| 30163 |
cd01948 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
true |
false |
true |
240 |
1e-46 |
183.49 |
98.33 |
1,434,2,236 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKNG 514
cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 515 IHVFSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSY 594
cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111115185 595 IKTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEPI 670
cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 32382 |
COG2200 |
Rtn |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
false |
false |
false |
256 |
1e-50 |
196.70 |
91.80 |
2,434,7,83,518,90,152 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKNG 514
COG2200 8 LRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRTWPRAGP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 515 IHVfSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSY 594
COG2200 88 LRL-AVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGTGYSSLSY 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111115185 595 IKTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEPI 670
COG2200 167 LKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPLPA 242
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
3e-45 |
178.56 |
97.93 |
1,434,3,236 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKNG 514
smart00052 4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 515 IHVFSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSY 594
smart00052 84 PLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSY 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111115185 595 IKTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEPI 670
smart00052 164 LKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 239
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 109613 |
pfam00563 |
EAL |
EAL domain |
EAL domain |
false |
false |
false |
236 |
2e-39 |
159.12 |
98.73 |
5,434,3,68,502,74,36,539,110,27,567,137,50,618,187,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKA---LREYKSFVS 511
pfam00563 4 LREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKAlaqLAEWRGNAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 512 KNGIHVFSINISPYSLKSQNFRIFLRDtLLKSQIPLQNICLEITETGILENFEIInKYFQELKSFGIKLALDDFGSGHTS 591
pfam00563 84 LPPDLPLSVNLSPASLLDPSFLEALLA-LKQGGLPPSRLVLEITESDLDEDLRLL-EALARLRSLGFRLALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111115185 592 LSYIKTLPIDLLKIDGSFIKAINSSEiDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKP 667
pfam00563 162 LSYLSRLPPDYIKIDRSFIKDLSDPE-SRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 236
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
7e-32 |
134.06 |
20.88 |
3,437,871,29,466,901,51,518,952,152 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 438 AIKNDFFTLYYQKINPLKKNLKPKIEILT-RLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKNGIH 516
PRK09776 872 MLEENQLMLQAQEIASPRIPEARNLWLISlRLWDCEGEIIDEGAFRPAAEDPALMHALDRWVIHELFQQGARAVASKGLS 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 517 VfSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSYIK 596
PRK09776 952 I-AIPLSVASLSSATLLPFLLEQLENSPLPPRLLHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLK 1030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111115185 597 TLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEPI 670
PRK09776 1031 AFMADYLKIDGELCANLQGNLMDEMLVSIINGIAQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRPQPL 1104
|
|
|
|
|
|
|
-1 |
| 34551 |
COG4943 |
COG4943 |
Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms] |
Predicted signal transduction protein containing sensor and EAL domains [Signal... |
false |
true |
false |
524 |
1e-26 |
116.60 |
44.27 |
3,436,274,125,561,402,8,573,410,96 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 437 KAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKNGIH 516
COG4943 275 RAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDLLRQHRDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 517 VFSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILE---NFEIINKYfqelKSFGIKLALDDFGSGHTSLS 593
COG4943 355 HVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFADpkkMTPIILRL----REAGHEIYIDDFGTGYSNLH 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111115185 594 YIKTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEP 669
COG4943 431 YLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKALP 506
|
|
|
|
|
|
|
-1 |
| 34606 |
COG5001 |
COG5001 |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms] |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF... |
false |
true |
false |
663 |
1e-25 |
113.58 |
34.24 |
4,438,411,6,445,417,64,511,481,6,518,487,151 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 439 IKNDFFtLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFvsKNGIHVf 518
COG5001 412 LEQELS-VHFQPIVDIVSGKTIALEALARWHSPEIGPVPPDVFIGIAERSGQIVELTRLLLAKALREARAW--PMDVRV- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 519 SINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSYIKTL 598
COG5001 488 SINLSARDLASMENVRRLLAIVSESCIAPHRLDFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRAL 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 111115185 599 PIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEP 669
COG5001 568 PLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMP 638
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
4e-22 |
101.77 |
36.25 |
5,434,404,40,474,445,7,482,452,113,595,568,20,618,588,52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGK-PIPNDQIfSLIDKYNLTVEVDKLVVKKALREYKSFVSKN 513
PRK13561 405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSwDLPDGLI-DRIESCGLMVTVGHWVLEESCRLLAAWQERG 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 514 GIHVFSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLS 593
PRK13561 484 IMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 594 YI---KTLPIDLLKIDGSFIKAINSseiDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEPI 670
PRK13561 564 QLqhmKSLPIDVLKIDKMFVDGLPE---DSSMVAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPLPI 640
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
1e-20 |
96.72 |
37.25 |
6,426,399,2,429,401,7,436,414,25,462,439,50,513,489,4,517,494,152 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 427 NQnKIFQYIL------KAIKNDFFTLYYQKINPLKKNLKPKiEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVK 500
PRK10060 400 NQ-RVFEYLWldtnlrKALENDQLVIHYQPKITWRGEVRSL-EALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVIL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 501 KALREYKSFVSKnGIHV-FSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIK 579
PRK10060 478 DVVRQAAKWRDK-GINLrVAVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQ 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 580 LALDDFGSGHTSLSYIKTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYG 659
PRK10060 557 VHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNER 636
|
250
....*....|
gi 111115185 660 QGFLWHKPEP 669
PRK10060 637 QGFLFAKPMP 646
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
6e-20 |
94.38 |
32.28 |
3,434,477,160,594,640,21,618,661,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKNG 514
PRK11829 478 LLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 515 IHVFSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSY 594
PRK11829 558 SLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRY 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111115185 595 ---IKTLPIDLLKIDGSFIKAINSseiDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEP 669
PRK11829 638 lnhLKSLPIHMIKLDKSFVKNLPE---DDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 712
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
2e-19 |
92.98 |
29.29 |
2,436,549,77,513,627,156 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 437 KAIKNDFFTLYYQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKSFVSKN-GI 515
PRK11359 550 EAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNiHI 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 516 HVFSINISPYSLKSQNFRIFLRDTLLKSQIPLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSYI 595
PRK11359 630 PALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRL 709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111115185 596 KTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHKPEP 669
PRK11359 710 VSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
3e-18 |
88.57 |
45.56 |
10,434,267,33,468,300,3,471,305,3,475,308,20,495,332,14,511,346,5,517,351,20,539,371,9,548,382,18,567,400,103 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 435 ILKAIKNDFFTLYYQKINPLKKNLKPKIEILTRlFDH--MGKpIPNDQIFSLIDKYNLTVEVD----KLVVKKALREYKS 508
PRK10551 268 ILTAIKREQFYVVYQPVVDTQTLRVTGLEVLLR-WRHptAGE-IPPDAFINYAEAQKLIVPLTqhlfELIARDAAELQKV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 509 FvsKNGIHvFSINISPYSLKSQNFRIFLRdtLLKSQIPLQ--NICLEITETGILENFEIInKYFQELKSFGIKLALDDFG 586
PRK10551 346 L--PVGAK-LGINIAPAHLHSDSFKADVQ--RLLASLPADhfQIVLEITERDMLQEEEAL-KLFAWLHSQGIEIAIDDFG 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 587 SGHTSLSYIKTLPIDLLKIDGSFIKAINSSEIDFVIIKSIKKIADTKNIKIIAEFVYNEEILKKINELEIDYGQGFLWHK 666
PRK10551 420 TGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISR 499
|
....
gi 111115185 667 PEPI 670
PRK10551 500 PLPL 503
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
4e-11 |
64.90 |
25.86 |
4,447,419,60,509,479,32,541,514,3,546,517,68 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 448 YQKINPLKKNLKPKIEILTRLFDHMGKPIPNDQIFSLIDKYNLTVEVDKLVVKKALREYKsfVSKNGIHVFSINISPYSL 527
PRK11059 420 YQQPVVTRDGQVHHRELMCRIRDGQGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLS--YWPEESQNLSINLSVDSL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111115185 528 KSQNFRIFLRDTLL---KSQipLQNICLEITETGILENFEIINKYFQELKSFGIKLALDDFGSGHTSLSYIKTLPIDLLK 604
PRK11059 498 LSRAFQRWLRDTLLqceRSQ--RKRLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIK 575
|
170
....*....|
gi 111115185 605 IDGSFIKAIN 614
PRK11059 576 LHPSLVRNIH 585
|
|
|
|
|
|
|
-1 |
|