|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
611-810 |
1.41e-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: 306.99 E-value: 1.41e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 611 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 690
Cdd:pfam05010 2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 691 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 770
Cdd:pfam05010 82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1209185250 771 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 810
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
614-813 |
8.55e-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: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 614 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 690
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 691 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 770
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1209185250 771 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 813
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
622-802 |
1.47e-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: 55.45 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 622 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaQMIEDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLS 701
Cdd:TIGR02168 218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEV-------SELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 702 DLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGL 778
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAEL 360
|
170 180
....*....|....*....|....
gi 1209185250 779 RKEQMKVESLERALQQKNQEIEEL 802
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETL 384
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
623-802 |
4.05e-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: 51.45 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 623 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTsQKSFQQLTMEKEQALADLNSVE 697
Cdd:pfam13851 41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL-EKELKDLKWEHEVLEQRFEKVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 698 RSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESAA 773
Cdd:pfam13851 120 RERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPDA 178
|
170 180
....*....|....*....|....*....
gi 1209185250 774 LhaglrkeQMKVESLERALQQKNQEIEEL 802
Cdd:pfam13851 179 L-------QAVTEKLEDVLESKNQLIKDL 200
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
622-813 |
7.35e-07 |
|
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: 52.07 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 622 IREEI--ITKEIEANEWKKK-----YEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLN 694
Cdd:COG4942 32 LQQEIaeLEKELAALKKEEKallkqLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 695 SV---------------ERSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEE 759
Cdd:COG4942 111 RAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1209185250 760 IAQvrtkAKAESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 813
Cdd:COG4942 190 LEA----LKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
638-813 |
1.19e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 638 KKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtsqksFQQLTMEKEQALADLNSVER--SLSDLFRRYENLKGVLE 715
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEE--------LEELEAELEELREELEKLEKllQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 716 GFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQK 795
Cdd:COG4717 143 ELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170
....*....|....*...
gi 1209185250 796 NQEIEELTKICDELIAKL 813
Cdd:COG4717 219 QEELEELEEELEQLENEL 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
617-811 |
2.18e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 617 AVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRK----IVAEYEKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALAD 692
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELeleeAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 693 LNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKcaqdylARVKQEEQRYQALK--IHAEEKLDKANEEIAQVRTKAKAE 770
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEA------ELAEAEEALLEAEAelAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1209185250 771 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIA 811
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-813 |
2.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 621 LIREEIITKEIEAN---------------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMiedeqrtsmtsqksfQQLT 683
Cdd:COG1196 188 LERLEDILGELERQleplerqaekaeryrELKEELKELEAEllLLKLRELEAELEELEAEL---------------EELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 684 MEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQV 763
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1209185250 764 RTK---AKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 813
Cdd:COG1196 329 EEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-808 |
2.58e-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: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 623 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKT---IAQMIEDeqrtsMTSQKSFQQltMEKEQALADLNSVERS 699
Cdd:TIGR02168 254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISR-----LEQQKQILR--ERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 700 LSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIH---AEEKLDKANEEIAQVRTKAKAESAALHA 776
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190
....*....|....*....|....*....|..
gi 1209185250 777 gLRKEqmkVESLERALQQKNQEIEELTKICDE 808
Cdd:TIGR02168 405 -LEAR---LERLEDRRERLQQEIEELLKKLEE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-813 |
5.01e-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: 50.44 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 619 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtSQKSFQQLTMEKEQALADLNSVER 698
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 699 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAGL 778
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190
....*....|....*....|....*....|....*...
gi 1209185250 779 RKEQMKVESLERA---LQQKNQEIEELTKICDELIAKL 813
Cdd:TIGR02168 838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
619-804 |
1.35e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 619 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVE- 697
Cdd:PRK04863 884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 698 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKL 753
Cdd:PRK04863 957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQML 1036
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185250 754 DKANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 804
Cdd:PRK04863 1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
632-816 |
1.79e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 632 EANEWKKKYEETRQEVLEMRKIVAEY------EKTIAQMIEDEQRTSMTSQksfqqLTMEKEQALadlnsVERsLSDLFR 705
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEV-----LSPEEEKEL-----VEK-IKELEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 706 RYENLKGVLEGFKKNEEALKKCAQdylARVKQEEQRyQALKIHAEEkLDKANEEIAQVRTKA---KAESAALHAGLRKEQ 782
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKE---LRKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAdelRKEADELHKEIVEAQ 222
|
170 180 190
....*....|....*....|....*....|....
gi 1209185250 783 MKVESLERALQQKNQEIEELTKICDELIAKLGKT 816
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
629-808 |
2.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 629 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIEdEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 708
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 709 NLKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEE--IAQVRTKAKAESAALHAGLR 779
Cdd:PTZ00121 1630 EEKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDekKAAEALKKEAEEAKKAEELK 1708
|
170 180 190
....*....|....*....|....*....|...
gi 1209185250 780 K----EQMKVESLERALQQKNQEIEELTKICDE 808
Cdd:PTZ00121 1709 KkeaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
619-809 |
2.96e-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: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 619 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedEQRTSMTSQKSFQQL--TMEKEQALADLNSV 696
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA----REDALNQSLKELMHQarTVLKARTEAHFNNN 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 697 ERSLSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAAL 774
Cdd:TIGR00618 768 EEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATL 844
|
170 180 190
....*....|....*....|....*....|....*
gi 1209185250 775 HAgLRKEQMKVESLERALQQKNQEIEELTKICDEL 809
Cdd:TIGR00618 845 GE-ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
622-780 |
3.25e-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: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 622 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQR-----TSMTSQKSFQQLTMEKEQALADLNSV 696
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlGNVRNNKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 697 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 776
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181
|
....
gi 1209185250 777 GLRK 780
Cdd:COG1579 182 RIRK 185
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
641-804 |
3.45e-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: 47.74 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 641 EETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSM---TSQKSFQQLTMEKEQALADLNSVERSLSDL---FRRYENLKGVL 714
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 715 EGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR----------TKAKAESAALHAGLRKEQMK 784
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrealDELRAELTLLNEEAANLRER 825
|
170 180
....*....|....*....|
gi 1209185250 785 VESLERALQQKNQEIEELTK 804
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEE 845
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
632-789 |
4.39e-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: 45.44 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 632 EANEWKKKYEET----RQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS-DLFRR 706
Cdd:pfam04012 12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELArEALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 707 YENLKGVLEGFKKN-------EEALKKCAQDYLARVKQEEQRYQALKihAEEKLDKANEEIAQVRTKAKAESAAlhAGLR 779
Cdd:pfam04012 92 KKSLEKQAEALETQlaqqrsaVEQLRKQLAALETKIQQLKAKKNLLK--ARLKAAKAQEAVQTSLGSLSTSSAT--DSFE 167
|
170
....*....|
gi 1209185250 780 KEQMKVESLE 789
Cdd:pfam04012 168 RIEEKIEERE 177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
632-808 |
5.52e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 632 EANEWKKKYEETRQEVLEMRKiVAEYEKTIAQMIEDEQrtsmtsQKSFQQLTMEKEQALADlnsvERSLSDLFRRYENLK 711
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEA------EAAADEAEAAEEKAEAA----EKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 712 GVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRK---EQMKVESL 788
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEA 1462
|
170 180
....*....|....*....|
gi 1209185250 789 ERALQQKnQEIEELTKICDE 808
Cdd:PTZ00121 1463 KKKAEEA-KKADEAKKKAEE 1481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
632-809 |
6.41e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 632 EANEW-KKKYEETRQEVLEMRKIVAEYeKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALADLNSVERSLSDLFRRYENL 710
Cdd:COG3206 175 KALEFlEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 711 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 783
Cdd:COG3206 253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327
|
170 180
....*....|....*....|....*.
gi 1209185250 784 KVESLERALQQKNQEIEELTKICDEL 809
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAEL 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
637-804 |
7.52e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 637 KKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 716
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 717 FKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKN 796
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
....*...
gi 1209185250 797 QEIEELTK 804
Cdd:COG4372 164 EELAALEQ 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
620-815 |
2.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 620 TLIREEIITKEIEanEWKKKYEETRQEVLEMRKivAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVE 697
Cdd:PRK03918 494 ELIKLKELAEQLK--ELEEKLKKYNLEELEKKA--EEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 698 RSLSDLFRRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESA 772
Cdd:PRK03918 570 EELAELLKELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1209185250 773 AL-----------HAGLRKEQMKvesLERALQQKNQEIEELTKICDELIAKLGK 815
Cdd:PRK03918 648 ELeelekkyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
623-814 |
2.17e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 623 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IED-EQRTSM----TSQKSFQQLTMEKEQALADLN 694
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeeaLNDlEARLSHsripEIQAELSKLEEEVSRIEARLR 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 695 SVERSLSDLfrryENLKGVLEGFKKNEEALKKCAQDylaRVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAesaal 774
Cdd:TIGR02169 816 EIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESR----- 883
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1209185250 775 HAGLRKEQMKVES----LERALQQKNQEIEELTKICDELIAKLG 814
Cdd:TIGR02169 884 LGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
638-808 |
2.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 638 KKYEETRQEVLEMRKivAEYEKTIAQMIE-DEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 716
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKK--AEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 717 FKKNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKN 796
Cdd:PTZ00121 1308 KKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAK 1377
|
170
....*....|..
gi 1209185250 797 QEIEELTKICDE 808
Cdd:PTZ00121 1378 KKADAAKKKAEE 1389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
624-815 |
3.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 624 EEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDL 703
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 704 FRRYENLKGVLEGFKKNEEALKK-------CAQ--------DYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAK 768
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvCGRelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1209185250 769 AESAALHagLRKEQMKVESLERALQQKN-QEIEELTKICDELIAKLGK 815
Cdd:PRK03918 491 KESELIK--LKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
612-801 |
5.43e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 612 ESDKTAVLTLIREEIITKEIEAnewkKKYEETRQEVLEMRKivAEYEKtiaQMIEDEQRTSMTSQKSFQQLTMEKEQALA 691
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKK--AEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 692 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLA----RVKQEEQRYQALKIHAEEKLDKANEEIAQVRT-- 765
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAee 1741
|
170 180 190
....*....|....*....|....*....|....*..
gi 1209185250 766 -KAKAESAALHAGlrkEQMKVESLERALQQKNQEIEE 801
Cdd:PTZ00121 1742 dKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRK 1775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
622-729 |
1.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 622 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 701
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100
....*....|....*....|....*...
gi 1209185250 702 DLFRRYENLKGVLEGFKKNEEALKKCAQ 729
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
708-812 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 708 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 784
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 1209185250 785 VESLERALQQKNQEIEELTKICDELIAK 812
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
612-813 |
1.28e-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: 42.65 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 612 ESDKTAVLTLIREEIITKEIEANEWKKKYEETRQ----EVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQL--TME 685
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLkeklELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkqEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 686 KEQALADLNSVERSLSdlfrryenlkgvlEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrt 765
Cdd:pfam02463 262 KEEEKLAQVLKENKEE-------------EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK--- 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1209185250 766 KAKAESAALHAGLRKEQMKvESLERALQQKNQEIEELTKICDELIAKL 813
Cdd:pfam02463 326 AEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLE 372
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
680-813 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 680 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 745
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185250 746 -----KIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 813
Cdd:COG1579 100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
632-798 |
2.18e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 632 EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAladlnsveRSLSDLFRRYENLK 711
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 712 GVLEGFKKNEEALKKCAQdylARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAALHAGLRK--EQMKVESLE 789
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKadELKKAEELK 1558
|
....*....
gi 1209185250 790 RALQQKNQE 798
Cdd:PTZ00121 1559 KAEEKKKAE 1567
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
623-816 |
2.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 623 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSmTSQKSFQqltmEKEQALADLNSVERSLSD 702
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK-EKEKELE----EVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 703 -------LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKA--ESAA 773
Cdd:PRK03918 222 eleklekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEyiKLSE 300
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1209185250 774 LHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 816
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
613-782 |
2.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 613 SDKTAVLTLIREEIITKEI-EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMieDEQRTSMTSQKSFQQLTMEKEQALA 691
Cdd:COG4717 62 QGRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 692 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KIHAEEKLDKAN 757
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 1209185250 758 EEIAQVRTKAKAESAALHAGLRKEQ 782
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
683-813 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 683 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKI---HAEEKLDKANE 758
Cdd:COG1579 1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1209185250 759 EIAQVRTkAKAESAALH--AGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 813
Cdd:COG1579 81 QLGNVRN-NKEYEALQKeiESLKRRI---SDLEDEILELMERIEELEEELAELEAEL 133
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
624-804 |
3.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 624 EEIITKEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 701
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 702 DLFRRYENLKGVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKE 781
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
170 180
....*....|....*....|...
gi 1209185250 782 QMKVESLERALQQKNQEIEELTK 804
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
685-817 |
3.77e-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: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 685 EKEQALA-DLNSVERSLSDLFRRYENLKGVL-EGFKKNEEALKKC--AQDYLARVKQEEQRYQALKIHAEEKLDKANEEI 760
Cdd:TIGR02169 674 AELQRLReRLEGLKRELSSLQSELRRIENRLdELSQELSDASRKIgeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209185250 761 AQVRTKAK---AESAALHAGLRKEQMKVESLERAL-----QQKNQEIEELTKICDELIAKLGKTD 817
Cdd:TIGR02169 754 ENVKSELKeleARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIE 818
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
623-791 |
4.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 623 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ--KSFQQLTMEKEQALADLNSVERSL 700
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEeiNGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 701 SDLFRRYENLKGVLEGFkknEEALKKCAQdyLARVKQEEQRYQALKIHAE-EKLDKANEEIAQVRTKAKAESAALHaGLR 779
Cdd:PRK03918 348 KELEKRLEELEERHELY---EEAKAKKEE--LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELK-KEI 421
|
170
....*....|...
gi 1209185250 780 KEQMK-VESLERA 791
Cdd:PRK03918 422 KELKKaIEELKKA 434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
629-774 |
4.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 629 KEIEAN-EWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedeqrtsmtsqksfqqltmeKEQALadlnsvERSLSDLFRRY 707
Cdd:PRK12704 58 ALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQ----------------------KEENL------DRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185250 708 ENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQAL-KIHAEEkldkANEEI-AQVRTKAKAESAAL 774
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEE----AKEILlEKVEEEARHEAAVL 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
605-805 |
4.78e-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: 40.48 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 605 LDGICLSESDKTAVLTLIREEIITKEIEANEWKKK----YEETRQEV----LEMR-KIVAEYEKTiaQMIEDEQRTSMTS 675
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKmilaFEELRVQAenarLEMHfKLKEDHEKI--QHLEEEYKKEIND 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 676 QKSFQQLTM----EKEQALADLNSVERSLSDLFRRYEnlkgvlEGFKKNEEALKKC--AQDYLAR----VKQEEQRYQAL 745
Cdd:pfam05483 238 KEKQVSLLLiqitEKENKMKDLTFLLEESRDKANQLE------EKTKLQDENLKELieKKDHLTKeledIKMSLQRSMST 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 746 KIHAEEKLDKANEEIAQ---------------------VRTKAKAESAALHAGLRKEQMKVES-------LERALQQKNQ 797
Cdd:pfam05483 312 QKALEEDLQIATKTICQlteekeaqmeelnkakaahsfVVTEFEATTCSLEELLRTEQQRLEKnedqlkiITMELQKKSS 391
|
....*...
gi 1209185250 798 EIEELTKI 805
Cdd:pfam05483 392 ELEEMTKF 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
602-815 |
4.99e-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: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 602 ESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAqmiedeqrtsmtsqksfqq 681
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 682 ltmEKEQALADLnsvERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKihaeEKLDKANEEIA 761
Cdd:TIGR02169 872 ---ELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELK----AKLEALEEELS 934
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185250 762 QVRTKAKA--ESAALHAGLRKEQMKVESLERALQQKN-------QEIEELTKICDELIAKLGK 815
Cdd:TIGR02169 935 EIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-777 |
5.45e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 619 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTS-------MTSQKSF------------ 679
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFldavrrlqylky 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 680 -----QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLD 754
Cdd:COG4942 144 laparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180
....*....|....*....|...
gi 1209185250 755 KANEEIAQVRTKAKAESAALHAG 777
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
613-801 |
6.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 613 SDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIE--DEQRTSMTSQKSFQQLTMEKEQAL 690
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeiEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185250 691 ADLNSVErSLSDLFRRYENLKGVLEGfkkneealkkcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---- 766
Cdd:COG3883 106 DVLLGSE-SFSDFLDRLSALSKIADA-----------DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkael 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1209185250 767 --AKAESAALHAGLRKEQMKVESLERALQQKNQEIEE 801
Cdd:COG3883 174 eaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| |
