helical protein, except for a short hydrophobic beta-hairpin known as the beta-tongue. HBL from Bacillus toyonensis BV-17 (a strain isolated from feces samples of healthy donors) has antitumor activity both in vitro and in vivo and may have potential as a treatment for colon cancer. For B. toyonesis HBL, combining HBL-B and HBL-L2 had no cytotoxicity but combining HBL-B and HBL-L1 does.
Pssm-ID: 439151 [Multi-domain] Cd Length: 231 Bit Score: 39.11 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 214 AQSVENYNELQSLYHNiqgQLAEATNKlKDADKQKESLETLEKNIKEK----DDLITILQQsldnMRTLLEKEKSEFQTE 289
Cdd:cd22653 70 NQNIINYNTQFQNYYD---TLVDAIDK-KDKETLKEGLTDLYKDISENkkevDQLIKDLKK----FRDKLSTDTQNFKND 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 290 KKALQ----EATVDQVTTLETKLEQLRIELDS--------STQ--NLDAKSNrDFVDDQQSYEEKqhasfQYNRLKEQLE 355
Cdd:cd22653 142 VNQLTssgaQQEVAILTDAKNQTTNLTETIDQaitalqniSNQwdTMGAKYK-SLLDNIDNIDPE-----DLEFIKEDLN 215
|
170
....*....|...
gi 398365551 356 SSKANWDSI-EYA 367
Cdd:cd22653 216 TAKDSWQDLkEYA 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
585-693 |
1.08e-30 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 116.49 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 585 QLSNSNGHISAHLVNKLSTELKRLEGELSASKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQMQSKL 664
Cdd:pfam12325 1 SVSTSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRY 80
|
90 100
....*....|....*....|....*....
gi 398365551 665 ETSLQLLGEKTEQVEELENDVSDLKEMMH 693
Cdd:pfam12325 81 ETTLELLGEKSEEVEELKADVEDLKEMYR 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-438 |
2.01e-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: 70.86 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 122 VEELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKL-IKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVK 200
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 201 DLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLET-LEKNIKEKDDLITILQQsldnmrtlL 279
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqLEELESKLDELAEELAE--------L 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 280 EKEKSEFQTEKKALQEatvdQVTTLETKLEQLRIELDSSTQNLDAKSNRdfVDDQQSYEEKQHASFQYNR-LKEQLESSK 358
Cdd:TIGR02168 343 EEKLEELKEELESLEA----ELEELEAELEELESRLEELEEQLETLRSK--VAQLELQIASLNNEIERLEaRLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 359 ANWDSIEYALNTKIVNLE-NRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQS 437
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
.
gi 398365551 438 I 438
Cdd:TIGR02168 497 L 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-472 |
4.29e-10 |
|
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: 63.16 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 186 LRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKL----KDADKQKESLETLEKNIKEK 261
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 262 DDLITILQQSLDNmrtlLEKEKSEFQTEKKALQEAT-----------VDQVTTLETKLEQLRIELDSSTQNLDAKSNRDF 330
Cdd:TIGR02169 750 EQEIENVKSELKE----LEARIEELEEDLHKLEEALndlearlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 331 VDDQQSYEEKQHASFQYNRLKEQLESSKANWDSieyaLNTKIVNLENRFESTMKEKNDIEEKYqtalrssetlgKQLEKE 410
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRL-----------GDLKKE 890
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365551 411 KENHSKavlEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQKENELKPHQENSNE 472
Cdd:TIGR02169 891 RDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
158-231 |
1.26e-09 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 55.01 E-value: 1.26e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365551 158 SSFFKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQ 231
Cdd:pfam12329 1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-692 |
2.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 140 IDDLTNELNR------------------KSQIETTDSSFFKL-IKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVK 200
Cdd:COG1196 191 LEDILGELERqleplerqaekaeryrelKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 201 DLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLE 280
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 281 KEKSEFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLDAKSNrdfvdDQQSYEEKQHASFQYNRLKEQLESSKAN 360
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 361 WDSIEYALNTKIVNLENRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKsslqsisd 440
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-------- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 441 dynllkkkyEIQRSQLEQKENELKPHQENSNEKIIDKIPVELTD----------SLNSMEGNIEDEWTLPQENSMLSLSM 510
Cdd:COG1196 498 ---------EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaayeaaleaALAAALQNIVVEDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 511 SKLGELESDPSLKPIYNESHETICSEESQHFDRKNVDFSIDDIPEEAAALQAIREGESMNSLNNTSIPYRRASV------ 584
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLagrlre 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 585 -----QLSNSNGHISAHLVNKLSTELKRLEGELsasKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQ 659
Cdd:COG1196 649 vtlegEGGSAGGSLTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 398365551 660 MQSKLETSLQLLGEKTEQ------------------VEELENDVSDLKEMM 692
Cdd:COG1196 726 LEEQLEAEREELLEELLEeeelleeealeelpeppdLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-494 |
4.62e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 186 LRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLI 265
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 266 TILQQSLDNMRTLLEKEKSEFQTEKKALQEatvdQVTTLETKLEQLRIELDSSTQNLDAKSNrdfvddqqsyeekqhasf 345
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRA------------------ 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 346 QYNRLKEqlesskanwdsieyalntKIVNLENRFESTMKEKNDIEekyqtalRSSETLGKQLEKEKENHSKAVLEVKDLE 425
Cdd:TIGR02168 811 ELTLLNE------------------EAANLRERLESLERRIAATE-------RRLEDLEEQIEELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365551 426 RRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQKENELKPHQENSNEKIIDKIpvELTDSLNSMEGNIE 494
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQLELRLE 932
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-385 |
2.90e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 196 RTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQgQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNM 275
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 276 RTL---LEKEKSEFQTEKKALQEATvDQVTTLETKLEQLRIELDSSTQNLDAKSNRDFVDDQQSYEEK---QHASFQYNR 349
Cdd:COG4913 688 AALeeqLEELEAELEELEEELDELK-GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaaALGDAVERE 766
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365551 350 LKEQLESSKAnwdsieyALNTKIVNLENRFESTMKE 385
Cdd:COG4913 767 LRENLEERID-------ALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-433 |
1.46e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 123 EELVKEISPEYLRLNKQIDDLTNELNR-KSQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAETELrqsnQIKALRTKVKD 201
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----ELAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 202 LEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQ----KESLETLEKNIKEKDDLITILQQSLDNMRT 277
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaatERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 278 LLEKEKSEFqtekkalqEATVDQVTTLETKLEQLRIELDsstqnldaksnrDFVDDQQSYEEKQHASFQ-YNRLKEQLES 356
Cdd:TIGR02168 867 LIEELESEL--------EALLNERASLEEALALLRSELE------------ELSEELRELESKRSELRReLEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 357 SKANWDSIEYALNTKIVNLENRFESTM----KEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLK 432
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEYSLTLeeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
.
gi 398365551 433 S 433
Cdd:TIGR02168 1007 A 1007
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-459 |
3.33e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 252 ETLEKNIKEKDDLITILQQSLDNMRTLL---EKEKSEFQTEKKAL-----QEATVDQVTTLETKLEQLRIELDSSTQNLD 323
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELeeaEAALEEFRQKNGLVdlseeAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 324 AKSNRDFVDDQQSYEEKQHASFQ-----YNRLKEQLESSKANW--DSIEY-ALNTKIVNLENRFEstmKEKNDIEEKYQT 395
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQqlraqLAELEAELAELSARYtpNHPDViALRAQIAALRAQLQ---QEAQRILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365551 396 ALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQK 459
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-464 |
6.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 241 LKDADKQKESL----ETLEKNIKEKDDLITILQQSLDNMRTLLEKEKSEFQTEKKALQ---EATVDQVTTLETKLEQLRI 313
Cdd:TIGR02168 195 LNELERQLKSLerqaEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEeelEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 314 EldsstqnldaksnrdFVDDQQSYEEKQHASFQYNRLKEQLESSKANWDSIEYALNTKIVNLENRFESTMKEKNDIEEKY 393
Cdd:TIGR02168 275 E---------------VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365551 394 QTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQKENELK 464
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-335 |
1.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 135 RLNKQIDDLTNELNRKSQIettdssFFKLIKEKDDLIDQLRKEGAKLAETELRQS---NQIKALRTKVKDLEYEVSELnD 211
Cdd:COG4717 50 RLEKEADELFKPQGRKPEL------NLKELKELEEELKEAEEKEEEYAELQEELEeleEELEELEAELEELREELEKL-E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 212 SSAQSVENYNELQSLyhniQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDN-MRTLLEKEKSEFQTEK 290
Cdd:COG4717 123 KLLQLLPLYQELEAL----EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElLEQLSLATEEELQDLA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365551 291 KALQEATvDQVTTLETKLEQLRIELDSSTQNLDAKSNRDFVDDQQ 335
Cdd:COG4717 199 EELEELQ-QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-438 |
1.74e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 188 QSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQkesLETLEKNIKEkddliti 267
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAE------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 268 lqqsldnmrtlLEKEKSEFQTEKKALQEATVDQVTTLETKLEQLRIELdsstqNLDAKSNRDFVDDQQSYEekqhasfQY 347
Cdd:COG4942 88 -----------LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-----LLSPEDFLDAVRRLQYLK-------YL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 348 NR-LKEQLESSKANWDSIEyALNTKIVNLENRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKavlEVKDLER 426
Cdd:COG4942 145 APaRREQAEELRADLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQ 220
|
250
....*....|..
gi 398365551 427 RAETLKSSLQSI 438
Cdd:COG4942 221 EAEELEALIARL 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
166-324 |
2.19e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 166 EKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNK----- 240
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 241 -LKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKEKSEFQTEKKALQEATVDqvttLETKLEQLRIELDSST 319
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE----LEAELEELEAEREELA 169
|
....*
gi 398365551 320 QNLDA 324
Cdd:COG1579 170 AKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-359 |
2.62e-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: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 164 IKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKL-- 241
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 242 ----------------KDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKEKSEFQTEKKALQEAtvdqvttlE 305
Cdd:COG4942 116 lgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE--------R 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365551 306 TKLEQLRieldSSTQNLDAKSNRDFVDDQQSYEEKQHASFQYNRLKEQLESSKA 359
Cdd:COG4942 188 AALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-685 |
4.89e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 117 YTEFTVEELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALR 196
Cdd:COG1196 215 YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 197 TKVKDLEYEVSELNDSSAQSVENYNELQslyhniqgqlAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMR 276
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELE----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 277 TLLEKEKSEFQTEKKALQEATVDQVTTLETKLEQlrieldsstqnldaksnrdfvddQQSYEEKQHASFQYNRLKEQLES 356
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAEL-----------------------AAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 357 SKANWDSIEYALNTKIVNLENRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKsslq 436
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL---- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 437 sisddynllkkkyEIQRSQLEQKENELKPHQENSNEKIIDKIPVELTD----------SLNSMEGNIEDEWTLPQENSML 506
Cdd:COG1196 498 -------------EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaayeaaleaALAAALQNIVVEDDEVAAAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 507 SLSMSKLGELESDPSLKPIYNESHETICSEESQHFDRKNVDFSIDDIPEEAAALQAIREGESMNSLNNTSIPYRRASV-- 584
Cdd:COG1196 565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLag 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 585 ---------QLSNSNGHISAHLVNKLSTELKRLEGELsasKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLK 655
Cdd:COG1196 645 rlrevtlegEGGSAGGSLTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590
....*....|....*....|....*....|
gi 398365551 656 RVEQMQSKLETSLQLLGEKTEQVEELENDV 685
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEE 751
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-460 |
1.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 121 TVEELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKLIKEKDDLIDQLRKegakLAETELRQSNQIKALRTKVK 200
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEEEINGIEERIK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 201 DLEYEVSELNDSSAQ-------------SVENYNELQSLYHNIQG--------QLAEATNKLKDADKQKESLETLEKNIK 259
Cdd:PRK03918 332 ELEEKEERLEELKKKlkelekrleeleeRHELYEEAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKIT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 260 EK-DDLITILQQSLDNM--------------RTLLEKEKSEFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLDA 324
Cdd:PRK03918 412 ARiGELKKEIKELKKAIeelkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 325 KS----NRDFVDDQQSYEEK---------QHASFQYNRLKEQLESSKANWDSIEYALNtKIVNLENRFESTMKEKNDIEE 391
Cdd:PRK03918 492 ESelikLKELAEQLKELEEKlkkynleelEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 392 KYQTALRSSETLGKQLEKEKENH--------------SKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLE 457
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERlkelepfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
...
gi 398365551 458 QKE 460
Cdd:PRK03918 651 ELE 653
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
171-474 |
3.70e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 171 IDQLRKEGAKLAEtelrqsnqikALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNiqgqlaeatnklkdadkqkES 250
Cdd:PLN03229 413 VDPERKVNMKKRE----------AVKTPVRELEGEVEKLKEQILKAKESSSKPSELALN-------------------EM 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 251 LETLEKNIKEK--DDLITI-LQQSLDNMRTLLEKEKSEFQTEKKALQE-------------ATVDQVTTLETKLEQLR-- 312
Cdd:PLN03229 464 IEKLKKEIDLEytEAVIAMgLQERLENLREEFSKANSQDQLMHPVLMEkieklkdefnkrlSRAPNYLSLKYKLDMLNef 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 313 ------IELDSSTQNLDAKSNRDF--VDDQQSYEEKQHAsfqynrLKEQLESSKA-NWDSIEYALNTKIVNLENRFESTM 383
Cdd:PLN03229 544 srakalSEKKSKAEKLKAEINKKFkeVMDRPEIKEKMEA------LKAEVASSGAsSGDELDDDLKEKVEKMKKEIELEL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 384 ----------------KEKNDIEEKYQTALRSS-ETLGKQLEKEKENhskaVLEVKDLERRAETLKSSLQSISDDYNL-L 445
Cdd:PLN03229 618 agvlksmglevigvtkKNKDTAEQTPPPNLQEKiESLNEEINKKIER----VIRSSDLKSKIELLKLEVAKASKTPDVtE 693
|
330 340 350
....*....|....*....|....*....|....*
gi 398365551 446 KKKYEIQRSQLEQK------ENELKPHQENSNEKI 474
Cdd:PLN03229 694 KEKIEALEQQIKQKiaealnSSELKEKFEELEAEL 728
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
173-364 |
3.77e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 173 QLRKEGAKLAETELRQsnQIKALRTKVKDLEYEVSE---------LNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKD 243
Cdd:COG3206 167 ELRREEARKALEFLEE--QLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 244 ADKQKESLETLEKNIKEkDDLITILQQSLDNMRTLLEKEKSEFQTEKKALQEATvDQVTTLETKLEQL--RIELDSSTQN 321
Cdd:COG3206 245 LRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALR-AQIAALRAQLQQEaqRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365551 322 LDAKSNRDFVDDQQSYEEKQHASF-----QYNRLKEQLESSKANWDSI 364
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELpeleaELRRLEREVEVARELYESL 370
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
136-352 |
9.63e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 136 LNKQIDDLTNELNR-KSQIETTDSSFFKL-------IKEKDDLIDQLRKEgAKLAETELRQ-SNQIKALRTKVKDLEYEV 206
Cdd:PHA02562 179 LNQQIQTLDMKIDHiQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEE-AKTIKAEIEElTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 207 SELNDSSAQ---SVENYNELQSLYHN-------------IQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQ 270
Cdd:PHA02562 258 NKLNTAAAKiksKIEQFQKVIKMYEKggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 271 SLDNMRTLLEKEKSEFQTE-------KKALQEATvDQVTTLETKLEQLRieldsstQNLDAKSNrdfvDDQQSYEEKQHA 343
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLvdkakkvKAAIEELQ-AEFVDNAEELAKLQ-------DELDKIVK----TKSELVKEKYHR 405
|
....*....
gi 398365551 344 SFQYNRLKE 352
Cdd:PHA02562 406 GIVTDLLKD 414
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
136-305 |
1.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 136 LNKQIDDLTNELNRKSQIETTDSsffklikekddlidqlRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQ 215
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHE----------------ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 216 SVENYNELQSlyhniqgQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKEKSEFQTEKKALQE 295
Cdd:COG2433 446 LERELSEARS-------EERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEK 518
|
170
....*....|
gi 398365551 296 ATVDQVTTLE 305
Cdd:COG2433 519 FTKEAIRRLE 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
246-690 |
1.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 246 KQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKEKS--EFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLd 323
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENieELIKEKEKELEEVLREINEISSELPELREELEKLEKEV- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 324 aksnrdfvddqQSYEEKQHASFQYNRLKEQLESSKAnwdsieyALNTKIVNLENRFESTMKEKNDIEEK----------- 392
Cdd:PRK03918 231 -----------KELEELKEEIEELEKELESLEGSKR-------KLEEKIRELEERIEELKKEIEELEEKvkelkelkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 393 ------------YQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLK---KKYEIQRSQLE 457
Cdd:PRK03918 293 eeyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 458 QKENELKPHQENSNEKIIDKI------PVELTDSLNSMEGNIEDewtLPQENSMLSLSMSKLGELESDPSL--KPIYNES 529
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELeelekaKEEIEEEISKITARIGE---LKKEIKELKKAIEELKKAKGKCPVcgRELTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 530 HETICSEesQHFDRKNVDFSIDDIPEEAAALQA-IREGESMNSLNNTSIPYRRASVQLSNsnghisahlvnkLSTELKRL 608
Cdd:PRK03918 450 RKELLEE--YTAELKRIEKELKEIEEKERKLRKeLRELEKVLKKESELIKLKELAEQLKE------------LEEKLKKY 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 609 EGE-LSASKELYDNLLKEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQMQSKLETSLQLLGEKT-EQVEELENDVS 686
Cdd:PRK03918 516 NLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
....
gi 398365551 687 DLKE 690
Cdd:PRK03918 596 ELEP 599
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
123-349 |
1.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 123 EELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAEtelrqsnQIKALRTKVKDL 202
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 203 EYEVSELNDsSAQSVENYNELQSLYHniQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKE 282
Cdd:COG4942 103 KEELAELLR-ALYRLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365551 283 KSEFQTEKKALQEATVDQ---VTTLETKLEQLRIELD---SSTQNLDAKSNRDFVDDQQSYEEKQHASFQYNR 349
Cdd:COG4942 180 LAELEEERAALEALKAERqklLARLEKELAELAAELAelqQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
213-468 |
2.65e-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: 41.36 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 213 SAQSVENYNELQSLYHNIQGQLAEATnKLKDADKQKESLE----TLEKNIKEKDDLITILQQsldnmrtllekeksEFQT 288
Cdd:pfam12128 219 NRQQVEHWIRDIQAIAGIMKIRPEFT-KLQQEFNTLESAElrlsHLHFGYKSDETLIASRQE--------------ERQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 289 EKKALQEatvdQVTTLETKLEQLRIEL--DSSTQNLDAKSNRDFVDdqqsYEEKQHASFQYNRLkEQLESSKANWDSIEY 366
Cdd:pfam12128 284 TSAELNQ----LLRTLDDQWKEKRDELngELSAADAAVAKDRSELE----ALEDQHGAFLDADI-ETAAADQEQLPSWQS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 367 ALNtkivNLENRFESTMKEKNDIEEKYQTAlrssetlgKQLEKEKENHSKAVLEvKDLERRAETLKSSLQSISDDYNLLK 446
Cdd:pfam12128 355 ELE----NLEERLKALTGKHQDVTAKYNRR--------RSKIKEQNNRDIAGIK-DKLAKIREARDRQLAVAEDDLQALE 421
|
250 260
....*....|....*....|..
gi 398365551 447 KKYeiqRSQLEQKENELKPHQE 468
Cdd:pfam12128 422 SEL---REQLEAGKLEFNEEEY 440
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
236-463 |
3.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 236 EATNKLKDADkqkESLETLEknikekdDLITILQQSLDNmrtlLEKEKS------EFQTEKKALQ-EATVDQVTTLETKL 308
Cdd:COG1196 176 EAERKLEATE---ENLERLE-------DILGELERQLEP----LERQAEkaeryrELKEELKELEaELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 309 EQLRIELDSstqnLDAKSNRDFVDDQQSYEEKQHASFQYNRLKEQLESSKANwdsiEYALNTKIVNLENRFESTMKEKND 388
Cdd:COG1196 242 EELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365551 389 IEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQKENEL 463
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
262-474 |
3.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 262 DDLITILQQSLDNmrtlLEKEKSEFQTEKKALQEatvdQVTTLETKLEQLRIELDSSTQNLDAKsNRDFVDDQQSYEEKQ 341
Cdd:COG3883 15 DPQIQAKQKELSE----LQAELEAAQAELDALQA----ELEELNEEYNELQAELEALQAEIDKL-QAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 342 hasfqyNRLKEQLESSKANWDSIEYA---LNTK-IVNLENRFESTmkekNDIEEKYQTALRSSETLGKQLEKEKENHSKA 417
Cdd:COG3883 86 ------EELGERARALYRSGGSVSYLdvlLGSEsFSDFLDRLSAL----SKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365551 418 VLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQKENELKPHQENSNEKI 474
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-691 |
3.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 136 LNKQIDDLTNELNRKSQIEttdssffKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEY---EVSELNDS 212
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIE-------ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 213 SAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLlEKEKSEFQTEKKA 292
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI-EKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 293 LQ------EATVDQVTTLETKLEQLRIELDSSTQNLDAKSNRDFVDDQQSYEEKQHASFQYNRLKEQLESSKANWDSIEY 366
Cdd:PRK03918 326 IEerikelEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 367 ALNtKIVNLENRFESTMKEKNDIEEKYQTALRSSETLGKQL--EKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNL 444
Cdd:PRK03918 406 EIS-KITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 445 LKKKYEIQRSQLEQKE--NELKPHQENSNEKIIDKIPVELTDslnsMEGNIEDEWTLPQENSMLSLSMSKLGELESdpSL 522
Cdd:PRK03918 485 LEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEE----YEKLKEKLIKLKGEIKSLKKELEKLEELKK--KL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 523 KPIYNESHETICSEESQHFDRKNVDF-SIDDIPEEAAALQAIREgeSMNSLNNTSIPYRRASVQLSNSNGHISAHL--VN 599
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFYN--EYLELKDAEKELEREEKELKKLEEELDKAFeeLA 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 600 KLSTELKRLEGELSA-----SKELYDNLLKEKTKANDEILRLLEE----NDKFNEVNKQKDDLLKRVEQMQSKLEtSLQL 670
Cdd:PRK03918 637 ETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAEleelEKRREEIKKTLEKLKEELEEREKAKK-ELEK 715
|
570 580
....*....|....*....|.
gi 398365551 671 LGEKTEQVEELENDVSDLKEM 691
Cdd:PRK03918 716 LEKALERVEELREKVKKYKAL 736
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-491 |
3.75e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 121 TVEELVKEISPEYLRLNKQIDDLTNELNRKSQIE-TTDSSFFKLIKE---KDDLIDQLRKEGAKLAETELRQSNQIKALR 196
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADlhkREKELSLEKEQNKRLWDRDTGNSITIDHLR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 197 TKVKDLEYEVSELNDS-SAQSVENYNELQSLYHNIQGQlAEATNKLKDADKQKESLETLEKNIKEKddlITILQQSLDNM 275
Cdd:pfam15921 419 RELDDRNMEVQRLEALlKAMKSECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEE---LTAKKMTLESS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 276 RTLLEKEKSEFQTEKKALqEATVDQVTTLET----KLEQLRIELDSSTQNLDAKSNRDFVDDQQSYEEKQhasfqYNRLK 351
Cdd:pfam15921 495 ERTVSDLTASLQEKERAI-EATNAEITKLRSrvdlKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV-----IEILR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 352 EQLES---------SKANWDSIEYALNTKIVNlENRFEstMKEKNDIEEKYQTALRSSETLGKQLEKEK----ENHSKAV 418
Cdd:pfam15921 569 QQIENmtqlvgqhgRTAGAMQVEKAQLEKEIN-DRRLE--LQEFKILKDKKDAKIRELEARVSDLELEKvklvNAGSERL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 419 LEVKDLERRAETL-------KSSLQSISDDYNLLKKKYEIQRSQLEQKENELKPHQENSNEKIidkipVELTDSLNSMEG 491
Cdd:pfam15921 646 RAVKDIKQERDQLlnevktsRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL-----EQTRNTLKSMEG 720
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
162-422 |
4.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 162 KLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKL 241
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 242 KDADKQKESLETLEKNIKEkddlitiLQQSLDNMRTLLEKEK------SEFQTEKKALQEATV--DQVTTLETKLEQLRI 313
Cdd:COG1340 102 AELNKAGGSIDKLRKEIER-------LEWRQQTEVLSPEEEKelvekiKELEKELEKAKKALEknEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 314 ELDSSTQNLdaksnrdfvddQQSYEEKQHASFQYNRLKEQLESSKANWDsieyALNTKIVNLENRFESTMKEKNDIEEKY 393
Cdd:COG1340 175 EAEEIHKKI-----------KELAEEAQELHEEMIELYKEADELRKEAD----ELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260
....*....|....*....|....*....
gi 398365551 394 QTALRSSETLGKQLEKEKENHSKAVLEVK 422
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
124-440 |
4.77e-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: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 124 ELVKEISPEYLRLNKQIDDLTNELNRK-SQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDL 202
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 203 EYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKNIKEKDDLITILQQSLDNMRTLLEKE 282
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 283 KSEFQTEKKALQEATVDQVTTLetKLEQLRIELDSSTQNLDaksnrdfvDDQQSYEEKQHASFQYNRLKEQLESSKANWD 362
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIE--------ELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365551 363 SIEYALNTKIVNLENRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISD 440
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-446 |
4.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 162 KLIKEKDDLIDQLRKEGAKLaETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELqslYHNIQGQLAEATNKL 241
Cdd:PRK03918 466 KELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE---YEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 242 KDADKQKESLETLEKNIKEkddlitiLQQSLDNmrtlLEKEKSEFQTEKKALQEATVDQvttLETKLEQLR------IEL 315
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAE-------LEKKLDE----LEEELAELLKELEELGFESVEE---LEERLKELEpfyneyLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 316 DSSTQNLDAKSNR---DFVDDQQSYEEKQHASFQYNRLKEQLESSKANWDSIEYAlntkivNLENRFESTMKEKNDIEEK 392
Cdd:PRK03918 608 KDAEKELEREEKElkkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE------ELREEYLELSRELAGLRAE 681
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365551 393 YQTALRSSETLGKQLEK---EKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLK 446
Cdd:PRK03918 682 LEELEKRREEIKKTLEKlkeELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| ClyA_HblB-like |
cd22653 |
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model ... |
214-367 |
5.44e-03 |
|
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model includes Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL (HBL), and is a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). HBL is composed of three distinct protein components, B, L1, and L2, which together possess hemolytic, cytotoxic, dermonecrotic, and vascular permeability activities in B. cereus. Although all three HBL components can individually bind to the membrane, it requires the three components to form a complex to form a pore. Structure of HblB shows an elongated, almost entirely alpha-helical protein, except for a short hydrophobic beta-hairpin known as the beta-tongue. HBL from Bacillus toyonensis BV-17 (a strain isolated from feces samples of healthy donors) has antitumor activity both in vitro and in vivo and may have potential as a treatment for colon cancer. For B. toyonesis HBL, combining HBL-B and HBL-L2 had no cytotoxicity but combining HBL-B and HBL-L1 does.
Pssm-ID: 439151 [Multi-domain] Cd Length: 231 Bit Score: 39.11 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 214 AQSVENYNELQSLYHNiqgQLAEATNKlKDADKQKESLETLEKNIKEK----DDLITILQQsldnMRTLLEKEKSEFQTE 289
Cdd:cd22653 70 NQNIINYNTQFQNYYD---TLVDAIDK-KDKETLKEGLTDLYKDISENkkevDQLIKDLKK----FRDKLSTDTQNFKND 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 290 KKALQ----EATVDQVTTLETKLEQLRIELDS--------STQ--NLDAKSNrDFVDDQQSYEEKqhasfQYNRLKEQLE 355
Cdd:cd22653 142 VNQLTssgaQQEVAILTDAKNQTTNLTETIDQaitalqniSNQwdTMGAKYK-SLLDNIDNIDPE-----DLEFIKEDLN 215
|
170
....*....|...
gi 398365551 356 SSKANWDSI-EYA 367
Cdd:cd22653 216 TAKDSWQDLkEYA 228
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
151-464 |
6.06e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 151 SQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAETE---LRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLY 227
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQAETELCAEAEemrARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 228 HNIQGQLAEatnklKDADKQKESLE--TLEKNIKEKDDLITIL---QQSLDNMRTLLEKEKSEFqTEKKALQEATVDQVT 302
Cdd:pfam01576 106 QDLEEQLDE-----EEAARQKLQLEkvTTEAKIKKLEEDILLLedqNSKLSKERKLLEERISEF-TSNLAEEEEKAKSLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 303 TLETKLEQLRIELDSSTQNlDAKSNRDFVDDQQSYE-EKQHASFQYNRLKEQLESSKANWDSIEYALNTkivnLENRFES 381
Cdd:pfam01576 180 KLKNKHEAMISDLEERLKK-EEKGRQELEKAKRKLEgESTDLQEQIAELQAQIAELRAQLAKKEEELQA----ALARLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 382 TMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLKKkyeiQRSQLEQKEN 461
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVT 330
|
...
gi 398365551 462 ELK 464
Cdd:pfam01576 331 ELK 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-691 |
6.27e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 122 VEELVKEISPEYLRLNKQIDDLTNEL----NRKSQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRT 197
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 198 KVKDLEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLEtlekniKEKDDLITILQQSLDNMRT 277
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE------DRRERLQQEIEELLKKLEE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 278 LLEKEKSEFQTEKKALQEATVDQVTTLETKLEQLRIELDSSTQNLDAKSNRD---------FVDDQQSYEEKQHA----- 343
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqarldsLERLQENLEGFSEGvkall 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 344 ------SFQYNRLKEQL-----------------------ESSKANWDSIEY-----------------------ALNTK 371
Cdd:TIGR02168 513 knqsglSGILGVLSELIsvdegyeaaieaalggrlqavvvENLNAAKKAIAFlkqnelgrvtflpldsikgteiqGNDRE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 372 IVNLENRFESTMKEKNDIEEKYQTALRS-------SETLGKQLEKEKENHSKAVLEVKD--------------------- 423
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsaktnssi 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 424 LERRAE--TLKSSLQSISDDYNLLKKKYEIQRSQLEQKENELKPHQENSNEKIIDKipVELTDSLNSMEGNIEdewTLPQ 501
Cdd:TIGR02168 673 LERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI--SALRKDLARLEAEVE---QLEE 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 502 ENSMLSLSMSKLGELESDPSLKPIYNESHETICSEEsqhfdRKNVDFSIDDIPEEAAALqaIREGESMNS-LNNTSIPYR 580
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKAL--REALDELRAeLTLLNEEAA 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 581 RASVQLSNSNGHISA--HLVNKLSTELKRLEGELSASKELYDNLLKEKTKANDEILRLLEENDKFNE----VNKQKDDL- 653
Cdd:TIGR02168 821 NLRERLESLERRIAAteRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELs 900
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 398365551 654 --LKRVEQMQSKLETSLQLLGEKTEQV----EELENDVSDLKEM 691
Cdd:TIGR02168 901 eeLRELESKRSELRRELEELREKLAQLelrlEGLEVRIDNLQER 944
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
158-690 |
7.25e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 158 SSFFKLIKEKDDLIDQLRKEGAKLAETEL---RQSNQIKALRTKVKDLEYEVSELNDSSAQSVENYNELQslyhNIQGQL 234
Cdd:PRK01156 131 NSIFVGQGEMDSLISGDPAQRKKILDEILeinSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 235 AEATNKLKDADKQKESLEtLEKNIKEKDdlITILQQSLDNMRTLLEKEK---SEFQTEKKALQEATVDQVTTLETKLEQL 311
Cdd:PRK01156 207 ADDEKSHSITLKEIERLS-IEYNNAMDD--YNNLKSALNELSSLEDMKNryeSEIKTAESDLSMELEKNNYYKELEERHM 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 312 RIEldsstqNLDAKSNRDFVDDQQSYEEkqhasfQYNRLKEQLESSKANWDSIEYALNtKIVNLE---NRFESTMKEKND 388
Cdd:PRK01156 284 KII------NDPVYKNRNYINDYFKYKN------DIENKKQILSNIDAEINKYHAIIK-KLSVLQkdyNDYIKKKSRYDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 389 I----------EEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLEQ 458
Cdd:PRK01156 351 LnnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 459 KENELKPHQEnsnekiidkipvELTDSLNSMEGNiedewtlpqenSMLSLSMSKLGElESDPSLKPIYNESHETIcSEES 538
Cdd:PRK01156 431 RIRALRENLD------------ELSRNMEMLNGQ-----------SVCPVCGTTLGE-EKSNHIINHYNEKKSRL-EEKI 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 539 QHFDRKNVDfsIDDIPEEAAALQAIREGESMNSLNNTSIPYRRASVQLSNSNGHIS----AHL-VNKLSTELKRLE-GEL 612
Cdd:PRK01156 486 REIEIEVKD--IDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINelkdKHDkYEEIKNRYKSLKlEDL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 613 SASKELYDNLL----------------KEKTKANDEILRLLEENDKFNEVNKQKDDLLKRVEQMQSKLETSLQLLGEKTE 676
Cdd:PRK01156 564 DSKRTSWLNALavislidietnrsrsnEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKI 643
|
570
....*....|....
gi 398365551 677 QVEELENDVSDLKE 690
Cdd:PRK01156 644 LIEKLRGKIDNYKK 657
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-464 |
7.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 191 QIKALRTKVKDLEYEVSELNDSSAQSVENYNELQSLYHNIqgqlaeatnklkdaDKQKESLETLEKnIKEKDDLITILQQ 270
Cdd:COG4913 205 PIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEAL--------------EDAREQIELLEP-IRELAERYAAARE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 271 SLDNMRTLLEKEKSEFQTEKKALqeatvdqvttLETKLEQLRIELDSSTQNLDAKSNRdfvddqqsyEEKQHAsfQYNRL 350
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLEL----------LEAELEELRAELARLEAELERLEAR---------LDALRE--ELDEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 351 KEQLESSKanWDSIEyALNTKIVNLEnrfestmKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKDlerRAET 430
Cdd:COG4913 329 EAQIRGNG--GDRLE-QLEREIERLE-------RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEA 395
|
250 260 270
....*....|....*....|....*....|....
gi 398365551 431 LKSSLQSISDDYNLLKKKYEIQRSQLEQKENELK 464
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
114-689 |
7.93e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 114 PKNYTEFTVEELVKEISPEYlrlNKQIDDLTNELNRKSQIEttDSSFFKLIKEKDDL---IDQLRKEGAKLAETELRQSN 190
Cdd:pfam15921 64 PRKIIAYPGKEHIERVLEEY---SHQVKDLQRRLNESNELH--EKQKFYLRQSVIDLqtkLQEMQMERDAMADIRRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 191 QIKALRTKVKDLEYEVSE--------LNDSSAQsvenYNELQSLYHNIQGQLAEATNKLKDADkqkeslETLEKNIKEKD 262
Cdd:pfam15921 139 SQEDLRNQLQNTVHELEAakclkedmLEDSNTQ----IEQLRKMMLSHEGVLQEIRSILVDFE------EASGKKIYEHD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 263 DLITIlqqSLDNMRTLLEKEKSEFQTEKKALQeatvDQVTTLETKLEQLRIELDSSTQNLdAKSNRDFVDDQQSYEEkqh 342
Cdd:pfam15921 209 SMSTM---HFRSLGSAISKILRELDTEISYLK----GRIFPVEDQLEALKSESQNKIELL-LQQHQDRIEQLISEHE--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 343 asFQYNRLKEQLESSKANWDSIEYALNTKIVNLENRFESTMKEKNDIEE---KYQTALRSS--------ETLGKQLEKEK 411
Cdd:pfam15921 278 --VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLEStvsQLRSELREAkrmyedkiEELEKQLVLAN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 412 ENHSKAVLEVKDLERRAETLKSSLQSISDDynLLKKKYEIQrsqLEQKENELKPHQENSNEKIIDKIPVELTDSlnsmeg 491
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLAD--LHKREKELS---LEKEQNKRLWDRDTGNSITIDHLRRELDDR------ 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 492 NIEDEWTlpqENSMLSLSMSKLGELESDPSLKPIYNESHETICSEESQHFDRKNVDFSIddIPEEAAALQAIREGESMNS 571
Cdd:pfam15921 425 NMEVQRL---EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV--VEELTAKKMTLESSERTVS 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 572 LNNTSIPYRRASVQLSNSNghisahlVNKLSTELKRLEGELSASKELYDNLLKEKTKAndEILRL-LEENDKFNEVNKQ- 649
Cdd:pfam15921 500 DLTASLQEKERAIEATNAE-------ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC--EALKLqMAEKDKVIEILRQq 570
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365551 650 ---------------------KDDLLKRVEQMQSKLETSLQLLGEKTEQVEELENDVSDLK 689
Cdd:pfam15921 571 ienmtqlvgqhgrtagamqveKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-478 |
8.60e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 141 DDLTNELNRKSQIETTDSSFFKLIKEKDDLIDQLRKEGAKLAETELRQSNQIKALRTKVKDLEYEVSELNDSSAQSVENY 220
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 221 NELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKNIKEkddLITILQQSLDNmrtlLEKEKSEFQTEKKALQEATvdq 300
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE---TIIKNNSEIKD----LTNQDSVKELIIKNLDNTR--- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 301 vTTLETKLEQLRIELDSSTQNLDAKsnrdfvddQQSYEEKQHASFQYNRLKEQLESSKANWDSIEYALNTKIVNLE---N 377
Cdd:TIGR04523 464 -ESLETQLKVLSRSINKIKQNLEQK--------QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLEsekK 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 378 RFESTMKEKNDIEEKYQTALRSSEtLGKQLEKEKENHSKAVLEVKDLERRAETLKSSLQSISDDYNLLKKKYEIQRSQLE 457
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEN-LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
330 340
....*....|....*....|.
gi 398365551 458 QKENELKpHQENSNEKIIDKI 478
Cdd:TIGR04523 614 SLEKELE-KAKKENEKLSSII 633
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
122-464 |
9.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 122 VEELVKEISPEYLRLNKQIDDLTNELNRKSQIETTDSSFFKLIKEKDDLIDQLRKEGAKLaETELRQSNQIKALRTKVKD 201
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 202 LEYEVSELNDSSAQSVENYNELQSLYHNIQGQLAEATNKLKDADKQKESLETLEKN---IKEKDDLITILQQSLDNMRTL 278
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleeLEERHELYEEAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 279 -----------LEKEKSEFQTEKKALQEAtVDQVTTLETKLEQLRIELDSSTQNLD-AKSNRDFVDDQQSYEEKQHASFQ 346
Cdd:PRK03918 378 kkrltgltpekLEKELEELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKkAKGKCPVCGRELTEEHRKELLEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365551 347 YNRLKEQLESSKANWDSIEYALNTKIVNLE---NRFESTMKEKNDIEEKYQTALRSSETLGKQLEKEKENHSKAVLEVKD 423
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398365551 424 LERRAETLKSSLQSIsddyNLLKKKYEIQRSQLEQKENELK 464
Cdd:PRK03918 537 LKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELA 573
|
|
| |
