|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
551-757 |
1.52e-08 |
|
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: 58.91 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKHARHVADLRAYyESEISALR---QKLEAK-------------DISAVEEWKkknEALVDRCGQLDSALT 614
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQEL-EEKLEELRlevSELEEEieelqkelyalanEISRLEQQK---QILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 615 EATSRVRTLEKKNNLLEIEVSDLRERFNAassaskiLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKE 694
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668249 695 ARLRQENKMFQDLLGEYESLGKEHGRVKDTL-----NMTENKLLDAHTQISDLKRMISKLEAQVKQAE 757
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
573-754 |
4.50e-08 |
|
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: 57.34 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 573 YESEISALRQKLEAKDISAV-EEWKKKNEALVdrcgQLDSALTEATSRVRTLEKKNNLLEIEVSDLRerfNAASSASKIL 651
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELkSELKNQEKKLE----EIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 652 QERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNMT 728
Cdd:TIGR04523 366 EEKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
170 180
....*....|....*....|....*.
gi 1958668249 729 ENKLLDAHTQISDLKRMISKLEAQVK 754
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLK 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-759 |
1.21e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 542 LASLEDpvMLSKIRQNLK--EKHARHVADLRAYyESEISALRQKLEAKDI-SAVEEWKKKNE---ALVDRCGQLDSALTE 615
Cdd:TIGR02168 188 LDRLED--ILNELERQLKslERQAEKAERYKEL-KAELRELELALLVLRLeELREELEELQEelkEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 616 ATSRVRTLEKKNNLLEIEVSDLRERFNAASSA-------SKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAF-ENAY 687
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEisrleqqKQILRERLANLERQLEELEAQLEELESKLDELAEELaELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 688 KLS------DDKEARLRQENKMFQDLLGEYESLGKEHGRVKD-------TLNMTENKLLDAHTQISDLKRMISKLEAQVK 754
Cdd:TIGR02168 345 KLEelkeelESLEAELEELEAELEELESRLEELEEQLETLRSkvaqlelQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
....*
gi 1958668249 755 QAEHE 759
Cdd:TIGR02168 425 ELLKK 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
571-757 |
2.05e-07 |
|
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: 55.07 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 571 AYYESEISALRQKLEA--KDISAVEEWKKKNEALVDrcgQLDSALTEATSRVRTLEKKNNLLEIEVSDLRERFNAASSAS 648
Cdd:TIGR02169 670 RSEPAELQRLRERLEGlkRELSSLQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 649 KILQERIEEMRTSnkekdntITRLKCRLQDLEEAFENAYKLSDDKEARLRQENkmFQDLLGEYESLGKEHGRVKDTLNMT 728
Cdd:TIGR02169 747 SSLEQEIENVKSE-------LKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREI 817
|
170 180
....*....|....*....|....*....
gi 1958668249 729 ENKLLDAHTQISDLKRMISKLEAQVKQAE 757
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
574-765 |
2.19e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 574 ESEISALRQKLEAKdISAVEEWKKKNEALVDRCGQLDSALTEAtsrvrtLEKKNNLLEiEVSDLRERFNAASSASKILQE 653
Cdd:COG1340 21 REEIEELKEKRDEL-NEELKELAEKRDELNAQVKELREEAQEL------REKRDELNE-KVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 654 RIEEMRTSNKEKDN---TITRLKCRLQDLEEAFENAyKLSDDKEARLRQENKMFQDLLGEYESLGKEHgrvkdtlnmteN 730
Cdd:COG1340 93 ELDELRKELAELNKaggSIDKLRKEIERLEWRQQTE-VLSPEEEKELVEKIKELEKELEKAKKALEKN-----------E 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958668249 731 KLLDAHTQISDLKRMISKLEAQVK------QAEHESMLSLR 765
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKelaeeaQELHEEMIELY 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
553-759 |
3.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 553 KIRQNLKEKHARHVADLRAYYESEISALRQKLEAKD------ISAVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKK 626
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEaeleelEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 627 NNLLEIEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQD 706
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958668249 707 LLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
618-761 |
3.73e-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: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 618 SRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARL 697
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958668249 698 RQENKMFQDLLGEYESLGKE-----HGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHESM 761
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
608-759 |
8.21e-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: 51.08 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 608 QLDSALTEATSRVRTLEKknnlleiEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAY 687
Cdd:COG1579 14 ELDSELDRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958668249 688 KlsddkearlrqeNKMFQDLLGEYESLGKEhgrvkdtLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:COG1579 87 N------------NKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
576-762 |
1.13e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 576 EISALRQKLEAKDiSAVEEWKKKNEALVdrcgQLDSALTEATSRVRTLEKKNNLLE--IEVSDLRERFNAASSASKILQE 653
Cdd:COG4717 72 ELKELEEELKEAE-EKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEnkmFQDLLGEYESLGKEHGRVKDTLNMTENKLL 733
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180
....*....|....*....|....*....
gi 1958668249 734 DAHTQISDLKRMISKLEAQVKQAEHESML 762
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
574-759 |
2.44e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 574 ESEISALRQKLEaKDISAVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQE 653
Cdd:TIGR02168 781 EAEIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNMTENKLL 733
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190
....*....|....*....|....*....|....
gi 1958668249 734 DAHTQIS--------DLKRMISKLEAQVKQAEHE 759
Cdd:TIGR02168 940 NLQERLSeeysltleEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
551-732 |
3.39e-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: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKHARHVADLrAYYESEISALRQKLEA-KDISAVEEWKKKN---EALVDRCGQLDSALTEATSRVRTLEKK 626
Cdd:TIGR02169 749 LEQEIENVKSELKELEARI-EELEEDLHKLEEALNDlEARLSHSRIPEIQaelSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 627 NNLLEIEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQD 706
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
170 180
....*....|....*....|....*.
gi 1958668249 707 LLGEYESLGKEHGRVKDTLNMTENKL 732
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
566-730 |
5.15e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 566 VADLRAYYESEISALRQK---LEAkDISAVEEWKKKNEALVD-----RCGQ--LDS----ALTEATSRVRTLEKKNNLLE 631
Cdd:PRK02224 410 AEDFLEELREERDELREReaeLEA-TLRTARERVEEAEALLEagkcpECGQpvEGSphveTIEEDRERVEELEAELEDLE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 632 IEVSDLRERFNAASSASKI-------------LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEAR-- 696
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAedrierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEae 568
|
170 180 190
....*....|....*....|....*....|....*
gi 1958668249 697 -LRQENKMFQDLLGEYESLGKEHGRVKDTLNMTEN 730
Cdd:PRK02224 569 eAREEVAELNSKLAELKERIESLERIRTLLAAIAD 603
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
554-780 |
6.03e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 554 IRQNLKEKHARhVADLRAYYESEISALRQKLEAKDiSAVEEWKKKN---------EALVDRCGQLDSALTEAT------- 617
Cdd:COG3206 162 LEQNLELRREE-ARKALEFLEEQLPELRKELEEAE-AALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARaelaeae 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 618 SRVRTLEKKNNL-----------------------LEIEVSDLRERFNAASSASKILQERIEEMRTS-NKEKDNTITRLK 673
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellqspviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 674 CRLQDLEEAfENAYKlsdDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNMTENKLldahtqisdlkrmiskLEAQV 753
Cdd:COG3206 320 AELEALQAR-EASLQ---AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL----------------EEARL 379
|
250 260
....*....|....*....|....*..
gi 1958668249 754 KQAEHESMLSLRHSAKAPTRPSRANTL 780
Cdd:COG3206 380 AEALTVGNVRVIDPAVVPLKPVSPKKL 406
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
574-772 |
6.64e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 574 ESEISALRQKLEAKDiSAVEEWKKKNEALVDRCGqLDSALTEATS-RVRTLEKKNNLLEIEVSDLRERFNAASSASKILQ 652
Cdd:PRK02224 271 EREREELAEEVRDLR-ERLEELEEERDDLLAEAG-LDDADAEAVEaRREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 653 ERIEEMRTSNKEKDNTITRLKCRLQDLEEAFEnayklsdDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNMTENKL 732
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958668249 733 LDAHTQISDLKRMISKLEAQVKQAEhesmlSLRHSAKAPT 772
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAE-----ALLEAGKCPE 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
551-757 |
6.88e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKE-----KHARHVADLRAYYEsEISALRQKLEAKDISAVEEWKKKNEALVDRCGQLD---SALTEATSRVRT 622
Cdd:PRK03918 475 ERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 623 LEKKNNLLEIEVSDLRERF--------NAASSASKILQERIEEMR----------TSNKEKDNTITRLKCRLQDLEEAFE 684
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 685 NAYKLSDD---KEARLRQENKMFQD-----LLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQA 756
Cdd:PRK03918 634 ELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
.
gi 1958668249 757 E 757
Cdd:PRK03918 714 E 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
574-757 |
8.70e-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: 50.07 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 574 ESEISALRQKLEA---------KDISAVEEWKKKN----EALVDRCGQLDSALTEATSRVRTLEKKNNLLEIEVSDLRER 640
Cdd:TIGR02169 701 ENRLDELSQELSDasrkigeieKEIEQLEQEEEKLkerlEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 641 FNAASSasKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEA-----FENAY--KLSDDKEARLRQENKMFQDLLGEYES 713
Cdd:TIGR02169 781 LNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlnrltLEKEYleKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958668249 714 LGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAE 757
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
577-749 |
1.28e-05 |
|
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: 49.05 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 577 ISALRQKLEAKDISAvEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQERIE 656
Cdd:pfam10174 326 IEVLKESLTAKEQRA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 657 EMRTSNKEKDNTITRLKCRLQDLEE----------AFENAykLSdDKE---ARLR-QENKMFQDLLGEYESLGKEHGRVK 722
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LS-EKEriiERLKeQREREDRERLEELESLKKENKDLK 481
|
170 180
....*....|....*....|....*..
gi 1958668249 723 DTLNMTENKLLDAHTQISDLKRMISKL 749
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSL 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-757 |
1.75e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 567 ADLRAYYESEISALRQKLEAKDiSAVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLLEIEVSDLRERFNAASS 646
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 647 ASKILQERIEEM-----RTSN------------------------------KEKDNTITRLKCRLQDLEEAFENAYKLSD 691
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668249 692 DKEARLRQENKMFQDLLGEYESLGKehgRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAE 757
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
566-756 |
1.83e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 566 VADLRAYYESEISALRQKLEAKDISA-------------VEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLLEI 632
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAqahneeaeslredADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 633 EVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsddkeARLRQENK---MFQDLLG 709
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA--------EALLEAGKcpeCGQPVEG 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958668249 710 E--YESLGKEHGRVKDtlnmTENKLLDAHTQISDLKRMISKLEAQVKQA 756
Cdd:PRK02224 464 SphVETIEEDRERVEE----LEAELEDLEEEVEEVEERLERAEDLVEAE 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
551-714 |
1.92e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEkHARHVADLrayyESEISALRQKLEA--KDISAVEEWKKKNEALVDrcgQLDSALTEATSRVRTLekKNN 628
Cdd:COG1579 19 LDRLEHRLKE-LPAELAEL----EDELAALEARLEAakTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNV--RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 629 ----LLEIEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE---- 700
Cdd:COG1579 89 keyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEreel 168
|
170
....*....|....*
gi 1958668249 701 -NKMFQDLLGEYESL 714
Cdd:COG1579 169 aAKIPPELLALYERI 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-762 |
2.00e-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: 48.90 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 555 RQNLKEKHARHVADLRAYYESEISALRQKLE--AKDISAVEEWKKKNEALVDrcgQLDSALTEATSRVRTLEKKNNLLEI 632
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEeaEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 633 EVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEE-------AFENAYKLSDDKEARLRQENKMFQ 705
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieelesELEALLNERASLEEALALLRSELE 897
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668249 706 DLLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVkqAEHESML 762
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL--SEEYSLT 952
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
559-757 |
3.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 559 KEKHARHVADLRAYYESE--ISALRQKLEAKdISAVEEWKKKNEALVDRCGQLDSALTEATSRVrtlekknNLLEIEVSD 636
Cdd:PRK03918 147 REKVVRQILGLDDYENAYknLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKELEEVLREI-------NEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 637 LRERFNAASSASKILQ---ERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMfQDLLGEYES 713
Cdd:PRK03918 219 LREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIK 297
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958668249 714 LGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAE 757
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
588-760 |
5.52e-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: 47.37 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 588 DISAVEEW-KKKNEALVD------RCGQLDSALTEATSRVRTLEKKNNLLEiEVSDLRERFNAAssASKILQERIEEMRT 660
Cdd:TIGR02169 161 EIAGVAEFdRKKEKALEEleeveeNIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY--EGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 661 SNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLlGEYESLgkehgRVKDtlnmtenKLLDAHTQIS 740
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL-GEEEQL-----RVKE-------KIGELEAEIA 304
|
170 180
....*....|....*....|
gi 1958668249 741 DLKRMISKLEAQVKQAEHES 760
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERL 324
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
574-759 |
1.55e-04 |
|
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: 45.78 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 574 ESEISALRQKLEakdisaveEWKKKNEalvdrcgQLDSalteatsRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQE 653
Cdd:TIGR04523 390 ESQINDLESKIQ--------NQEKLNQ-------QKDE-------QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLgkehgrvkdtlnmtENKLL 733
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL--------------EEKVK 513
|
170 180
....*....|....*....|....*.
gi 1958668249 734 DAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESK 539
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
552-759 |
2.15e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 552 SKIRQNLKEKHARHVADLRAYyeSEISALRQKLEAKdISAVEEWKKKNEALVDRcgqldsaLTEATSRVRTLEKKNNLLE 631
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREI--NEISSELPELREE-LEKLEKEVKELEELKEE-------IEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 632 IEVSDLRERFNAASSASKILQERI----------EEMRTSNKEKDNT---ITRLKCRLQDLEEAFENAYKLSDD---KEA 695
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVkelkelkekaEEYIKLSEFYEEYldeLREIEKRLSRLEEEINGIEERIKEleeKEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668249 696 RLRQENKMFQDLLGEYESLGKEH---GRVKDTL-NMTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHelyEEAKAKKeELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
619-700 |
2.93e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 619 RVRTLEKKNNLLEIEVSDLRERFNAASSASKILQER-IEEMRtsNKEKDNTITRLKCRLQ--DLEEAFENaYKLSDDKEA 695
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeIEDLR--RQLDTLTVERARLQLEldNLRLAAED-FRQKYEDEL 95
|
....*
gi 1958668249 696 RLRQE 700
Cdd:pfam00038 96 NLRTS 100
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
551-782 |
3.02e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKHARHVADLRAYYESEISALRQKLEakdisaveEWKKKNEALVDRCGQLDSALTEATSRVRTLEKknnlL 630
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIE--------RYEEQREQARETRDEADEVLEEHEERREELET----L 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 631 EIEVSDLRERFNAASSASKILQERIEEMR--TSNKEKDNTITRLKCRLQDLE-EAFENAYK-LSDDKEA---RLRQENKM 703
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRerLEELEEERDDLLAEAGLDDADaEAVEARREeLEDRDEElrdRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 704 FQDLLGEYESLGK--------------EHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQA-----EHESMLSL 764
Cdd:PRK02224 337 AQAHNEEAESLREdaddleeraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdlgNAEDFLEE 416
|
250
....*....|....*...
gi 1958668249 765 RHSAKAPTRPSRANTLAT 782
Cdd:PRK02224 417 LREERDELREREAELEAT 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
567-757 |
3.36e-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: 43.37 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 567 ADLRAYYE-----SEISALRQKLEA--KDISAVEewkkknealvDRCGQLDSALTEATSRVRTLEKKNNLLEIEVSDLRE 639
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKElpAELAELE----------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 640 RFnaassasKILQERIEEMRTsNKEKDN---TITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGK 716
Cdd:COG1579 74 RI-------KKYEEQLGNVRN-NKEYEAlqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958668249 717 EhgrvkdtlnmtenklLDAhtQISDLKRMISKLEAQVKQAE 757
Cdd:COG1579 146 E---------------LDE--ELAELEAELEELEAEREELA 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
545-759 |
3.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 545 LEDPVMLSKIRQnLKEkharHVADLRAYYEsEISALRQKLEA-KDIsaVEEWKKKNEAlVDRCGQLDSALteATSRVRTL 623
Cdd:COG4913 218 LEEPDTFEAADA-LVE----HFDDLERAHE-ALEDAREQIELlEPI--RELAERYAAA-RERLAELEYLR--AALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 624 EKKNNLLEIEVSDLRERFNAASSASKILQERIEEMRTS--------NKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEA 695
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREEldeleaqiRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958668249 696 RLRQenkMFQDLLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:COG4913 367 LLAA---LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
550-759 |
3.75e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 550 MLSKIRQNL----KEK-HARHVADLRayyeSEISALRQKLEAKDISAVEEWKKKNEALVDRcgqLDSALTEATSRVRTLE 624
Cdd:TIGR02169 192 IIDEKRQQLerlrREReKAERYQALL----KEKREYEGYELLKEKEALERQKEAIERQLAS---LEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 625 KKNNLLEIEVSDLRERFNAASSASKI-LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKM 703
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668249 704 FQDLLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
645-760 |
4.64e-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: 44.28 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 645 SSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKmfqdllgEYESLGKEHGRVKDT 724
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-------DLARLEAEVEQLEER 748
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958668249 725 LNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHES 760
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
551-750 |
5.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKhARHVADLRAYYEsEISALRQKLEAKDISaVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLL 630
Cdd:PRK03918 209 INEISSELPEL-REELEKLEKEVK-ELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 631 E---------IEVSDLRERFNAA-----------SSASKILQERIEEmRTSNKEKDNTITRLKCRLQDLEEAFENAYKLS 690
Cdd:PRK03918 286 KelkekaeeyIKLSEFYEEYLDElreiekrlsrlEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668249 691 DD---KEARLRQENKMF-----QDLLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLE 750
Cdd:PRK03918 365 EEakaKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
563-763 |
5.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 563 ARHVADLRAYYESEISALRQKLEAKDISAVEEWkkknEALVDRCGQLDSALTEATSRVRTLEKKNnlLEIEVSDLRERFN 642
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLEE--LEQEIAALLAEAG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 643 AASSASkiLQERIEEMRtsnkekdntitrlkcRLQDLEEAFENAyklsddkEARLRQENKMFQDLL--GEYESLGKEHGR 720
Cdd:COG4717 381 VEDEEE--LRAALEQAE---------------EYQELKEELEEL-------EEQLEELLGELEELLeaLDEEELEEELEE 436
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958668249 721 VKDTLNMTENKLLDAHTQISDLkrmisklEAQVKQAEHESMLS 763
Cdd:COG4717 437 LEEELEELEEELEELREELAEL-------EAELEQLEEDGELA 472
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
633-760 |
5.55e-04 |
|
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: 42.20 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 633 EVSDLRERFnaassasKILQERIEEMRTSNKEKDNTITRLKCRLQDLEeafenayKLSDDK---------------EARL 697
Cdd:pfam15619 68 EVRVLRERL-------RRLQEKERDLERKLKEKEAELLRLRDQLKRLE-------KLSEDKnlaereelqkkleqlEAKL 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958668249 698 RQENKMFQDLLGEYESLGKEHGRvkdTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHES 760
Cdd:pfam15619 134 EDKDEKIQDLERKLELENKSFRR---QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
556-759 |
6.01e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 556 QNLKEKHARHVADLRAYYESEISAlRQKLEAKDISAVEEWKKKNEalvdrcgqldsalteatsRVRTLEKKNNLLEievs 635
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAA-RQKLQLEKVTTEAKIKKLEE------------------DILLLEDQNSKLS---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 636 dlRERfnaassasKILQERIEEMRTS---NKEKDNTITRLKCRlqdlEEAfenaykLSDDKEARLRQENKMFQDLlgeye 712
Cdd:pfam01576 152 --KER--------KLLEERISEFTSNlaeEEEKAKSLSKLKNK----HEA------MISDLEERLKKEEKGRQEL----- 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958668249 713 slgkEHGRVKdtlnmTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:pfam01576 207 ----EKAKRK-----LEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-759 |
6.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKHARHVADLRAYyESEISALRQKLEAKDIsAVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLL 630
Cdd:COG1196 244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 631 EIEVSDLRERFNAassaskiLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 710
Cdd:COG1196 322 EEELAELEEELEE-------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958668249 711 YESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAEHE 759
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
542-756 |
6.51e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.05 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 542 LASLEDPVMLSKIrQNLKEKHARHVADLRAYYE--SEISALRQKLEAKDISAVEEWKKKNEALVDRCGQLdsaLTEATSR 619
Cdd:cd00176 23 LSSTDYGDDLESV-EALLKKHEALEAELAAHEErvEALNELGEQLIEEGHPDAEEIQERLEELNQRWEEL---RELAEER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 620 VRTLEkknnlleiEVSDLRERFNAASSASKILQERIEEMRTSNKEKD-NTITRLKCRLQDLEEAFENayklsddKEARLR 698
Cdd:cd00176 99 RQRLE--------EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKHKELEEELEA-------HEPRLK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668249 699 QENKMFQDLLGEYESLGKEHgrvkdtlnmTENKLLDAHTQISDLKRMISKLEAQVKQA 756
Cdd:cd00176 164 SLNELAEELLEEGHPDADEE---------IEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
551-738 |
6.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKHARHVADLRAYyESEISALRQKLEAkdISAVEE--WKKKN-EALVDRCGQLD---SALTEATSRVRTLE 624
Cdd:COG4913 615 LEAELAELEEELAEAEERLEAL-EAELDALQERREA--LQRLAEysWDEIDvASAEREIAELEaelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 625 KKNNLLEIEVSDLRERFNAASSASKILQERIEEMRTSnkekdntITRLKCRLQDLEEAFENAykLSDDKEARLRQEnkMF 704
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-------LDELQDRLEAAEDLARLE--LRALLEERFAAA--LG 760
|
170 180 190
....*....|....*....|....*....|....*
gi 1958668249 705 QDLLGEY-ESLGKEHGRVKDTLNMTENKLLDAHTQ 738
Cdd:COG4913 761 DAVERELrENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
542-755 |
9.92e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 542 LASLEDPVMLSKIRQNLKEKhARHVADLRAYYESEISALRQKLEAKDISA------VEEWKKK-------NEALVDRCGQ 608
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAaeleaeAEEKREAaaeaeeeAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 609 LDSALTEATSRVRTLEKKNNLLEiEVSDLRERFNAassaskiLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENA-- 686
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLA-AIADAEDEIER-------LREKREALAELNDERRERLAEKRERKRELEAEFDEAri 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 687 ------------Y------KLSDDKEAR--LRQENKMFQDLLGEYESLGKEHgrvkDTLNMTENKLLDAHTQISDLKRMI 746
Cdd:PRK02224 649 eearedkeraeeYleqveeKLDELREERddLQAEIGAVENELEELEELRERR----EALENRVEALEALYDEAEELESMY 724
|
....*....
gi 1958668249 747 SKLEAQVKQ 755
Cdd:PRK02224 725 GDLRAELRQ 733
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
610-755 |
1.01e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 610 DSALTEATSRVR------TLEKKNNL-LEIEVSDLRERFNAASSaskiLQERIEEMRTsnkEKDNTITRLKCRLQDLEEA 682
Cdd:PRK09039 52 DSALDRLNSQIAeladllSLERQGNQdLQDSVANLRASLSAAEA----ERSRLQALLA---ELAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958668249 683 FENAYKLSDDKEARLrqenkmfqDLLGE-YESLGKEHGRVKDTLNMTENKLLDAHTQISDL-KRMISKLEAQVKQ 755
Cdd:PRK09039 125 LDSEKQVSARALAQV--------ELLNQqIAALRRQLAALEAALDASEKRDRESQAKIADLgRRLNVALAQRVQE 191
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
590-759 |
1.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 590 SAVEEWKKKNEALVDRCGQLDSALTEatsRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTI 669
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSE---QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 670 TRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKL 749
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170
....*....|
gi 1958668249 750 EAQVKQAEHE 759
Cdd:COG4372 163 QEELAALEQE 172
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
556-749 |
1.32e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 556 QNLKEKHARHVADLRAYYESeISALRQKLEAKDISAVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLLEIEVS 635
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEA-ANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 636 DLRERFNAASSASKILQERIEEMRTSNK-------EKDNTITRLKCRLQDL------EEAFENAYKLS-DDKEARLRQEN 701
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAgaqrkeEEAERKQLQAKlQQTEEELRSLS 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958668249 702 KMFQDLLGEYESLGKEHGRVKDTLNMTENKLLDAHTQISDLKRMISKL 749
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
594-765 |
2.98e-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: 40.77 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 594 EWKKKN-EALVDRcgqLDSALTEATSRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQERIEEMrtsNKEKDNTITRL 672
Cdd:smart00787 136 EWRMKLlEGLKEG---LDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL---EDCDPTELDRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 673 KCRLQDLEEAFENAYKLSDDKEARLRQenkmfqdllgeyeslgkehgrVKDTLNMTENKLLDAHTQISDLKRM------- 745
Cdd:smart00787 210 KEKLKKLLQEIMIKVKKLEELEEELQE---------------------LESKIEDLTNKKSELNTEIAEAEKKleqcrgf 268
|
170 180
....*....|....*....|....
gi 1958668249 746 ----ISKLEAQVKQAEHESMLSLR 765
Cdd:smart00787 269 tfkeIEKLKEQLKLLQSLTGWKIT 292
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
526-661 |
4.44e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 526 QSQLPGTANSVPECIS----------LASLEdpVMLSKIRQNLKEKHARhVADLRAyyesEISALRQKLEAKDISAVEEW 595
Cdd:COG3206 246 RAQLGSGPDALPELLQspviqqlraqLAELE--AELAELSARYTPNHPD-VIALRA----QIAALRAQLQQEAQRILASL 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668249 596 KKKNEALVDRCGQLDSALTEATSRVRTLekknNLLEIEVSDLRERFNAASSASKILQERIEEMRTS 661
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
560-789 |
4.80e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 560 EKHARHVADLRAYYESEISAlrqklEAKDISAVEEWKKKNEAlvdRCGQLDSALTEATSRVRTLEKKNNLLEIEVSDLRE 639
Cdd:pfam01576 853 ERARRQAQQERDELADEIAS-----GASGKSALQDEKRRLEA---RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 640 RFNAASSASKILQERIEEMRTSNKEkdntitrLKCRLQDLEEAFENAYKLSDDK-EARLRQENKMFqdllgEYESlgKEH 718
Cdd:pfam01576 925 ELAAERSTSQKSESARQQLERQNKE-------LKAKLQEMEGTVKSKFKSSIAAlEAKIAQLEEQL-----EQES--RER 990
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958668249 719 GRVKDTLNMTENKLLDAHTQISDLKRMISKLEAQVKQAeHESMLSLRHS-AKAPTRPSRANTlatsdvSRRK 789
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKG-NSRMKQLKRQlEEAEEEASRANA------ARRK 1055
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
551-711 |
5.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 551 LSKIRQNLKEKHARHVADLrayyESEISAL----RQKLEAKDI-SAVEEWKKKNEALVDRCGQLDSALTEATSRVRTLEK 625
Cdd:PRK03918 572 LAELLKELEELGFESVEEL----EERLKELepfyNEYLELKDAeKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 626 KNNLLEIEVSD-----LRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKE--ARLR 698
Cdd:PRK03918 648 ELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALErvEELR 727
|
170
....*....|...
gi 1958668249 699 QENKMFQDLLGEY 711
Cdd:PRK03918 728 EKVKKYKALLKER 740
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
613-686 |
7.63e-03 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 36.49 E-value: 7.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958668249 613 LTEATSRVRTLEKKNNLLEIEVSDLRERFNAASSASKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENA 686
Cdd:COG3074 6 LEELEAKVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKIDEV 79
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
574-789 |
8.18e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 574 ESEISAlrQKLEAKDISAVEEWKKKNEALvdrcgQLDSALTEATSRVRTLEKKNNLLEIEVSDLRERFNAASS------- 646
Cdd:pfam01576 613 EKAISA--RYAEERDRAEAEAREKETRAL-----SLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvheler 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 647 ASKILQERIEEMRTSNKEKDNTIT-------RLKCRLQDLEEAFENAYKLSDDK-EARLRQENKMFQDLLGEYESLGKEH 718
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEELEDELQatedaklRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVRELEAELEDERKQR 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668249 719 GRVKDTLNMTENKLLDAHTQISDLKR-------MISKLEAQVKQAEHESmlslrhsakAPTRPSRANTLATSDVSRRK 789
Cdd:pfam01576 766 AQAVAAKKKLELDLKELEAQIDAANKgreeavkQLKKLQAQMKDLQREL---------EEARASRDEILAQSKESEKK 834
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
567-752 |
8.21e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 567 ADLRAY--YESEISALRQKLEaKDISaVEEWKkkneALVDRCGQLDSALTEATSRVRTLEKKNNLL-----EIEVSDLRE 639
Cdd:COG2433 340 AALKAYdaYKNKFERVEKKVP-PDVD-RDEVK----ARVIRGLSIEEALEELIEKELPEEEPEAERekeheERELTEEEE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 640 RFnaassasKILQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLsddKEARLRQENKMFQDllGEYESLGKEHG 719
Cdd:COG2433 414 EI-------RRLEEQVERLEAEVEELEAELEEKDERIERLER------EL---SEARSEERREIRKD--REISRLDREIE 475
|
170 180 190
....*....|....*....|....*....|...
gi 1958668249 720 RVKDTLNMTENKLLDAHTQISDLKRMIsKLEAQ 752
Cdd:COG2433 476 RLERELEEERERIEELKRKLERLKELW-KLEHS 507
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
583-699 |
9.26e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.67 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668249 583 KLEAkdisavEEWKKKNEALVDRCGQLDSALTEATSRVRTLEKKNNLLEIEVsdlrERFNAASSASKILQERIEEMRTSN 662
Cdd:pfam12718 6 KLEA------ENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEV----EKLEEQLKEAKEKAEESEKLKTNN 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958668249 663 KekdnTITRlkcRLQDLEEAFENAYKLSDDKEARLRQ 699
Cdd:pfam12718 76 E----NLTR---KIQLLEEELEESDKRLKETTEKLRE 105
|
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