|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
592-798 |
2.91e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 592 LSKIRQNLKEKHARhIADLRAYY---ESEINSLKQKLEA--KEISGVEDWKitnQILVDRCGQLDSALHEATSRVRTLEN 666
Cdd:TIGR02168 255 LEELTAELQELEEK-LEELRLEVselEEEIEELQKELYAlaNEISRLEQQK---QILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 667 KNNLLEIEVNDLRERFSAassaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQ 746
Cdd:TIGR02168 331 KLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 508083049 747 DLLGEYESLGKEHRRVKDALNT-----TENKLLDAYTQISDLKRMISKLEAQVKQVE 798
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
581-811 |
1.32e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 581 ISLTSlEDPVILSKI---------RQNLKEKHARhIADLRAYYESEINSLKQKLEAKEISgVEDWKITNQI--------- 642
Cdd:COG3206 140 ISYTS-PDPELAAAVanalaeaylEQNLELRREE-ARKALEFLEEQLPELRKELEEAEAA-LEEFRQKNGLvdlseeakl 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 643 LVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKI---------LQERIEEMRTSSKEKDNTIIRL 713
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqlraqlaeLEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 714 KSRLQDLeeafenayklsddkEAQLKQE-NKMFQDLLGEYESLGKEHRRVKDALNTTENKLL---DAYTQISDLKRmisk 789
Cdd:COG3206 297 RAQIAAL--------------RAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLER---- 358
|
250 260
....*....|....*....|..
gi 508083049 790 lEAQVKQVEHENMLSLRHNSRI 811
Cdd:COG3206 359 -EVEVARELYESLLQRLEEARL 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
594-800 |
3.25e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 594 KIRQNLKEKHARHIADLRAYYESEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEI 673
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 674 EVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYE 753
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 508083049 754 SLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
616-811 |
4.06e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 616 SEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQER 695
Cdd:TIGR04523 162 NDLKKQKEELENELNL-LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 696 IEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKE-----HRRVKDALNTTE 770
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQE 320
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 508083049 771 NKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLRHNSRI 811
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
654-800 |
4.95e-07 |
|
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: 52.23 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 654 LHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKlsdd 733
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 508083049 734 keaqlkqeNKMFQDLLGEYESLGKEhrrvkdaLNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:COG1579 88 --------NKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
592-798 |
9.69e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 592 LSKIRQNLKEKhARHIADLRAYYESEINSLKQKLEAKEISGVEDWKITNQI--LVDRCGQLDSALHEATSRVRTLENKNN 669
Cdd:TIGR02168 714 LEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeLEERLEEAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 670 LLEIEVNDLRERFSAASSASKIL-------QERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQEN 742
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 508083049 743 KMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVE 798
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
591-803 |
4.59e-06 |
|
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: 51.22 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 591 ILSKIRQNLKEKHARHIADLrAYYESEINSLKQKLEAKEIS-GVEDWK-ITNQI--LVDRCGQLDSALHEATSRVRTLEN 666
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEARlSHSRIPeIQAELskLEEEVSRIEARLREIEQKLNRLTL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 667 KNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQ 746
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 747 DLLGEYESLGKEHRRVKDALNTTENKL---LDAYTQIS----------DLKRMISKLEAQVKQVEHENML 803
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELseiEDPKGEDEeipeeelsleDVQAELQRVEEEIRALEPVNML 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
615-773 |
7.03e-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: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 615 ESEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQE 694
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508083049 695 RIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTENKL 773
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-797 |
8.83e-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: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 596 RQNLKEKHARHIADLRAYYESEINSLKQKLE--AKEISGVEDWKITNQILVDrcgQLDSALHEATSRVRTLENKNNLLEI 673
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEeaEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 674 EVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFEnayKLSDDKEAQLKQENKMFQDL---LG 750
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE---ELESELEALLNERASLEEALallRS 894
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 508083049 751 EYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQV 797
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
617-793 |
1.99e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 617 EINSLKQKLEAKEiSGVEDWkitnQILVDRCGQLDSALHEATSRVRTLENKNNLLE--IEVNDLRERFSAASSASKILQE 694
Cdd:COG4717 72 ELKELEEELKEAE-EKEEEY----AELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 695 RIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQEnkmFQDLLGEYESLGKEHRRVKDALNTTENKLL 774
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*....
gi 508083049 775 DAYTQISDLKRMISKLEAQ 793
Cdd:COG4717 224 ELEEELEQLENELEAAALE 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
614-800 |
2.14e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 614 YESEINSLKQKLEAKEISGVEDwKITNQilVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRerfSAASSASKILQ 693
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKS-ELKNQ--EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 694 ERIEEMRTSSKEKD---NTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTE 770
Cdd:TIGR04523 367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190
....*....|....*....|....*....|
gi 508083049 771 NKLLDAYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
600-798 |
2.66e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 600 KEKHARHIADLRAYYESEINSLKQKLEAK-EISGVEDwkitnqiLVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDL 678
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKrRIERLEK-------FIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 679 RERFSAASSASKILQ---ERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMfQDLLGEYESL 755
Cdd:PRK03918 220 REELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKL 298
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 508083049 756 GKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVE 798
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
592-796 |
5.00e-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: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 592 LSKIRQNLKEkharhIADLRAYYESEINSLKQKLEA--------KEISGVEDWKITNQI--LVDRCGQLDSALHEATSRV 661
Cdd:TIGR02168 181 LERTRENLDR-----LEDILNELERQLKSLERQAEKaerykelkAELRELELALLVLRLeeLREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 662 RTLENKNNLLEIEVNDLRERFSAassaskiLQERIEEMRTSSKEKDNTIIRLKSRLQ--------------DLEEAFENA 727
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQilrerlanlerqleELEAQLEEL 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508083049 728 YKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQ 796
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
617-800 |
5.35e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 617 EINSLKQKLEAKEISG-VEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAassaskiLQER 695
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK-------LKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 696 IEEMRTSSKEKDNTIIRLKSRLQDLEEAFE------NAYKLS-DDKEAQLKQENkmFQDLLGEYESLGKEHRRVKDALNT 768
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEeleedlHKLEEAlNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190
....*....|....*....|....*....|....*....
gi 508083049 769 TENKLLD-------AYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:TIGR02169 817 IEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKE 855
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
586-800 |
1.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 586 LEDPVILSKIRQnLKEkharHIADLRAYYEsEINSLKQKLEA-KEIsgVEDWK--ITNQILVDRCGQLDSALH--EATSR 660
Cdd:COG4913 218 LEEPDTFEAADA-LVE----HFDDLERAHE-ALEDAREQIELlEPI--RELAEryAAARERLAELEYLRAALRlwFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 661 VRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTS-SKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLK 739
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508083049 740 QENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRmisKLEAQVKQVEHE 800
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAE 427
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
608-776 |
1.47e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 608 ADLRAYYE-----SEINSLKQKLEA--KEISGVEDwKITnqilvdrcgQLDSALHEATSRVRTLENKNNLLEIEVNDLRE 680
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKElpAELAELED-ELA---------ALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 681 RFsaassasKILQERIEEMRTS------SKEKDNtiirLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYES 754
Cdd:COG1579 74 RI-------KKYEEQLGNVRNNkeyealQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
170 180
....*....|....*....|..
gi 508083049 755 LGKEHRRVKDALNTTENKLLDA 776
Cdd:COG1579 143 KKAELDEELAELEAELEELEAE 164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-806 |
3.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 583 LTSLEDpvILSKIRQNLK--EKHARhIAdlRAYYEseinsLKQKLEAKEISGvedWKITNQILVDRCGQLDSALHEATSR 660
Cdd:COG1196 188 LERLED--ILGELERQLEplERQAE-KA--ERYRE-----LKEELKELEAEL---LLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 661 VRTLENKNNLLEIEVNDLRERFSAassaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQ 740
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508083049 741 ENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLR 806
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
686-800 |
3.25e-04 |
|
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: 45.05 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 686 SSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKmfqdllgEYESLGKEHRRVKDA 765
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-------DLARLEAEVEQLEER 748
|
90 100 110
....*....|....*....|....*....|....*
gi 508083049 766 LNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
591-798 |
4.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 591 ILSKIRQNLKE-----KHARHIADLRAYYEsEINSLKQKLEAKEISGVE----DWKITNQILVDRCGQLdSALHEATSRV 661
Cdd:PRK03918 474 KERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEkkaeEYEKLKEKLIKLKGEI-KSLKKELEKL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 662 RTLENKNNLLEIEVNDLRERFSA--------ASSASKILQERIEEMR----------TSSKEKDNTIIRLKSRLQDLEEA 723
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 724 FENAYKLSDD---KEAQLKQENKMFQD-----LLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVK 795
Cdd:PRK03918 632 FEELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
...
gi 508083049 796 QVE 798
Cdd:PRK03918 712 ELE 714
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
591-755 |
4.65e-04 |
|
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: 42.99 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 591 ILSKIRQ--NLKEKHARHIADLrayyESEINSLKQKLEAKEISgVEDwkitnqiLVDRCGQLDSALHEATSRVRTLEN-- 666
Cdd:COG1579 15 LDSELDRleHRLKELPAELAEL----EDELAALEARLEAAKTE-LED-------LEKEIKRLELEIEEVEARIKKYEEql 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 667 ---KNN----LLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLK 739
Cdd:COG1579 83 gnvRNNkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|.
gi 508083049 740 QE-----NKMFQDLLGEYESL 755
Cdd:COG1579 163 AEreelaAKIPPELLALYERI 183
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
618-790 |
6.59e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 618 INSLKQKLEAKEISGVedwkiTNQILVD----RCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQ 693
Cdd:pfam10174 326 IEVLKESLTAKEQRAA-----ILQTEVDalrlRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 694 ERIEEMRTSSKEKDNTIIRLKSRLQDLEE----------AFENAykLSDDK---EAQLKQENKMFQDLLGEYESLGKEHR 760
Cdd:pfam10174 401 KKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LSEKEriiERLKEQREREDRERLEELESLKKENK 478
|
170 180 190
....*....|....*....|....*....|
gi 508083049 761 RVKDALNTTENKLLDAYTQISDLKRMISKL 790
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSL 508
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
626-806 |
6.82e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 626 EAKEISGVEDWKITNQI--LVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERfsaASSASKILQERIEEMRTSS 703
Cdd:COG1340 1 SKTDELSSSLEELEEKIeeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE---AQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 704 KEKDNTIIRLKSRLQDLEEAFENAYKLSDDK------EAQLKQENKMFQ----------DLLGEYESLGKEHRRVKDALN 767
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGgsidklRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKKALE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 508083049 768 tTENKLLDAYTQISDLKRMISKLEAQVK------QVEHENMLSLR 806
Cdd:COG1340 158 -KNEKLKELRAELKELRKEAEEIHKKIKelaeeaQELHEEMIELY 201
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
674-801 |
7.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 674 EVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQEN-------KMFQ 746
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqEELE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 508083049 747 DLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHEN 801
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
660-741 |
7.25e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 660 RVRTLENKNNLLEIEVNDLRERFSAASSASKILQER-IEEMR----TSSKEKDNTIIRLKSrLQDLEEAFENAYklsdDK 734
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeIEDLRrqldTLTVERARLQLELDN-LRLAAEDFRQKY----ED 93
|
....*..
gi 508083049 735 EAQLKQE 741
Cdd:pfam00038 94 ELNLRTS 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-800 |
1.06e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 592 LSKIRQNLKEKHARHIADLRAYyESEINSLKQKLEAKEisgvedwkitnqilvDRCGQLDSALHEATSRVRTLENKNNLL 671
Cdd:COG1196 244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELE---------------LELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 672 EIEVNDLRERF-----SAASSASKI--LQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKM 744
Cdd:COG1196 308 EERRRELEERLeeleeELAELEEELeeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 508083049 745 FQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
593-800 |
1.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 593 SKIRQNLKEKHARHIADLRayyesEINSLKQKLE--AKEISGVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNL 670
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLR-----EINEISSELPelREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 671 LEIEVNDLRERFSAASSASKILQE---------RIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQE 741
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 508083049 742 NKMFQDLLGEYESLGKEHRRVKDALNTTEN-----KLLDAYTqISDLKRMISKLEAQVKQVEHE 800
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEElerlkKRLTGLT-PEKLEKELEELEKAKEEIEEE 406
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
615-796 |
1.53e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 615 ESEINSLKQKLEA--KEISGVEDwkiTNQilvdrcgQLDSALHEATSRVRTLENKNNL-------LEIEVNDLRERFSAA 685
Cdd:TIGR04523 334 NKIISQLNEQISQlkKELTNSES---ENS-------EKQRELEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQNQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 686 SSASKILQERIEEMRTSSKEKD-------NTIIRLKSRLQDLEE---AFENAYKLSDDKEAQLKQENKmfqDLLGEYESL 755
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEkeierlkETIIKNNSEIKDLTNqdsVKELIIKNLDNTRESLETQLK---VLSRSINKI 480
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 508083049 756 GKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQ 796
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-751 |
2.33e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 596 RQNLKEKHARHIADLRAYYESEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEAtsRVRTLENKNNLLEIEV 675
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEEL 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508083049 676 NDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKM--FQDLLGE 751
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSE 527
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
615-800 |
2.75e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.27 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 615 ESEINSLKQKLEAKEiSGVEDWKITNQILVDRCGQLDSALHeatsrvrTLENKNNLL-------EIEVNDLRERFsaass 687
Cdd:pfam15619 10 LHKIKELQNELAELQ-SKLEELRKENRLLKRLQKRQEKALG-------KYEGTESELpqliarhNEEVRVLRERL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 688 asKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEeafenayKLSDDK---------------EAQLKQENKMFQDLLGEY 752
Cdd:pfam15619 77 --RRLQEKERDLERKLKEKEAELLRLRDQLKRLE-------KLSEDKnlaereelqkkleqlEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 508083049 753 ESLGKEHRRvkdALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 800
Cdd:pfam15619 148 ELENKSFRR---QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
664-809 |
2.88e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 664 LENKNNLLEIEVNDLRERFSAASSaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKlsdDKEAQLKQENK 743
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNS----IKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK---EKLKKLLQEIM 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 508083049 744 MFQDLLGEyesLGKEHRRVKDALNTTENKLLDAYTQISDLKRM-----------ISKLEAQVKQVEHENMLSLRHNS 809
Cdd:smart00787 222 IKVKKLEE---LEEELQELESKIEDLTNKKSELNTEIAEAEKKleqcrgftfkeIEKLKEQLKLLQSLTGWKITKLS 295
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
645-796 |
2.88e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 645 DRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRtssKEKDNTIIRLKSRLQDLEEAF 724
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR---EERDELREREAELEATLRTAR 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508083049 725 ENAyklsdDKEAQLKQENK---MFQDLLGEYESLGKEHRRVKDAlnTTENKLLDAYTQISDLKRMISKLEAQVKQ 796
Cdd:PRK02224 440 ERV-----EEAEALLEAGKcpeCGQPVEGSPHVETIEEDRERVE--ELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
591-837 |
3.00e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 591 ILSKIRQNLkEKHARHIADLRAYyeSEINSLKQKLEAKEISGveDWKITNQILVDRCGQLDSA---LHEATSRVRTLENK 667
Cdd:TIGR02169 192 IIDEKRQQL-ERLRREREKAERY--QALLKEKREYEGYELLK--EKEALERQKEAIERQLASLeeeLEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 668 NNLLEIEVNDLRERFSAASSASKI-LQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQ 746
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 747 DLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLRHNSRIHVRPSRantlATSDV 826
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR----LSEEL 422
|
250
....*....|.
gi 508083049 827 SRRKWLIPGAE 837
Cdd:TIGR02169 423 ADLNAAIAGIE 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
651-798 |
3.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 651 DSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFEN---- 726
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 727 AYK--LSDDKEAQLkQENKMFQDLLGEYESLGKEHRRVKDALNTT-------ENKLLDAYTQISDLKRMISKLEAQVKQV 797
Cdd:COG3883 95 LYRsgGSVSYLDVL-LGSESFSDFLDRLSALSKIADADADLLEELkadkaelEAKKAELEAKLAELEALKAELEAAKAEL 173
|
.
gi 508083049 798 E 798
Cdd:COG3883 174 E 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
607-773 |
4.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 607 IADLR---AYYESEINSLKQKL-EAKEIsgVEDWKITNQILVDRCGqLDSALHEATS-RVRTLENKNNLLEIEVNDLRER 681
Cdd:PRK02224 260 IEDLRetiAETEREREELAEEVrDLRER--LEELEEERDDLLAEAG-LDDADAEAVEaRREELEDRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 682 FSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDL---LGEYESLGKE 758
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdLGNAEDFLEE 416
|
170
....*....|....*
gi 508083049 759 HRRVKDALNTTENKL 773
Cdd:PRK02224 417 LREERDELREREAEL 431
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
690-814 |
5.17e-03 |
|
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: 39.66 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 690 KILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEafenayKLSDDKEAQLKQENKMFQDLLGEYESLGKEH-RRVKDALNT 768
Cdd:pfam04012 25 KMLEQAIRDMQSELVKARQALAQTIARQKQLER------RLEQQTEQAKKLEEKAQAALTKGNEELAREAlAEKKSLEKQ 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 508083049 769 TENK---LLDAYTQISDLKRMISKLEAQVKQVEHE-NMLSLRHNSRIHVR 814
Cdd:pfam04012 99 AEALetqLAQQRSAVEQLRKQLAALETKIQQLKAKkNLLKARLKAAKAQE 148
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
583-763 |
6.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 583 LTSLEDPVILSKIRQNLKEKHARHIADLRAYYESEINSLKQKLEAKEIS------GVEDwkitNQILVDRCGQLDsALHE 656
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeaGVED----EEELRAALEQAE-EYQE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 657 ATSRVRTLENKNNLLEIEVNDLRERFSAASsaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAykLSDDKEA 736
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQL--EEDGELA 472
|
170 180
....*....|....*....|....*..
gi 508083049 737 QLKQEnkmFQDLLGEYESLGKEHRRVK 763
Cdd:COG4717 473 ELLQE---LEELKAELRELAEEWAALK 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-801 |
7.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 657 ATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSkEKDNTIIRLKS---RLQDLEEAFENAyKLSDD 733
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASaerEIAELEAELERL-DASSD 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508083049 734 KEAQLKQEnkmFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHEN 801
Cdd:COG4913 686 DLAALEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
649-798 |
7.51e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 649 QLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNtiiRLKSRLQDL-------- 720
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERARALyrsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 721 -EEAFENAYKLSD--DKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALnttENKLLDAYTQISDLKRMISKLEAQVKQV 797
Cdd:COG3883 104 yLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQAEQ 180
|
.
gi 508083049 798 E 798
Cdd:COG3883 181 E 181
|
|
| DUF4472 |
pfam14739 |
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ... |
635-726 |
9.14e-03 |
|
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.
Pssm-ID: 464291 [Multi-domain] Cd Length: 107 Bit Score: 37.28 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508083049 635 DWKITNQILVDrcgQLDSALHEATSRVRTLEnkNNLLEIEVNDLRERFSAASsaskiLQERIEEMRTSSKEKDNTIIRLK 714
Cdd:pfam14739 14 DLQIENNKLRE---QYEAEKFELKNKLLNLE--NRVLELELRLEKAAEEIQD-----LRERLRELEDDRRELAEEFVALK 83
|
90
....*....|..
gi 508083049 715 SRLQDLEEAFEN 726
Cdd:pfam14739 84 KNYQALSKELEA 95
|
|
| |
