|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
615-814 |
4.21e-99 |
|
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: 305.83 E-value: 4.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 615 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 694
Cdd:pfam05010 2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 695 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 774
Cdd:pfam05010 82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1209185233 775 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 814
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
618-817 |
9.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 618 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 694
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 695 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 774
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1209185233 775 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 817
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
626-806 |
1.83e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 626 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaQMIEDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLS 705
Cdd:TIGR02168 218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEV-------SELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 706 DLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGL 782
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAEL 360
|
170 180
....*....|....*....|....
gi 1209185233 783 RKEQMKVESLERALQQKNQEIEEL 806
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETL 384
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
627-806 |
5.20e-07 |
|
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: 51.06 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 627 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTsQKSFQQLTMEKEQALADLNSVE 701
Cdd:pfam13851 41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL-EKELKDLKWEHEVLEQRFEKVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 702 RSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESAA 777
Cdd:pfam13851 120 RERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPDA 178
|
170 180
....*....|....*....|....*....
gi 1209185233 778 LhaglrkeQMKVESLERALQQKNQEIEEL 806
Cdd:pfam13851 179 L-------QAVTEKLEDVLESKNQLIKDL 200
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
626-817 |
1.10e-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: 51.69 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 626 IREEI--ITKEIEANEWKKK-----YEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLN 698
Cdd:COG4942 32 LQQEIaeLEKELAALKKEEKallkqLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 699 SV---------------ERSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEE 763
Cdd:COG4942 111 RAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1209185233 764 IAQvrtkAKAESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 817
Cdd:COG4942 190 LEA----LKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
642-817 |
1.41e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 642 KKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtsqksFQQLTMEKEQALADLNSVER--SLSDLFRRYENLKGVLE 719
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEE--------LEELEAELEELREELEKLEKllQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 720 GFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQK 799
Cdd:COG4717 143 ELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170
....*....|....*...
gi 1209185233 800 NQEIEELTKICDELIAKL 817
Cdd:COG4717 219 QEELEELEEELEQLENEL 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-815 |
2.76e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 621 AVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRK----IVAEYEKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALAD 696
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELeleeAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 697 LNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKcaqdylARVKQEEQRYQALK--IHAEEKLDKANEEIAQVRTKAKAE 774
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEA------ELAEAEEALLEAEAelAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1209185233 775 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIA 815
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
625-817 |
2.90e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 625 LIREEIITKEIEAN---------------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMiedeqrtsmtsqksfQQLT 687
Cdd:COG1196 188 LERLEDILGELERQleplerqaekaeryrELKEELKELEAEllLLKLRELEAELEELEAEL---------------EELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 688 MEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQV 767
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1209185233 768 RTK---AKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 817
Cdd:COG1196 329 EEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
627-808 |
3.00e-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: 51.21 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 627 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKT---IAQMIEDeqrtsMTSQKSFQQltMEKEQALADLNSVERS 703
Cdd:TIGR02168 254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISR-----LEQQKQILR--ERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 704 LSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIH---AEEKLDKANEEIAQVRTKAKAESAALHA 780
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180
....*....|....*....|....*...
gi 1209185233 781 gLRKEqmkVESLERALQQKNQEIEELTK 808
Cdd:TIGR02168 405 -LEAR---LERLEDRRERLQQEIEELLK 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-817 |
6.18e-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: 50.06 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 623 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtSQKSFQQLTMEKEQALADLNSVER 702
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 703 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAGL 782
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190
....*....|....*....|....*....|....*...
gi 1209185233 783 RKEQMKVESLERA---LQQKNQEIEELTKICDELIAKL 817
Cdd:TIGR02168 838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
623-808 |
1.83e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 623 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVE- 701
Cdd:PRK04863 884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 702 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKL 757
Cdd:PRK04863 957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQML 1036
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185233 758 DKANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 808
Cdd:PRK04863 1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
636-820 |
2.65e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 636 EANEWKKKYEETRQEVLEMRKIVAEY------EKTIAQMIEDEQRTSMTSQksfqqLTMEKEQALadlnsVERsLSDLFR 709
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEV-----LSPEEEKEL-----VEK-IKELEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 710 RYENLKGVLEGFKKNEEALKKCaqdylarvkqEEQRYQALKIHAE-----EKLDKANEEIAQVRTKA---KAESAALHAG 781
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAEL----------KELRKEAEEIHKKikelaEEAQELHEEMIELYKEAdelRKEADELHKE 217
|
170 180 190
....*....|....*....|....*....|....*....
gi 1209185233 782 LRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 820
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-812 |
2.92e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 633 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIEdEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 712
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 713 NLKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEE--IAQVRTKAKAESAALHAGLR 783
Cdd:PTZ00121 1630 EEKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDekKAAEALKKEAEEAKKAEELK 1708
|
170 180 190
....*....|....*....|....*....|...
gi 1209185233 784 K----EQMKVESLERALQQKNQEIEELTKICDE 812
Cdd:PTZ00121 1709 KkeaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
623-813 |
3.38e-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: 47.66 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 623 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedEQRTSMTSQKSFQQL--TMEKEQALADLNSV 700
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA----REDALNQSLKELMHQarTVLKARTEAHFNNN 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 701 ERSLSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAAL 778
Cdd:TIGR00618 768 EEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATL 844
|
170 180 190
....*....|....*....|....*....|....*
gi 1209185233 779 HAgLRKEQMKVESLERALQQKNQEIEELTKICDEL 813
Cdd:TIGR00618 845 GE-ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
626-784 |
3.85e-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: 46.07 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 626 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQR-----TSMTSQKSFQQLTMEKEQALADLNSV 700
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlGNVRNNKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 701 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 780
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181
|
....
gi 1209185233 781 GLRK 784
Cdd:COG1579 182 RIRK 185
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
645-808 |
4.25e-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: 47.36 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 645 EETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSM---TSQKSFQQLTMEKEQALADLNSVERSLSDL---FRRYENLKGVL 718
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 719 EGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR----------TKAKAESAALHAGLRKEQMK 788
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrealDELRAELTLLNEEAANLRER 825
|
170 180
....*....|....*....|
gi 1209185233 789 VESLERALQQKNQEIEELTK 808
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEE 845
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
636-793 |
5.77e-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: 45.06 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 636 EANEWKKKYEET----RQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS-DLFRR 710
Cdd:pfam04012 12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELArEALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 711 YENLKGVLEGFKKN-------EEALKKCAQDYLARVKQEEQRYQALKihAEEKLDKANEEIAQVRTKAKAESAAlhAGLR 783
Cdd:pfam04012 92 KKSLEKQAEALETQlaqqrsaVEQLRKQLAALETKIQQLKAKKNLLK--ARLKAAKAQEAVQTSLGSLSTSSAT--DSFE 167
|
170
....*....|
gi 1209185233 784 KEQMKVESLE 793
Cdd:pfam04012 168 RIEEKIEERE 177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
636-812 |
6.31e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 636 EANEWKKKYEETRQEVLEMRKiVAEYEKTIAQMIEDEQrtsmtsQKSFQQLTMEKEQALADlnsvERSLSDLFRRYENLK 715
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEA------EAAADEAEAAEEKAEAA----EKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 716 GVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRK---EQMKVESL 792
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEA 1462
|
170 180
....*....|....*....|
gi 1209185233 793 ERALQQKnQEIEELTKICDE 812
Cdd:PTZ00121 1463 KKKAEEA-KKADEAKKKAEE 1481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
636-813 |
7.78e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 636 EANEW-KKKYEETRQEVLEMRKIVAEYeKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALADLNSVERSLSDLFRRYENL 714
Cdd:COG3206 175 KALEFlEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 715 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 787
Cdd:COG3206 253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327
|
170 180
....*....|....*....|....*.
gi 1209185233 788 KVESLERALQQKNQEIEELTKICDEL 813
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAEL 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
641-808 |
1.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 641 KKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 720
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 721 FKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKN 800
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
....*...
gi 1209185233 801 QEIEELTK 808
Cdd:COG4372 164 EELAALEQ 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
624-819 |
2.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 624 TLIREEIITKEIEanEWKKKYEETRQEVLEMRKivAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVE 701
Cdd:PRK03918 494 ELIKLKELAEQLK--ELEEKLKKYNLEELEKKA--EEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 702 RSLSDLFRRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESA 776
Cdd:PRK03918 570 EELAELLKELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1209185233 777 AL-----------HAGLRKEQMKvesLERALQQKNQEIEELTKICDELIAKLGK 819
Cdd:PRK03918 648 ELeelekkyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
627-818 |
2.75e-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: 44.67 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 627 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IED-EQRTSM----TSQKSFQQLTMEKEQALADLN 698
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeeaLNDlEARLSHsripEIQAELSKLEEEVSRIEARLR 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 699 SVERSLSDLfrryENLKGVLEGFKKNEEALKKCAQDylaRVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAesaal 778
Cdd:TIGR02169 816 EIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESR----- 883
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1209185233 779 HAGLRKEQMKVES----LERALQQKNQEIEELTKICDELIAKLG 818
Cdd:TIGR02169 884 LGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-812 |
2.82e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 642 KKYEETRQEVLEMRKivAEYEKTIAQMIE-DEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 720
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKK--AEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 721 FKKNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKN 800
Cdd:PTZ00121 1308 KKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAK 1377
|
170
....*....|..
gi 1209185233 801 QEIEELTKICDE 812
Cdd:PTZ00121 1378 KKADAAKKKAEE 1389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
628-819 |
3.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 628 EEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDL 707
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 708 FRRYENLKGVLEGFKKNEEALKK-------CAQ--------DYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAK 772
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvCGRelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1209185233 773 AESAALHagLRKEQMKVESLERALQQKN-QEIEELTKICDELIAKLGK 819
Cdd:PRK03918 491 KESELIK--LKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
616-805 |
6.31e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 616 ESDKTAVLTLIREEIITKEIEAnewkKKYEETRQEVLEMRKivAEYEKtiaQMIEDEQRTSMTSQKSFQQLTMEKEQALA 695
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKK--AEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 696 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLA----RVKQEEQRYQALKIHAEEKLDKANEEIAQVRT-- 769
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAee 1741
|
170 180 190
....*....|....*....|....*....|....*..
gi 1209185233 770 -KAKAESAALHAGlrkEQMKVESLERALQQKNQEIEE 805
Cdd:PTZ00121 1742 dKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRK 1775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
626-733 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 626 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 705
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100
....*....|....*....|....*...
gi 1209185233 706 DLFRRYENLKGVLEGFKKNEEALKKCAQ 733
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
712-816 |
1.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 712 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 788
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 1209185233 789 VESLERALQQKNQEIEELTKICDELIAK 816
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
684-817 |
1.48e-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: 41.06 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 684 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 749
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185233 750 -----KIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 817
Cdd:COG1579 100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
616-817 |
1.52e-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: 42.27 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 616 ESDKTAVLTLIREEIITKEIEANEWKKKYEETRQ----EVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQL--TME 689
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLkeklELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkqEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 690 KEQALADLNSVERSLSdlfrryenlkgvlEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrt 769
Cdd:pfam02463 262 KEEEKLAQVLKENKEE-------------EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK--- 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1209185233 770 KAKAESAALHAGLRKEQMKvESLERALQQKNQEIEELTKICDELIAKL 817
Cdd:pfam02463 326 AEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLE 372
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
636-802 |
2.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 636 EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAladlnsveRSLSDLFRRYENLK 715
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 716 GVLEGFKKNEEALKKCAQdylARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAALHAGLRK--EQMKVESLE 793
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKadELKKAEELK 1558
|
....*....
gi 1209185233 794 RALQQKNQE 802
Cdd:PTZ00121 1559 KAEEKKKAE 1567
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
627-820 |
2.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 627 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSmTSQKSFQqltmEKEQALADLNSVERSLSD 706
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK-EKEKELE----EVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 707 -------LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKA--ESAA 777
Cdd:PRK03918 222 eleklekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEyiKLSE 300
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1209185233 778 LHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 820
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
617-786 |
2.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 617 SDKTAVLTLIREEIITKEI-EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMieDEQRTSMTSQKSFQQLTMEKEQALA 695
Cdd:COG4717 62 QGRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 696 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KIHAEEKLDKAN 761
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 1209185233 762 EEIAQVRTKAKAESAALHAGLRKEQ 786
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
628-808 |
3.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 628 EEIITKEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 705
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 706 DLFRRYENLKGVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKE 785
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
170 180
....*....|....*....|...
gi 1209185233 786 QMKVESLERALQQKNQEIEELTK 808
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
687-817 |
3.62e-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: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 687 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKI---HAEEKLDKANE 762
Cdd:COG1579 1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1209185233 763 EIAQVRTkAKAESAALH--AGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 817
Cdd:COG1579 81 QLGNVRN-NKEYEALQKeiESLKRRI---SDLEDEILELMERIEELEEELAELEAEL 133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
689-821 |
4.46e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 689 EKEQALA-DLNSVERSLSDLFRRYENLKGVL-EGFKKNEEALKKC--AQDYLARVKQEEQRYQALKIHAEEKLDKANEEI 764
Cdd:TIGR02169 674 AELQRLReRLEGLKRELSSLQSELRRIENRLdELSQELSDASRKIgeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209185233 765 AQVRTKAK---AESAALHAGLRKEQMKVESLERAL-----QQKNQEIEELTKICDELIAKLGKTD 821
Cdd:TIGR02169 754 ENVKSELKeleARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIE 818
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
627-795 |
4.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 627 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ--KSFQQLTMEKEQALADLNSVERSL 704
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEeiNGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 705 SDLFRRYENLKGVLEGFkknEEALKKCAQdyLARVKQEEQRYQALKIHAE-EKLDKANEEIAQVRTKAKAESAALHaGLR 783
Cdd:PRK03918 348 KELEKRLEELEERHELY---EEAKAKKEE--LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELK-KEI 421
|
170
....*....|...
gi 1209185233 784 KEQMK-VESLERA 795
Cdd:PRK03918 422 KELKKaIEELKKA 434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
633-778 |
4.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 633 KEIEAN-EWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedeqrtsmtsqksfqqltmeKEQALadlnsvERSLSDLFRRY 711
Cdd:PRK12704 58 ALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQ----------------------KEENL------DRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185233 712 ENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQAL-KIHAEEkldkANEEI-AQVRTKAKAESAAL 778
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEE----AKEILlEKVEEEARHEAAVL 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
609-809 |
6.16e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 609 LDGICLSESDKTAVLTLIREEIITKEIEANEWKKK----YEETRQEV----LEMR-KIVAEYEKTiaQMIEDEQRTSMTS 679
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKmilaFEELRVQAenarLEMHfKLKEDHEKI--QHLEEEYKKEIND 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 680 QKSFQQLTM----EKEQALADLNSVERSLSDLFRRYEnlkgvlEGFKKNEEALKKC--AQDYLAR----VKQEEQRYQAL 749
Cdd:pfam05483 238 KEKQVSLLLiqitEKENKMKDLTFLLEESRDKANQLE------EKTKLQDENLKELieKKDHLTKeledIKMSLQRSMST 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 750 KIHAEEKLDKANEEIAQ---------------------VRTKAKAESAALHAGLRKEQMKVES-------LERALQQKNQ 801
Cdd:pfam05483 312 QKALEEDLQIATKTICQlteekeaqmeelnkakaahsfVVTEFEATTCSLEELLRTEQQRLEKnedqlkiITMELQKKSS 391
|
....*...
gi 1209185233 802 EIEELTKI 809
Cdd:pfam05483 392 ELEEMTKF 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-819 |
6.16e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 606 ESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAqmiedeqrtsmtsqksfqq 685
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 686 ltmEKEQALADLnsvERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKihaeEKLDKANEEIA 765
Cdd:TIGR02169 872 ---ELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELK----AKLEALEEELS 934
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185233 766 QVRTKAKA--ESAALHAGLRKEQMKVESLERALQQKN-------QEIEELTKICDELIAKLGK 819
Cdd:TIGR02169 935 EIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
623-781 |
6.93e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 623 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTS-------MTSQKSF------------ 683
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFldavrrlqylky 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185233 684 -----QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLD 758
Cdd:COG4942 144 laparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180
....*....|....*....|...
gi 1209185233 759 KANEEIAQVRTKAKAESAALHAG 781
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAA 246
|
|
| |
