|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
416-615 |
1.33e-98 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 299.28 E-value: 1.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 416 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 495
Cdd:pfam05010 2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 496 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 575
Cdd:pfam05010 82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217372989 576 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 615
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
419-618 |
9.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 419 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 495
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 496 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 575
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217372989 576 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 618
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-607 |
2.95e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 427 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaQMIEDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLS 506
Cdd:TIGR02168 218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEV-------SELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 507 DLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGL 583
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAEL 360
|
170 180
....*....|....*....|....
gi 2217372989 584 RKEQMKVESLERALQQKNQEIEEL 607
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETL 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-618 |
1.47e-06 |
|
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: 50.92 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 424 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSV-- 501
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAELLRAly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 502 -------------ERSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQv 568
Cdd:COG4942 115 rlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEA- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217372989 569 rtkAKAESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 618
Cdd:COG4942 193 ---LKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
443-618 |
3.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 443 KKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtsqksFQQLTMEKEQALADLNSVER--SLSDLFRRYENLKGVLE 520
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEE--------LEELEAELEELREELEKLEKllQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 521 GFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQK 600
Cdd:COG4717 143 ELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170
....*....|....*...
gi 2217372989 601 NQEIEELTKICDELIAKL 618
Cdd:COG4717 219 QEELEELEEELEQLENEL 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
419-616 |
3.43e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 419 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKE---QAL 495
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 496 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQ-EEQRYQALK--IHAEEKLDKANEEIAQVRTKA 572
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAelAEAEEELEELAEELLEALRAA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217372989 573 KAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIA 616
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
428-607 |
4.05e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 47.98 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 428 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTsQKSFQQLTMEKEQALADLNSVE 502
Cdd:pfam13851 41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL-EKELKDLKWEHEVLEQRFEKVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 503 RSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESAA 578
Cdd:pfam13851 120 RERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPDA 178
|
170 180
....*....|....*....|....*....
gi 2217372989 579 LhaglrkeQMKVESLERALQQKNQEIEEL 607
Cdd:pfam13851 179 L-------QAVTEKLEDVLESKNQLIKDL 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
426-618 |
4.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 426 LIREEIITKEIEAN---------------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMiedeqrtsmtsqksfQQLT 488
Cdd:COG1196 188 LERLEDILGELERQleplerqaekaeryrELKEELKELEAEllLLKLRELEAELEELEAEL---------------EELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 489 MEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQV 568
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217372989 569 RTK---AKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 618
Cdd:COG1196 329 EEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-613 |
5.08e-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: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 428 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKT---IAQMIEDeqrtsMTSQKSFQQltMEKEQALADLNSVERS 504
Cdd:TIGR02168 254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISR-----LEQQKQILR--ERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 505 LSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIH---AEEKLDKANEEIAQVRTKAKAESAALHA 581
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190
....*....|....*....|....*....|..
gi 2217372989 582 gLRKEqmkVESLERALQQKNQEIEELTKICDE 613
Cdd:TIGR02168 405 -LEAR---LERLEDRRERLQQEIEELLKKLEE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
424-618 |
7.72e-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: 49.28 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 424 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtSQKSFQQLTMEKEQALADLNSVER 503
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 504 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAGL 583
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217372989 584 RKEQMKVESLERA---LQQKNQEIEELTKICDELIAKL 618
Cdd:TIGR02168 838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
424-609 |
1.93e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 424 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVE- 502
Cdd:PRK04863 884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 503 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKL 558
Cdd:PRK04863 957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQML 1036
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217372989 559 DKANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 609
Cdd:PRK04863 1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
434-613 |
3.99e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 434 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIEdEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 513
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 514 NLKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEE--IAQVRTKAKAESAALHAGLR 584
Cdd:PTZ00121 1630 EEKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDekKAAEALKKEAEEAKKAEELK 1708
|
170 180 190
....*....|....*....|....*....|...
gi 2217372989 585 K----EQMKVESLERALQQKNQEIEELTKICDE 613
Cdd:PTZ00121 1709 KkeaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-609 |
5.41e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 446 EETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSM---TSQKSFQQLTMEKEQALADLNSVERSLSDL---FRRYENLKGVL 519
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 520 EGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR----------TKAKAESAALHAGLRKEQMK 589
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrealDELRAELTLLNEEAANLRER 825
|
170 180
....*....|....*....|
gi 2217372989 590 VESLERALQQKNQEIEELTK 609
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEE 845
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
424-614 |
6.59e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 424 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedEQRTSMTSQKSFQQL--TMEKEQALADLNSV 501
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA----REDALNQSLKELMHQarTVLKARTEAHFNNN 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 502 ERSLSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAAL 579
Cdd:TIGR00618 768 EEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATL 844
|
170 180 190
....*....|....*....|....*....|....*
gi 2217372989 580 HAgLRKEQMKVESLERALQQKNQEIEELTKICDEL 614
Cdd:TIGR00618 845 GE-ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
427-585 |
7.07e-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: 44.53 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 427 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQR-----TSMTSQKSFQQLTMEKEQALADLNSV 501
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlGNVRNNKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 502 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 581
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181
|
....
gi 2217372989 582 GLRK 585
Cdd:COG1579 182 RIRK 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
437-594 |
8.55e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 44.29 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 437 EANEWKKKYEET----RQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS-DLFRR 511
Cdd:pfam04012 12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELArEALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 512 YENLKGVLEGFKKN-------EEALKKCAQDYLARVKQEEQRYQALKihAEEKLDKANEEIAQVRTKAKAESAAlhAGLR 584
Cdd:pfam04012 92 KKSLEKQAEALETQlaqqrsaVEQLRKQLAALETKIQQLKAKKNLLK--ARLKAAKAQEAVQTSLGSLSTSSAT--DSFE 167
|
170
....*....|
gi 2217372989 585 KEQMKVESLE 594
Cdd:pfam04012 168 RIEEKIEERE 177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
437-613 |
8.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 437 EANEWKKKYEETRQEVLEMRKiVAEYEKTIAQMIEDEQrtsmtsQKSFQQLTMEKEQALADlnsvERSLSDLFRRYENLK 516
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEA------EAAADEAEAAEEKAEAA----EKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 517 GVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRK---EQMKVESL 593
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEA 1462
|
170 180
....*....|....*....|
gi 2217372989 594 ERALQQKnQEIEELTKICDE 613
Cdd:PTZ00121 1463 KKKAEEA-KKADEAKKKAEE 1481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
437-614 |
1.05e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 437 EANEW-KKKYEETRQEVLEMRKIVAEYeKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALADLNSVERSLSDLFRRYENL 515
Cdd:COG3206 175 KALEFlEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 516 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 588
Cdd:COG3206 253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327
|
170 180
....*....|....*....|....*.
gi 2217372989 589 KVESLERALQQKNQEIEELTKICDEL 614
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAEL 353
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
437-621 |
1.83e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 437 EANEWKKKYEETRQEVLEMRKIVAEY------EKTIAQMIEDEQRTSMTSQksfqqLTMEKEQALadlnsVERsLSDLFR 510
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEV-----LSPEEEKEL-----VEK-IKELEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 511 RYENLKGVLEGFKKNEEALKKCAQdylARVKQEEQRyQALKIHAEEkLDKANEEIAQVRTKA---KAESAALHAGLRKEQ 587
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKE---LRKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAdelRKEADELHKEIVEAQ 222
|
170 180 190
....*....|....*....|....*....|....
gi 2217372989 588 MKVESLERALQQKNQEIEELTKICDELIAKLGKT 621
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
442-609 |
3.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 442 KKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 521
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 522 FKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKN 601
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
....*...
gi 2217372989 602 QEIEELTK 609
Cdd:COG4372 164 EELAALEQ 171
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
443-613 |
3.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 443 KKYEETRQEVLEMRKivAEYEKTIAQMIE-DEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 521
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKK--AEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 522 FKKNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKN 601
Cdd:PTZ00121 1308 KKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAK 1377
|
170
....*....|..
gi 2217372989 602 QEIEELTKICDE 613
Cdd:PTZ00121 1378 KKADAAKKKAEE 1389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
428-619 |
4.22e-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: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 428 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IED-EQRTSM----TSQKSFQQLTMEKEQALADLN 499
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeeaLNDlEARLSHsripEIQAELSKLEEEVSRIEARLR 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 500 SVERSLSDLfrryENLKGVLEGFKKNEEALKKCAQDylaRVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAesaal 579
Cdd:TIGR02169 816 EIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESR----- 883
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217372989 580 HAGLRKEQMKVES----LERALQQKNQEIEELTKICDELIAKLG 619
Cdd:TIGR02169 884 LGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
417-606 |
7.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 417 ESDKTAVLTLIREEIITKEIEAnewkKKYEETRQEVLEMRKivaeyEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALA 496
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 497 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLA----RVKQEEQRYQALKIHAEEKLDKANEEIAQVRT-- 570
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAee 1741
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217372989 571 -KAKAESAALHAGlrkEQMKVESLERALQQKNQEIEE 606
Cdd:PTZ00121 1742 dKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRK 1775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
425-620 |
1.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 425 TLIREEIITKEIEanEWKKKYEETRQEVLEMRKivAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVE 502
Cdd:PRK03918 494 ELIKLKELAEQLK--ELEEKLKKYNLEELEKKA--EEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 503 RSLSDLFRRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESA 577
Cdd:PRK03918 570 EELAELLKELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217372989 578 AL-----------HAGLRKEQMKvesLERALQQKNQEIEELTKICDELIAKLGK 620
Cdd:PRK03918 648 ELeelekkyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
429-620 |
1.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 429 EEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDL 508
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 509 FRRYENLKGVLEGFKKNEEALKK-------CAQ--------DYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAK 573
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvCGRelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217372989 574 AESAALHagLRKEQMKVESLERALQQKN-QEIEELTKICDELIAKLGK 620
Cdd:PRK03918 491 KESELIK--LKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
513-617 |
1.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 513 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 589
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 2217372989 590 VESLERALQQKNQEIEELTKICDELIAK 617
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
427-534 |
1.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 427 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 506
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100
....*....|....*....|....*...
gi 2217372989 507 DLFRRYENLKGVLEGFKKNEEALKKCAQ 534
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEER 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
485-618 |
2.64e-03 |
|
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: 39.91 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 485 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 550
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217372989 551 -----KIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 618
Cdd:COG1579 100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
418-606 |
2.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 418 SDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIE--DEQRTSMTSQKSFQQLTMEKEQAL 495
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeiEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 496 ADLNSVErSLSDLFRRYENLKGVLEGfkkneealkkcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---- 571
Cdd:COG3883 106 DVLLGSE-SFSDFLDRLSALSKIADA-----------DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkael 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217372989 572 --AKAESAALHAGLRKEQMKVESLERALQQKNQEIEE 606
Cdd:COG3883 174 eaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
437-603 |
3.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 437 EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAladlnsveRSLSDLFRRYENLK 516
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 517 GVLEGFKKNEEALKKCAQdylARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAALHAGLRK--EQMKVESLE 594
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKadELKKAEELK 1558
|
....*....
gi 2217372989 595 RALQQKNQE 603
Cdd:PTZ00121 1559 KAEEKKKAE 1567
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
429-609 |
4.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 429 EEIITKEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 506
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 507 DLFRRYENLKGVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKE 586
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
170 180
....*....|....*....|...
gi 2217372989 587 QMKVESLERALQQKNQEIEELTK 609
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
418-587 |
5.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 418 SDKTAVLTLIREEIITKEI-EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMieDEQRTSMTSQKSFQQLTMEKEQALA 496
Cdd:COG4717 62 QGRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 497 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KIHAEEKLDKAN 562
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 2217372989 563 EEIAQVRTKAKAESAALHAGLRKEQ 587
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
434-579 |
5.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 434 KEIEAN-EWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedeqrtsmtsqksfqqltmeKEQALadlnsvERSLSDLFRRY 512
Cdd:PRK12704 58 ALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQ----------------------KEENL------DRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217372989 513 ENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQAL-KIHAEEkldkANEEI-AQVRTKAKAESAAL 579
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEE----AKEILlEKVEEEARHEAAVL 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
490-622 |
6.09e-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: 39.67 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 490 EKEQALA-DLNSVERSLSDLFRRYENLKGVL-EGFKKNEEALKKC--AQDYLARVKQEEQRYQALKIHAEEKLDKANEEI 565
Cdd:TIGR02169 674 AELQRLReRLEGLKRELSSLQSELRRIENRLdELSQELSDASRKIgeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217372989 566 AQVRTKAK---AESAALHAGLRKEQMKVESLERAL-----QQKNQEIEELTKICDELIAKLGKTD 622
Cdd:TIGR02169 754 ENVKSELKeleARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIE 818
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
417-618 |
7.44e-03 |
|
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: 39.57 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 417 ESDKTAVLTLIREEIITKEIEANEWKKKYEETRQ----EVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQL--TME 490
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLkeklELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkqEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 491 KEQALADLNSVERSLSdlfrryenlkgvlEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrt 570
Cdd:pfam02463 262 KEEEKLAQVLKENKEE-------------EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK--- 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217372989 571 KAKAESAALHAGLRKEQMKvESLERALQQKNQEIEELTKICDELIAKL 618
Cdd:pfam02463 326 AEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLE 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-582 |
7.47e-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: 38.98 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 424 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTS-------MTSQKSF------------ 484
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFldavrrlqylky 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 485 -----QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLD 559
Cdd:COG4942 144 laparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180
....*....|....*....|...
gi 2217372989 560 KANEEIAQVRTKAKAESAALHAG 582
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
428-621 |
7.79e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 428 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSmTSQKSFQqltmEKEQALADLNSVERSLSD 507
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK-EKEKELE----EVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 508 -------LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKA--ESAA 578
Cdd:PRK03918 222 eleklekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEyiKLSE 300
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217372989 579 LHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 621
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
488-618 |
8.08e-03 |
|
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: 38.37 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 488 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKI---HAEEKLDKANE 563
Cdd:COG1579 1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217372989 564 EIAQVRTkAKAESAALH--AGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 618
Cdd:COG1579 81 QLGNVRN-NKEYEALQKeiESLKRRI---SDLEDEILELMERIEELEEELAELEAEL 133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-620 |
9.25e-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: 39.28 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 407 ESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAqmiedeqrtsmtsqksfqq 486
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372989 487 ltmEKEQALADLnsvERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKihaeEKLDKANEEIA 566
Cdd:TIGR02169 872 ---ELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELK----AKLEALEEELS 934
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217372989 567 QVRTKAKA--ESAALHAGLRKEQMKVESLERALQQKN-------QEIEELTKICDELIAKLGK 620
Cdd:TIGR02169 935 EIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
|
|
|