|
Name |
Accession |
Description |
Interval |
E-value |
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
579-674 |
1.85e-05 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 45.98 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 579 QQAKADFE--------ELKALKKKIVVLKAERSKEAATLENVLRQQtlLEARLAEEKEIFRRFREEkFAEDMEKTRAELL 650
Cdd:COG2825 42 KAAQKKLEkefkkrqaELQKLEKELQALQEKLQKEAATLSEEERQK--KERELQKKQQELQRKQQE-AQQDLQKRQQELL 118
|
90 100
....*....|....*....|....
gi 15222544 651 NKYYERSEKIFRHIAETENASHMV 674
Cdd:COG2825 119 QPILEKIQKAIKEVAKEEGYDLVL 142
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
578-671 |
5.91e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 43.73 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 578 NQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQtlLEARLAEEKEIFRRFREeKFAEDMEKTRAELLNKYYERS 657
Cdd:smart00935 24 EKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREK--KEKELQKKVQEFQRKQQ-KLQQDLQKRQQEELQKILDKI 100
|
90
....*....|....
gi 15222544 658 EKIFRHIAETENAS 671
Cdd:smart00935 101 NKAIKEVAKKKGYD 114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
306-718 |
8.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 306 QAETLREQAPIDWKQVPCLKHKKQNKRKPQ--KSSARPKKMSGENVNLATLMRE-KRARKEAESKARLAIVDKTHEDKAR 382
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADeaKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 383 LD----VAEKNRKGLEDKTK----KGTFGAERRDVTDVTRVDKARPITVGQKGSSGRSVDRERSGLDTSGSKRPCSSKEV 454
Cdd:PTZ00121 1472 ADeakkKAEEAKKADEAKKKaeeaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 455 VPALDKRRrigsgdvdlsagprllanADHSFRYEYKVRDSPFSADRVECARFLRKVVGAPGEPEHEFLAEadlfEKWARA 534
Cdd:PTZ00121 1552 KKAEELKK------------------AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE----EKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 535 EcqavgannllisrydrNLRSAREKILELEgKLKNAERTIAYNNQQAKADFEELKalkkkivvlKAERSKEAATLENVLR 614
Cdd:PTZ00121 1610 E----------------EAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKK---------KAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 615 QQtllEARLAEEKEifRRFREEKFAEDMEKTRAELLNKYYERSEKifrhiaetenASHMVKMHAQATGTLSCLKFLADED 694
Cdd:PTZ00121 1664 AE---EAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKK----------AEELKKKEAEEKKKAEELKKAEEEN 1728
|
410 420
....*....|....*....|....
gi 15222544 695 KIPIPASTFEEFEDEAKEWKDKID 718
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
546-675 |
2.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 546 ISRYDRNLRSAREKILELEGKLKNAERtiaynnqqakaDFEELKALKKKIVVL---KAERSKEAATLENVLRQQTL---- 618
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKK-----------ELEKLEELKKKLAELekkLDELEEELAELLKELEELGFesve 588
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222544 619 -LEARLAEEKEIFRRFREEKFAEDMEKTRAELLNKYYERSEKIFRHIAETENASHMVK 675
Cdd:PRK03918 589 eLEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
557-660 |
3.17e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 557 REKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTLLEARLAEEKEIFRRFREE 636
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
90 100
....*....|....*....|....
gi 15222544 637 kfAEDMEKTRAELLNKYYERSEKI 660
Cdd:TIGR02169 373 --LEEVDKEFAETRDELKDYREKL 394
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
579-671 |
8.02e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 579 QQAKADFEEL-KALKKKIVVLKAERSKEAATLENVlrQQTLLEARLAEEKEI------FRRFREeKFAEDMEKTRAELLN 651
Cdd:pfam03938 18 KAAQAQLEKKfKKRQAELEAKQKELQKLYEELQKD--GALLEEEREEKEQELqkkeqeLQQLQQ-KAQQELQKKQQELLQ 94
|
90 100
....*....|....*....|
gi 15222544 652 KYYERSEKIFRHIAETENAS 671
Cdd:pfam03938 95 PIQDKINKAIKEVAKEKGYD 114
|
|
| Transposase_28 |
pfam04195 |
Putative gypsy type transposon; This family of plant genes are thought to be related to gypsy ... |
169-222 |
8.73e-04 |
|
Putative gypsy type transposon; This family of plant genes are thought to be related to gypsy type transposons.
Pssm-ID: 461222 Cd Length: 69 Bit Score: 38.44 E-value: 8.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15222544 169 FTETGLRFPIPDFLMRFCRNRQIAISQLTVASIRTAACLQMLC-ARCGIPLSVEL 222
Cdd:pfam04195 6 FFEAGLRLPFSPFFCDVLNFYGLAPLHLNPNSILILSIFAVLCeSFLGVPPSLPL 60
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
579-674 |
1.85e-05 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 45.98 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 579 QQAKADFE--------ELKALKKKIVVLKAERSKEAATLENVLRQQtlLEARLAEEKEIFRRFREEkFAEDMEKTRAELL 650
Cdd:COG2825 42 KAAQKKLEkefkkrqaELQKLEKELQALQEKLQKEAATLSEEERQK--KERELQKKQQELQRKQQE-AQQDLQKRQQELL 118
|
90 100
....*....|....*....|....
gi 15222544 651 NKYYERSEKIFRHIAETENASHMV 674
Cdd:COG2825 119 QPILEKIQKAIKEVAKEEGYDLVL 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
523-660 |
5.19e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 523 AEADLFEKWARAECQAVGANnlLISRYDRNLRSAREKILELEGKLKNAERTI-AYNNQQAKADFEELKALKKKIVVLKAE 601
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEA--ELEELRAELARLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222544 602 RSKEAATLENVLRQQTLLEARLAEEKEIFRRFREE--KFAEDMEKTRAELLNKYYERSEKI 660
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEaaALLEALEEELEALEEALAEAEAAL 414
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
578-671 |
5.91e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 43.73 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 578 NQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQtlLEARLAEEKEIFRRFREeKFAEDMEKTRAELLNKYYERS 657
Cdd:smart00935 24 EKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREK--KEKELQKKVQEFQRKQQ-KLQQDLQKRQQEELQKILDKI 100
|
90
....*....|....
gi 15222544 658 EKIFRHIAETENAS 671
Cdd:smart00935 101 NKAIKEVAKKKGYD 114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
306-718 |
8.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 306 QAETLREQAPIDWKQVPCLKHKKQNKRKPQ--KSSARPKKMSGENVNLATLMRE-KRARKEAESKARLAIVDKTHEDKAR 382
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADeaKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 383 LD----VAEKNRKGLEDKTK----KGTFGAERRDVTDVTRVDKARPITVGQKGSSGRSVDRERSGLDTSGSKRPCSSKEV 454
Cdd:PTZ00121 1472 ADeakkKAEEAKKADEAKKKaeeaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 455 VPALDKRRrigsgdvdlsagprllanADHSFRYEYKVRDSPFSADRVECARFLRKVVGAPGEPEHEFLAEadlfEKWARA 534
Cdd:PTZ00121 1552 KKAEELKK------------------AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE----EKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 535 EcqavgannllisrydrNLRSAREKILELEgKLKNAERTIAYNNQQAKADFEELKalkkkivvlKAERSKEAATLENVLR 614
Cdd:PTZ00121 1610 E----------------EAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKK---------KAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 615 QQtllEARLAEEKEifRRFREEKFAEDMEKTRAELLNKYYERSEKifrhiaetenASHMVKMHAQATGTLSCLKFLADED 694
Cdd:PTZ00121 1664 AE---EAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKK----------AEELKKKEAEEKKKAEELKKAEEEN 1728
|
410 420
....*....|....*....|....
gi 15222544 695 KIPIPASTFEEFEDEAKEWKDKID 718
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
546-675 |
2.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 546 ISRYDRNLRSAREKILELEGKLKNAERtiaynnqqakaDFEELKALKKKIVVL---KAERSKEAATLENVLRQQTL---- 618
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKK-----------ELEKLEELKKKLAELekkLDELEEELAELLKELEELGFesve 588
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222544 619 -LEARLAEEKEIFRRFREEKFAEDMEKTRAELLNKYYERSEKIFRHIAETENASHMVK 675
Cdd:PRK03918 589 eLEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
557-660 |
3.17e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 557 REKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTLLEARLAEEKEIFRRFREE 636
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
90 100
....*....|....*....|....
gi 15222544 637 kfAEDMEKTRAELLNKYYERSEKI 660
Cdd:TIGR02169 373 --LEEVDKEFAETRDELKDYREKL 394
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
579-671 |
8.02e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 579 QQAKADFEEL-KALKKKIVVLKAERSKEAATLENVlrQQTLLEARLAEEKEI------FRRFREeKFAEDMEKTRAELLN 651
Cdd:pfam03938 18 KAAQAQLEKKfKKRQAELEAKQKELQKLYEELQKD--GALLEEEREEKEQELqkkeqeLQQLQQ-KAQQELQKKQQELLQ 94
|
90 100
....*....|....*....|
gi 15222544 652 KYYERSEKIFRHIAETENAS 671
Cdd:pfam03938 95 PIQDKINKAIKEVAKEKGYD 114
|
|
| Transposase_28 |
pfam04195 |
Putative gypsy type transposon; This family of plant genes are thought to be related to gypsy ... |
169-222 |
8.73e-04 |
|
Putative gypsy type transposon; This family of plant genes are thought to be related to gypsy type transposons.
Pssm-ID: 461222 Cd Length: 69 Bit Score: 38.44 E-value: 8.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15222544 169 FTETGLRFPIPDFLMRFCRNRQIAISQLTVASIRTAACLQMLC-ARCGIPLSVEL 222
Cdd:pfam04195 6 FFEAGLRLPFSPFFCDVLNFYGLAPLHLNPNSILILSIFAVLCeSFLGVPPSLPL 60
|
|
| DUF1204 |
pfam06721 |
Protein of unknown function (DUF1204); This family represents the C-terminus of a number of ... |
567-728 |
1.09e-03 |
|
Protein of unknown function (DUF1204); This family represents the C-terminus of a number of Arabidopsis thaliana hypothetical proteins of unknown function. Family members contain a conserved DFD motif.
Pssm-ID: 284198 [Multi-domain] Cd Length: 243 Bit Score: 41.68 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 567 LKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTLLEARLAEEKEIFRRfREEKFAEDMEKTR 646
Cdd:pfam06721 7 LEKCLESASKDAAHAKDAHAALAVEKEKMAEALADLARCQDDAEEEKEKTDELADRAKSEKKRLRE-RREEYAEFQRRKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 647 ----AELLNKyyeRSEKIFRHIAETENASHMVKMHAQATGTLSCLKFLADEDKIPIPASTF-EEFEDEAKEWKDKIDAFV 721
Cdd:pfam06721 86 ldhmADLFQA---RLDRIKAHIDDKKAAEPKFLDFNQVCGNIALLDALVEAGEIEIKSDDLmLRLIADADALEAEVEAFE 162
|
....*..
gi 15222544 722 VTELVNG 728
Cdd:pfam06721 163 ITDIEDD 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
536-632 |
1.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 536 CQAVGANNLLISRYDRNLRSAREKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQ 615
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90
....*....|....*..
gi 15222544 616 QTLLEARLAEEKEIFRR 632
Cdd:COG4942 92 IAELRAELEAQKEELAE 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
529-651 |
1.76e-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: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 529 EKWARAEcQAVGANNLLISRYDRNLRSAREKILELEGKLKNAERTIA------YNNQQAKADFE-ELKALKKKIVVLKAE 601
Cdd:TIGR02168 239 EELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelYALANEISRLEqQKQILRERLANLERQ 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15222544 602 RSKEAATLENVLRQQTLLEARLAEEKEIFRRFREEK--FAEDMEKTRAELLN 651
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELesLEAELEELEAELEE 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
546-670 |
2.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 546 ISRYDRNLRSAREKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTLLEARLAE 625
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15222544 626 EKEifRRFREEKFAEDMEKTRAELLNKYYERSEKIFRHIAETENA 670
Cdd:COG1196 384 LAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
519-685 |
2.80e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 519 HEFLAEADLFEKWARAECQAVGANNLLISRyDRNLRSAREKILELEGKLKNAERTIAYNNQQAkADFEELKA-LKKK--- 594
Cdd:pfam13166 324 EDIESEAEVLNSQLDGLRRALEAKRKDPFK-SIELDSVDAKIESINDLVASINELIAKHNEIT-DNFEEEKNkAKKKlrl 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 595 --IVVLKAERSKEAATLENVLRQQTLLEARLAEEKEIFRRFREEKfAEDMEKTR-----AELLNKY---YERSEKIFRHI 664
Cdd:pfam13166 402 hlVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEI-KELEAQLRdhkpgADEINKLlkaFGFGELELSFN 480
|
170 180
....*....|....*....|.
gi 15222544 665 AETENASHMVKMHAQATGTLS 685
Cdd:pfam13166 481 EEGKGYRIIRKGGSQAAETLS 501
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
546-710 |
2.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 546 ISRYDRNLRSAREKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTLLEARLAE 625
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 626 -EKEIfrrfreEKFAEDMEKTRAELlnkyyERSEKIFRHIAETENASHMVKMHAQATGTLSCLKFLADEDKIPIPASTFE 704
Cdd:COG4372 148 rEEEL------KELEEQLESLQEEL-----AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
....*.
gi 15222544 705 EFEDEA 710
Cdd:COG4372 217 AEELLE 222
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
327-718 |
3.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 327 KKQNKRKPQKSSARPKKMSGENVNLATLMREKRARKEAEsKARLAIVDKTHEDKARLDVA---EKNRKGLEDKTKKGTFG 403
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAE-EARKAEDAKRVEIARKAEDArkaEEARKAEDAKKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 404 AER-RDVTDVTRVDKARPITVGQKGSSGRSVDRERSGLDTSGSKRPCSSKEVVPALDKRRRIGSGDVDLSAGPRLLANAD 482
Cdd:PTZ00121 1184 AEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 483 HSFRYEYKVR-DSPFSADRVECARFLRKvvgAPGEPEHEFLAEADLFEKWARAECQAVGANnllisrydRNLRSAREKIL 561
Cdd:PTZ00121 1264 HFARRQAAIKaEEARKADELKKAEEKKK---ADEAKKAEEKKKADEAKKKAEEAKKADEAK--------KKAEEAKKKAD 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 562 ELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTllEARLAEE------------KEI 629
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEakkkaeedkkkaDEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 630 FRRFREEKFAEDM-----EKTRAELLNKYYERSEKI--FRHIAETENASHMVKMHAQATGTLSCLKFLADEDKipipasT 702
Cdd:PTZ00121 1411 KKAAAAKKKADEAkkkaeEKKKADEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK------K 1484
|
410
....*....|....*.
gi 15222544 703 FEEFEDEAKEWKDKID 718
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKAD 1500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
546-666 |
4.30e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 546 ISRYDRNLRSAREKILELEGKLKNAERTIA-YNNQQAKA-DFEELKALKKKIVVLKAERSK------EA-ATLENVLRQQ 616
Cdd:COG1579 47 LEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVrNNKEYEALQKEIESLKRRISDledeilELmERIEELEEEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15222544 617 TLLEARLAEEKEIFRRFREEkFAEDMEKTRAElLNKYYERSEKIFRHIAE 666
Cdd:COG1579 127 AELEAELAELEAELEEKKAE-LDEELAELEAE-LEELEAEREELAAKIPP 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
554-716 |
4.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 554 RSAREKILELEgklKNAERTIaynnQQAKADFEELKalKKKIVVLKAERSKEAATLENVLRQQTL----LEARLAEEKEI 629
Cdd:PRK12704 27 KIAEAKIKEAE---EEAKRIL----EEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 630 FRRFRE---------EKFAEDMEKTRAELLNKYYERSEKIFRHIAETENASHMVKmhAQATGTLscLKFLADEDKIPIpA 700
Cdd:PRK12704 98 LDRKLEllekreeelEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA--EEAKEIL--LEKVEEEARHEA-A 172
|
170
....*....|....*.
gi 15222544 701 STFEEFEDEAKEWKDK 716
Cdd:PRK12704 173 VLIKEIEEEAKEEADK 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
550-670 |
5.64e-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: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 550 DRNLRSAREKILELEGKLKNAERT---IAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQTLLEARLAEE 626
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15222544 627 KEIFR---------RFREEKFAEDMEKTRAELLNKYYERSEKIFRHIAETENA 670
Cdd:COG4913 740 EDLARlelralleeRFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
543-660 |
8.54e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 543 NLLISRYDRNLRSAREKILELEGKLKNAERTiaYNNQQAKAdfEELKALKKKivvLKAERSKEAatlenvlrQQTLLEAR 622
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKL--KEELEEKK--EKLQEEEDK---LLEEAEKEA--------QQAIKEAK 583
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15222544 623 lAEEKEIFRRFREEKFAEDMEKTRAEL------LNKYYERSEKI 660
Cdd:PRK00409 584 -KEADEIIKELRQLQKGGYASVKAHELiearkrLNKANEKKEKK 626
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
537-670 |
8.57e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 537 QAVGANNLLISRYDRNLRSAREKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERSKEAATLENVLRQQ 616
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15222544 617 TLLEARLAEEKEifRRFREEKFAEDMEKTRAELLNKYYERSEKIFRHIAETENA 670
Cdd:COG1196 354 EEAEAELAEAEE--ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
546-720 |
8.68e-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: 39.67 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 546 ISRYDRNLRSAREKILELEGKLKNAERTIAYNNQQAKADFEELKALKKKIVVLKAERskeaatlENVLRQQTLLEARLAE 625
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-------ENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222544 626 -----------EKEIFRRFREEKFAEDMEKTRAelLNKYYERSEKIFRHIAETENASHMVKMHAqatgtlsclkfladED 694
Cdd:TIGR02169 770 leedlhkleeaLNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYL--------------EK 833
|
170 180
....*....|....*....|....*.
gi 15222544 695 KIpipastfEEFEDEAKEWKDKIDAF 720
Cdd:TIGR02169 834 EI-------QELQEQRIDLKEQIKSI 852
|
|
| |
