|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-731 |
3.99e-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: 61.23 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 525 LSKIRQNLKEKHARhIADLRAYY---ESEINSLKQKLEA--KEISGVEDWKitnQILVDRCGQLDSALHEATSRVRTLEN 599
Cdd:TIGR02168 255 LEELTAELQELEEK-LEELRLEVselEEEIEELQKELYAlaNEISRLEQQK---QILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 600 KNNLLEIEVNDLRERFSAassaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQ 679
Cdd:TIGR02168 331 KLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462529254 680 DLLGEYESLGKEHRRVKDALNT-----TENKLLDAYTQISDLKRMISKLEAQVKQVE 731
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
514-744 |
1.44e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 514 ISLTSlEDPVILSKI---------RQNLKEKHARhIADLRAYYESEINSLKQKLEAKEISgVEDWKITNQI--------- 575
Cdd:COG3206 140 ISYTS-PDPELAAAVanalaeaylEQNLELRREE-ARKALEFLEEQLPELRKELEEAEAA-LEEFRQKNGLvdlseeakl 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 576 LVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKI---------LQERIEEMRTSSKEKDNTIIRL 646
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqlraqlaeLEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 647 KSRLQDLeeafenayklsddkEAQLKQE-NKMFQDLLGEYESLGKEHRRVKDALNTTENKLL---DAYTQISDLKRmisk 722
Cdd:COG3206 297 RAQIAAL--------------RAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLER---- 358
|
250 260
....*....|....*....|..
gi 2462529254 723 lEAQVKQVEHENMLSLRHNSRI 744
Cdd:COG3206 359 -EVEVARELYESLLQRLEEARL 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
527-733 |
3.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 527 KIRQNLKEKHARHIADLRAYYESEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEI 606
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 607 EVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYE 686
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462529254 687 SLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
549-744 |
5.84e-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: 53.87 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 549 SEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQER 628
Cdd:TIGR04523 162 NDLKKQKEELENELNL-LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 629 IEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKE-----HRRVKDALNTTE 703
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQE 320
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462529254 704 NKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLRHNSRI 744
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
587-733 |
8.36e-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: 51.46 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 587 LHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKlsdd 666
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462529254 667 keaqlkqeNKMFQDLLGEYESLGKEhrrvkdaLNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:COG1579 88 --------NKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-731 |
1.30e-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: 52.75 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 525 LSKIRQNLKEKhARHIADLRAYYESEINSLKQKLEAKEISGVEDWKITNQI--LVDRCGQLDSALHEATSRVRTLENKNN 602
Cdd:TIGR02168 714 LEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeLEERLEEAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 603 LLEIEVNDLRERFSAASSASKIL-------QERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQEN 675
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462529254 676 KMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVE 731
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
524-736 |
6.11e-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: 50.45 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 524 ILSKIRQNLKEKHARHIADLrAYYESEINSLKQKLEAKEIS-GVEDWK-ITNQI--LVDRCGQLDSALHEATSRVRTLEN 599
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEARlSHSRIPeIQAELskLEEEVSRIEARLREIEQKLNRLTL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 600 KNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQ 679
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 680 DLLGEYESLGKEHRRVKDALNTTENKL---LDAYTQIS----------DLKRMISKLEAQVKQVEHENML 736
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELseiEDPKGEDEeipeeelsleDVQAELQRVEEEIRALEPVNML 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
548-706 |
7.63e-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: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 548 ESEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQE 627
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462529254 628 RIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTENKL 706
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
529-730 |
1.13e-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: 49.67 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 529 RQNLKEKHARHIADLRAYYESEINSLKQKLE--AKEISGVEDWKITNQILVDrcgQLDSALHEATSRVRTLENKNNLLEI 606
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEeaEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 607 EVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFEnayKLSDDKEAQLKQENKMFQDL---LG 683
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE---ELESELEALLNERASLEEALallRS 894
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462529254 684 EYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQV 730
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
550-726 |
2.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 550 EINSLKQKLEAKEiSGVEDWkitnQILVDRCGQLDSALHEATSRVRTLENKNNLLE--IEVNDLRERFSAASSASKILQE 627
Cdd:COG4717 72 ELKELEEELKEAE-EKEEEY----AELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 628 RIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQEnkmFQDLLGEYESLGKEHRRVKDALNTTENKLL 707
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*....
gi 2462529254 708 DAYTQISDLKRMISKLEAQ 726
Cdd:COG4717 224 ELEEELEQLENELEAAALE 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
547-733 |
3.19e-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: 48.09 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 547 YESEINSLKQKLEAKEISGVEDwKITNQilVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRerfSAASSASKILQ 626
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKS-ELKNQ--EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 627 ERIEEMRTSSKEKD---NTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTE 703
Cdd:TIGR04523 367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190
....*....|....*....|....*....|
gi 2462529254 704 NKLLDAYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
533-731 |
3.46e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 533 KEKHARHIADLRAYYESEINSLKQKLEAK-EISGVEDwkitnqiLVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDL 611
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKrRIERLEK-------FIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 612 RERFSAASSASKILQ---ERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMfQDLLGEYESL 688
Cdd:PRK03918 220 REELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKL 298
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462529254 689 GKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVE 731
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-729 |
6.28e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 525 LSKIRQNLKEkharhIADLRAYYESEINSLKQKLEA--------KEISGVEDWKITNQI--LVDRCGQLDSALHEATSRV 594
Cdd:TIGR02168 181 LERTRENLDR-----LEDILNELERQLKSLERQAEKaerykelkAELRELELALLVLRLeeLREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 595 RTLENKNNLLEIEVNDLRERFSAassaskiLQERIEEMRTSSKEKDNTIIRLKSRLQ--------------DLEEAFENA 660
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQilrerlanlerqleELEAQLEEL 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462529254 661 YKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQ 729
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
550-733 |
7.18e-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: 46.98 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 550 EINSLKQKLEAKEISG-VEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAassaskiLQER 628
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK-------LKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 629 IEEMRTSSKEKDNTIIRLKSRLQDLEEAFE------NAYKLS-DDKEAQLKQEnkMFQDLLGEYESLGKEHRRVKDALNT 701
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEeleedlHKLEEAlNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462529254 702 TENKLLD-------AYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:TIGR02169 817 IEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKE 855
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-733 |
1.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 519 LEDPVILSKIRQnLKEkharHIADLRAYYEsEINSLKQKLEA-KEIsgVEDWK--ITNQILVDRCGQLDSALH--EATSR 593
Cdd:COG4913 218 LEEPDTFEAADA-LVE----HFDDLERAHE-ALEDAREQIELlEPI--RELAEryAAARERLAELEYLRAALRlwFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 594 VRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTS-SKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLK 672
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462529254 673 QENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRmisKLEAQVKQVEHE 733
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAE 427
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
541-709 |
2.92e-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: 43.76 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 541 ADLRAYYE-----SEINSLKQKLEA--KEISGVEDwKITnqilvdrcgQLDSALHEATSRVRTLENKNNLLEIEVNDLRE 613
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKElpAELAELED-ELA---------ALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 614 RFsaassasKILQERIEEMRTS------SKEKDNtiirLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYES 687
Cdd:COG1579 74 RI-------KKYEEQLGNVRNNkeyealQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
170 180
....*....|....*....|..
gi 2462529254 688 LGKEHRRVKDALNTTENKLLDA 709
Cdd:COG1579 143 KKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-733 |
3.71e-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: 44.66 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 619 SSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKmfqdllgEYESLGKEHRRVKDA 698
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-------DLARLEAEVEQLEER 748
|
90 100 110
....*....|....*....|....*....|....*
gi 2462529254 699 LNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
516-739 |
4.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 516 LTSLEDpvILSKIRQNLK--EKHARhIAdlRAYYEseinsLKQKLEAKEISGvedWKITNQILVDRCGQLDSALHEATSR 593
Cdd:COG1196 188 LERLED--ILGELERQLEplERQAE-KA--ERYRE-----LKEELKELEAEL---LLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 594 VRTLENKNNLLEIEVNDLRERFSAassaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQ 673
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462529254 674 ENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLR 739
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
524-731 |
6.36e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 524 ILSKIRQNLKE-----KHARHIADLRAYYEsEINSLKQKLEAKEISGVE----DWKITNQILVDRCGQLdSALHEATSRV 594
Cdd:PRK03918 474 KERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEkkaeEYEKLKEKLIKLKGEI-KSLKKELEKL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 595 RTLENKNNLLEIEVNDLRERFSA--------ASSASKILQERIEEMR----------TSSKEKDNTIIRLKSRLQDLEEA 656
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 657 FENAYKLSDD---KEAQLKQENKMFQD-----LLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVK 728
Cdd:PRK03918 632 FEELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
...
gi 2462529254 729 QVE 731
Cdd:PRK03918 712 ELE 714
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
551-723 |
8.01e-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: 43.66 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 551 INSLKQKLEAKEISGVedwkiTNQILVD----RCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQ 626
Cdd:pfam10174 326 IEVLKESLTAKEQRAA-----ILQTEVDalrlRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 627 ERIEEMRTSSKEKDNTIIRLKSRLQDLEE----------AFENAykLSDDK---EAQLKQENKMFQDLLGEYESLGKEHR 693
Cdd:pfam10174 401 KKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LSEKEriiERLKEQREREDRERLEELESLKKENK 478
|
170 180 190
....*....|....*....|....*....|
gi 2462529254 694 RVKDALNTTENKLLDAYTQISDLKRMISKL 723
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSL 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
524-688 |
8.07e-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: 42.22 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 524 ILSKIRQ--NLKEKHARHIADLrayyESEINSLKQKLEAKEISgVEDwkitnqiLVDRCGQLDSALHEATSRVRTLEN-- 599
Cdd:COG1579 15 LDSELDRleHRLKELPAELAEL----EDELAALEARLEAAKTE-LED-------LEKEIKRLELEIEEVEARIKKYEEql 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 600 ---KNN----LLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLK 672
Cdd:COG1579 83 gnvRNNkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|.
gi 2462529254 673 QE-----NKMFQDLLGEYESL 688
Cdd:COG1579 163 AEreelaAKIPPELLALYERI 183
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
593-674 |
9.15e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 593 RVRTLENKNNLLEIEVNDLRERFSAASSASKILQER-IEEMR----TSSKEKDNTIIRLKSrLQDLEEAFENAYklsdDK 667
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeIEDLRrqldTLTVERARLQLELDN-LRLAAEDFRQKY----ED 93
|
....*..
gi 2462529254 668 EAQLKQE 674
Cdd:pfam00038 94 ELNLRTS 100
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
607-734 |
1.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 607 EVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQEN-------KMFQ 679
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqEELE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462529254 680 DLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHEN 734
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
559-739 |
1.30e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 559 EAKEISGVEDWKITNQI--LVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERfsaASSASKILQERIEEMRTSS 636
Cdd:COG1340 1 SKTDELSSSLEELEEKIeeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE---AQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 637 KEKDNTIIRLKSRLQDLEEAFENAYKLSDDK------EAQLKQENKMFQ----------DLLGEYESLGKEHRRVKDALN 700
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGgsidklRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKKALE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462529254 701 tTENKLLDAYTQISDLKRMISKLEAQVK------QVEHENMLSLR 739
Cdd:COG1340 158 -KNEKLKELRAELKELRKEAEEIHKKIKelaeeaQELHEEMIELY 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
525-733 |
1.39e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 525 LSKIRQNLKEKHARHIADLRAYyESEINSLKQKLEAKEisgvedwkitnqilvDRCGQLDSALHEATSRVRTLENKNNLL 604
Cdd:COG1196 244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELE---------------LELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 605 EIEVNDLRERF-----SAASSASKI--LQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKM 677
Cdd:COG1196 308 EERRRELEERLeeleeELAELEEELeeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462529254 678 FQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
526-733 |
1.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 526 SKIRQNLKEKHARHIADLRayyesEINSLKQKLE--AKEISGVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNL 603
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLR-----EINEISSELPelREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 604 LEIEVNDLRERFSAASSASKILQE---------RIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQE 674
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462529254 675 NKMFQDLLGEYESLGKEHRRVKDALNTTEN-----KLLDAYTqISDLKRMISKLEAQVKQVEHE 733
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEElerlkKRLTGLT-PEKLEKELEELEKAKEEIEEE 406
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
548-738 |
2.58e-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: 41.93 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 548 ESEINSLKQKLEA--KEISGVEDwkiTNQilvdrcgQLDSALHEATSRVRTLENKNNL-------LEIEVNDLRERFSAA 618
Cdd:TIGR04523 334 NKIISQLNEQISQlkKELTNSES---ENS-------EKQRELEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQNQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 619 SSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDA 698
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462529254 699 LNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSL 738
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
529-684 |
2.86e-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: 41.97 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 529 RQNLKEKHARHIADLRAYYESEINSLKQKLEAKEISgVEDWKITNQILVDRCGQLDSALHEAtsRVRTLENKNNLLEIEV 608
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEEL 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462529254 609 NDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKM--FQDLLGE 684
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSE 527
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
597-742 |
3.15e-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: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 597 LENKNNLLEIEVNDLRERFSAASSaskiLQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKlsdDKEAQLKQENK 676
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNS----IKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK---EKLKKLLQEIM 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462529254 677 MFQDLLGEyesLGKEHRRVKDALNTTENKLLDAYTQISDLKRM-----------ISKLEAQVKQVEHENMLSLRHNS 742
Cdd:smart00787 222 IKVKKLEE---LEEELQELESKIEDLTNKKSELNTEIAEAEKKleqcrgftfkeIEKLKEQLKLLQSLTGWKITKLS 295
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
578-729 |
3.38e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 578 DRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRtssKEKDNTIIRLKSRLQDLEEAF 657
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR---EERDELREREAELEATLRTAR 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462529254 658 ENAyklsdDKEAQLKQENK---MFQDLLGEYESLGKEHRRVKDAlnTTENKLLDAYTQISDLKRMISKLEAQVKQ 729
Cdd:PRK02224 440 ERV-----EEAEALLEAGKcpeCGQPVEGSPHVETIEEDRERVE--ELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
607-733 |
3.91e-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: 39.89 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 607 EVNDLRERFsaassasKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEeafenayKLSDDK---------------EAQL 671
Cdd:pfam15619 68 EVRVLRERL-------RRLQEKERDLERKLKEKEAELLRLRDQLKRLE-------KLSEDKnlaereelqkkleqlEAKL 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462529254 672 KQENKMFQDLLGEYESLGKEHRRvkdALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHE 733
Cdd:pfam15619 134 EDKDEKIQDLERKLELENKSFRR---QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
584-731 |
4.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 584 DSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFEN---- 659
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 660 AYK--LSDDKEAQLkQENKMFQDLLGEYESLGKEHRRVKDALNTT-------ENKLLDAYTQISDLKRMISKLEAQVKQV 730
Cdd:COG3883 95 LYRsgGSVSYLDVL-LGSESFSDFLDRLSALSKIADADADLLEELkadkaelEAKKAELEAKLAELEALKAELEAAKAEL 173
|
.
gi 2462529254 731 E 731
Cdd:COG3883 174 E 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
524-770 |
4.14e-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: 41.21 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 524 ILSKIRQNLkEKHARHIADLRAYyeSEINSLKQKLEAKEISGveDWKITNQILVDRCGQLDSA---LHEATSRVRTLENK 600
Cdd:TIGR02169 192 IIDEKRQQL-ERLRREREKAERY--QALLKEKREYEGYELLK--EKEALERQKEAIERQLASLeeeLEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 601 NNLLEIEVNDLRERFSAASSASKI-LQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQ 679
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 680 DLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLRHNSRIHVRPSRantlATSDV 759
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR----LSEEL 422
|
250
....*....|.
gi 2462529254 760 SRRKWLIPGAE 770
Cdd:TIGR02169 423 ADLNAAIAGIE 433
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
540-706 |
6.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 540 IADLR---AYYESEINSLKQKL-EAKEIsgVEDWKITNQILVDRCGqLDSALHEATS-RVRTLENKNNLLEIEVNDLRER 614
Cdd:PRK02224 260 IEDLRetiAETEREREELAEEVrDLRER--LEELEEERDDLLAEAG-LDDADAEAVEaRREELEDRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 615 FSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDL---LGEYESLGKE 691
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdLGNAEDFLEE 416
|
170
....*....|....*
gi 2462529254 692 HRRVKDALNTTENKL 706
Cdd:PRK02224 417 LREERDELREREAEL 431
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
623-747 |
7.30e-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: 39.28 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 623 KILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEafenayKLSDDKEAQLKQENKMFQDLLGEYESLGKEH-RRVKDALNT 701
Cdd:pfam04012 25 KMLEQAIRDMQSELVKARQALAQTIARQKQLER------RLEQQTEQAKKLEEKAQAALTKGNEELAREAlAEKKSLEKQ 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462529254 702 TENK---LLDAYTQISDLKRMISKLEAQVKQVEHE-NMLSLRHNSRIHVR 747
Cdd:pfam04012 99 AEALetqLAQQRSAVEQLRKQLAALETKIQQLKAKkNLLKARLKAAKAQE 148
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
590-734 |
8.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 590 ATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSkEKDNTIIRLKS---RLQDLEEAFENAyKLSDD 666
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASaerEIAELEAELERL-DASSD 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462529254 667 KEAQLKQEnkmFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHEN 734
Cdd:COG4913 686 DLAALEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
582-731 |
9.51e-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: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 582 QLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNtiiRLKSRLQDL-------- 653
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERARALyrsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529254 654 -EEAFENAYKLSD--DKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALnttENKLLDAYTQISDLKRMISKLEAQVKQV 730
Cdd:COG3883 104 yLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQAEQ 180
|
.
gi 2462529254 731 E 731
Cdd:COG3883 181 E 181
|
|
| |
