|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
439-888 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 678.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 439 EVVGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVG 518
Cdd:COG5001 226 LLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAG 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 519 DLLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMYSEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGT 598
Cdd:COG5001 306 DELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 599 DVTELMKNADMAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKH 678
Cdd:COG5001 386 DAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQH 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 679 PKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHNQGFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEA 758
Cdd:COG5001 466 PERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 759 LDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITL 838
Cdd:COG5001 546 LELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIAL 625
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446532590 839 SKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVSSKDVWRLLHK 888
Cdd:COG5001 626 AHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| DUF4084 |
pfam13321 |
Domain of unknown function (DUF4084); This family of Firmicute proteins is frequently ... |
1-304 |
2.34e-157 |
|
Domain of unknown function (DUF4084); This family of Firmicute proteins is frequently associated with the EAL, GGDEF and PAS families, pfam00563, pfam00990, and pfam00989. The exact function is not known.
Pssm-ID: 372562 Cd Length: 304 Bit Score: 462.87 E-value: 2.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 1 MINQKKYVHFVMIYIIIFSLWIFLIPKNLNIKEIGILFLFCFAALFSCYCLYKAIKKMKRGDKLFWVLLLCTCLCGLTME 80
Cdd:pfam13321 1 MINQKKYVHFVTMYIIIFSLWIFLIPKDLNIKEIGILFLFCFATLFSCYCLYKAIKKMKRGDKLFWVLVLCTCLCGLTME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 81 ITLFLHSLSIYDQVIFSYTALPFFIVQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIIIMNIYFTLTFILDRSSFRMLT 160
Cdd:pfam13321 81 ITLFLHSLSIYDQVIFSYKALPFFIVQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIVIMNIYFTLTFILDISSFRMLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 161 TDHWVLIGYFIAQSLVIYAVISLYRREQYSASRISLIIGFTIILVYGYIHLFQLNAGMKTSSEVSYLIHTASILLIGLSS 240
Cdd:pfam13321 161 TDTWVLIGYFIAQSLVIYAVISLYRREEYSSSRISLIIGFTIILVYGYIHLFQLNAGIKPSSEVSYLIHTASILLIGLSS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446532590 241 ILYILDKPMQHETKTKYYRFDYVRFILPYFSIIITFSFIIFQPWDDKFMLIGLVLSLILLFLRQ 304
Cdd:pfam13321 241 ILYILDKPIQHETKTKYYRFDYVRFILPYFSIIITFSFIIFQPWDDKFMLIGLVLSLILLFLRQ 304
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
449-887 |
6.44e-119 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 376.33 E-value: 6.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 449 DITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAqtSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKR 528
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 529 LRSCLRSKDVVARQGGDEFTILLPDMySEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNAD 608
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHT-SQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 609 MAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELAKALQQNEFFLEYQPQVSTkTKQIIGFEALIRWKHPKLGIVSPAQ 688
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 689 FIPLAEETGFIIELGNWILRTACLEAKRWHNQGFShLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIA 768
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 769 INQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIA 848
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420 430
....*....|....*....|....*....|....*....
gi 446532590 849 EGVETEEQWKFLYEQNCDNIQGFFISKPVSSKDVWRLLH 887
Cdd:PRK10060 617 EGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYK 655
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
641-878 |
2.00e-110 |
|
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.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 338.75 E-value: 2.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 641 GELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHnQ 720
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 721 GFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSS 800
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532590 801 LAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVS 878
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
640-877 |
6.06e-101 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 314.15 E-value: 6.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 640 EGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHN 719
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 720 QGFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYS 799
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532590 800 SLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPV 877
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
642-876 |
4.58e-75 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 245.30 E-value: 4.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 642 ELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWhnQG 721
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 722 FSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSL 801
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446532590 802 AYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKP 876
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
463-625 |
3.65e-49 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 171.37 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 463 LAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQ 542
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 543 GGDEFTILLPDMYSEkSAAFIAEQI-LNILNKPFFIQGEE-LSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKN 620
Cdd:TIGR00254 81 GGEEFVVILPGTPLE-DALSKAERLrDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 446532590 621 RFVFF 625
Cdd:TIGR00254 160 RVVVA 164
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
335-462 |
1.56e-13 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 73.86 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 335 ALSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFIDSKDHDLLKKAL-QLTKKGRPQTL 413
Cdd:COG5809 135 ALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIsQLLKDGGIAQG 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446532590 414 EVRTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEH 462
Cdd:COG5809 215 EVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLRK 263
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
339-455 |
2.26e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 56.15 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 339 SEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFtAYYC-EVESYSLLHFIDSKDHDLLKKALQLTKKGRPQT--LEV 415
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIF-GYSAeELIGRNVLELIPEEDREEVRERIERRLEGEPEPvsEER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446532590 416 RTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYE 455
Cdd:TIGR00229 80 RVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKE 119
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
341-450 |
4.49e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 46.26 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 341 QRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFI----DSKDHDLLKKALQLTkkGRPQTLEVR 416
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIpeedDAEVAELLRQALLQG--EESRGFEVS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 446532590 417 TKEKEGYYYYLHITLIP-TFINKEVVGMFGIARDI 450
Cdd:pfam00989 79 FRVPDGRPRHVEVRASPvRDAGGEILGFLGVLRDI 113
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
439-888 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 678.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 439 EVVGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVG 518
Cdd:COG5001 226 LLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAG 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 519 DLLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMYSEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGT 598
Cdd:COG5001 306 DELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 599 DVTELMKNADMAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKH 678
Cdd:COG5001 386 DAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQH 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 679 PKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHNQGFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEA 758
Cdd:COG5001 466 PERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 759 LDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITL 838
Cdd:COG5001 546 LELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIAL 625
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446532590 839 SKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVSSKDVWRLLHK 888
Cdd:COG5001 626 AHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| DUF4084 |
pfam13321 |
Domain of unknown function (DUF4084); This family of Firmicute proteins is frequently ... |
1-304 |
2.34e-157 |
|
Domain of unknown function (DUF4084); This family of Firmicute proteins is frequently associated with the EAL, GGDEF and PAS families, pfam00563, pfam00990, and pfam00989. The exact function is not known.
Pssm-ID: 372562 Cd Length: 304 Bit Score: 462.87 E-value: 2.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 1 MINQKKYVHFVMIYIIIFSLWIFLIPKNLNIKEIGILFLFCFAALFSCYCLYKAIKKMKRGDKLFWVLLLCTCLCGLTME 80
Cdd:pfam13321 1 MINQKKYVHFVTMYIIIFSLWIFLIPKDLNIKEIGILFLFCFATLFSCYCLYKAIKKMKRGDKLFWVLVLCTCLCGLTME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 81 ITLFLHSLSIYDQVIFSYTALPFFIVQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIIIMNIYFTLTFILDRSSFRMLT 160
Cdd:pfam13321 81 ITLFLHSLSIYDQVIFSYKALPFFIVQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIVIMNIYFTLTFILDISSFRMLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 161 TDHWVLIGYFIAQSLVIYAVISLYRREQYSASRISLIIGFTIILVYGYIHLFQLNAGMKTSSEVSYLIHTASILLIGLSS 240
Cdd:pfam13321 161 TDTWVLIGYFIAQSLVIYAVISLYRREEYSSSRISLIIGFTIILVYGYIHLFQLNAGIKPSSEVSYLIHTASILLIGLSS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446532590 241 ILYILDKPMQHETKTKYYRFDYVRFILPYFSIIITFSFIIFQPWDDKFMLIGLVLSLILLFLRQ 304
Cdd:pfam13321 241 ILYILDKPIQHETKTKYYRFDYVRFILPYFSIIITFSFIIFQPWDDKFMLIGLVLSLILLFLRQ 304
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
386-887 |
2.18e-122 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 382.60 E-value: 2.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 386 LLHFIDSKDHDLLKKALQLTKKGRPQTLEVRTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEHLAF 465
Cdd:COG2200 76 LLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 466 HDALTGLPNRRKFEKDLKNILNTAQTSAND-VAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQGG 544
Cdd:COG2200 156 LDLLLLLLLRRLLLLLLLLLLLLLLALALLaLLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 545 DEFTILLPDMYSEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKNRFVF 624
Cdd:COG2200 236 GGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 625 FSKEISIAQNEIQfLEGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGN 704
Cdd:COG2200 316 FAAAEARARRRLA-LESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 705 WILRTACLEAKRWHNQGFShLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQN 784
Cdd:COG2200 395 WVLERALRQLARWPERGLD-LRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 785 LGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQN 864
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
490 500
....*....|....*....|...
gi 446532590 865 CDNIQGFFISKPVSSKDVWRLLH 887
Cdd:COG2200 554 CDYAQGYLFGRPLPLEELEALLR 576
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
449-887 |
6.44e-119 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 376.33 E-value: 6.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 449 DITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAqtSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKR 528
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 529 LRSCLRSKDVVARQGGDEFTILLPDMySEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNAD 608
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHT-SQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 609 MAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELAKALQQNEFFLEYQPQVSTkTKQIIGFEALIRWKHPKLGIVSPAQ 688
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 689 FIPLAEETGFIIELGNWILRTACLEAKRWHNQGFShLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIA 768
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 769 INQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIA 848
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420 430
....*....|....*....|....*....|....*....
gi 446532590 849 EGVETEEQWKFLYEQNCDNIQGFFISKPVSSKDVWRLLH 887
Cdd:PRK10060 617 EGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYK 655
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
641-878 |
2.00e-110 |
|
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.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 338.75 E-value: 2.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 641 GELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHnQ 720
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 721 GFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSS 800
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532590 801 LAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVS 878
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
455-882 |
4.13e-107 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 349.07 E-value: 4.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 455 EKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQtsanDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLR 534
Cdd:PRK11359 367 KSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 535 SKDVVARQGGDEFTILLPDMySEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMypDYGTDVTELMKNADMAMYRA 614
Cdd:PRK11359 443 PDQYLCRIEGTQFVLVSLEN-DVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 615 KANGKNRFVFFSKEISIAQNEIQFLEGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAE 694
Cdd:PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 695 ETGFIIELGNWILRTACLEAKRWHNQGFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQS 774
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTE 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 775 VVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETE 854
Cdd:PRK11359 680 IFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETK 759
|
410 420
....*....|....*....|....*...
gi 446532590 855 EQWKFLYEQNCDNIQGFFISKPVSSKDV 882
Cdd:PRK11359 760 EQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
640-877 |
6.06e-101 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 314.15 E-value: 6.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 640 EGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHN 719
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 720 QGFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYS 799
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532590 800 SLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPV 877
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
463-877 |
1.39e-79 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 270.82 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 463 LAFHDALTGLPNRRKFEKDLKNILNTAQTSAndvaVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQ 542
Cdd:PRK13561 230 NATRFPVSDLPNKALLMALLEQVVARKQTTA----LMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 543 GGDEFTILLPDMYSEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYpDYGTDVTELMKNADMAMYRAKANGKNRF 622
Cdd:PRK13561 306 SGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARRKGKNQI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 623 VFFSKEISIAQNEIQFLEGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIEL 702
Cdd:PRK13561 385 QFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTV 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 703 GNWILRTACLEAKRWHNQGFShLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQL 782
Cdd:PRK13561 465 GHWVLEESCRLLAAWQERGIM-LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 783 QNLGIQISIDDFGTGYSSLAYLTKY---PINTLKIAREFICGIttsPLEEAIISSIITLSKELNLEVIAEGVETEEQWKF 859
Cdd:PRK13561 544 RNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDW 620
|
410
....*....|....*...
gi 446532590 860 LYEQNCDNIQGFFISKPV 877
Cdd:PRK13561 621 LLKAGVGIAQGFLFARAL 638
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
439-877 |
1.13e-75 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 268.46 E-value: 1.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 439 EVVGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVG 518
Cdd:PRK09776 640 ENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAG 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 519 DLLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMySEKSAAFIAEQILNILN-KPFFIQGEELSITPSIGIAMYPDYG 597
Cdd:PRK09776 720 DALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDC-NVESARFIATRIISAINdYHFPWEGRVYRVGASAGITLIDANN 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 598 TDVTELMKNADMAMYRAKANGKNRFVFFSKEISIAQNEIQFLE-GELAKALQQNEFFLEYQPQVSTKTKQIIGF-EALIR 675
Cdd:PRK09776 799 HQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSlAEQWRMIKENQLMMLAHGVASPRIPEARNHwLISLR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 676 WKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLE-AKRWHNQGFShlkVGVNLSVVQFNHTNLIPTISKVLEETEL 754
Cdd:PRK09776 879 LWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQaAKAVASKGLS---IALPLSVAGLSSPTLLPFLLEQLENSPL 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 755 KPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISS 834
Cdd:PRK09776 956 PPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISI 1035
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446532590 835 IITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPV 877
Cdd:PRK09776 1036 IQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
409-881 |
1.55e-75 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 260.26 E-value: 1.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 409 RPQTLEVRTKEKEGYYYYlHITLIPTFINKEV-VGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILn 487
Cdd:PRK11829 177 RAMAKELEDIGDHGVLHH-QLTLPAHHQDDELgVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEI- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 488 TAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMYSEKSAAFIAEQI 567
Cdd:PRK11829 255 ASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 568 LNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELAKAL 647
Cdd:PRK11829 335 MSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 648 QQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHNQGFShLKV 727
Cdd:PRK11829 415 ENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVS-LPL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 728 GVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYL--- 804
Cdd:PRK11829 494 SVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhl 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446532590 805 TKYPINTLKIAREFICGIttsPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVSSKD 881
Cdd:PRK11829 574 KSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE 647
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
642-876 |
4.58e-75 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 245.30 E-value: 4.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 642 ELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWhnQG 721
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 722 FSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSL 801
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446532590 802 AYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKP 876
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
426-625 |
6.38e-74 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 243.73 E-value: 6.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 426 YLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDR 505
Cdd:COG2199 76 LLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 506 FKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMySEKSAAFIAEQILNILNK-PFFIQGEELSI 584
Cdd:COG2199 156 FKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEQlPFELEGKELRV 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446532590 585 TPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKNRFVFF 625
Cdd:COG2199 235 TVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
465-623 |
3.03e-72 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 234.37 E-value: 3.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 465 FHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQGG 544
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446532590 545 DEFTILLPDMySEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKNRFV 623
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
639-881 |
6.10e-70 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 240.97 E-value: 6.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 639 LEGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWH 718
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 719 nQGFSHLKVGVNLSVVQFNHTNLIPTISKVLEETELKPEALDIEITESIAINQNQSVvAKLEQLQNLGIQISIDDFGTGY 798
Cdd:COG4943 352 -AADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAIDDFGTGY 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 799 SSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVS 878
Cdd:COG4943 430 SSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLP 509
|
...
gi 446532590 879 SKD 881
Cdd:COG4943 510 AEE 512
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
464-621 |
9.67e-66 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 217.12 E-value: 9.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 464 AFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQG 543
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 544 GDEFTILLPD--MYSEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKNR 621
Cdd:pfam00990 81 GDEFAILLPEtsLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
462-625 |
7.60e-65 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 214.42 E-value: 7.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 462 HLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVAR 541
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 542 QGGDEFTILLPDMySEKSAAFIAEQILNILNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKNR 621
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 446532590 622 FVFF 625
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
463-625 |
3.65e-49 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 171.37 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 463 LAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQ 542
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 543 GGDEFTILLPDMYSEkSAAFIAEQI-LNILNKPFFIQGEE-LSITPSIGIAMYPDYGTDVTELMKNADMAMYRAKANGKN 620
Cdd:TIGR00254 81 GGEEFVVILPGTPLE-DALSKAERLrDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 446532590 621 RFVFF 625
Cdd:TIGR00254 160 RVVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
446-623 |
9.10e-48 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 177.02 E-value: 9.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 446 IARDITTLYEKQKQ------VEH---LAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHD 516
Cdd:PRK09581 265 LARVRTQIRRKRYQdalrnnLEQsieMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 517 VGDLLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMYSEKsAAFIAEQI-LNILNKPFFI--QGEELSITPSIGIAMY 593
Cdd:PRK09581 345 AGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIED-AIAVAERIrRKIAEEPFIIsdGKERLNVTVSIGVAEL 423
|
170 180 190
....*....|....*....|....*....|
gi 446532590 594 PDYGTDVTELMKNADMAMYRAKANGKNRFV 623
Cdd:PRK09581 424 RPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
640-891 |
1.33e-47 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 177.88 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 640 EGELAKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACLEAKRWHN 719
Cdd:PRK10551 265 GKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 720 QGFSHLKVGVNLSVVQFNHTNLIPTISKVLEEteLKPEALDI--EITESIAINQNQSVvAKLEQLQNLGIQISIDDFGTG 797
Cdd:PRK10551 345 VLPVGAKLGINISPAHLHSDSFKADVQRLLAS--LPADHFQIvlEITERDMVQEEEAT-KLFAWLHSQGIEIAIDDFGTG 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 798 YSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPV 877
Cdd:PRK10551 422 HSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501
|
250
....*....|....
gi 446532590 878 SSKDVWRLLHKKTT 891
Cdd:PRK10551 502 PLEDFVRWLKEPYT 515
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
467-632 |
4.36e-32 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 126.72 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 467 DALTGLPNRRKFEKDLKNilNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQGGDE 546
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 547 FTILLPDmYSEKSAAFIAEQI-LNILNKPFFIQGEELSITPSIGIAMYpDYGTDVTELMKNADMAMYRAKANGKNRFVFF 625
Cdd:PRK09894 210 FIICLKA-ATDEEACRAGERIrQLIANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRNRVMFI 287
|
....*..
gi 446532590 626 SKEISIA 632
Cdd:PRK09894 288 DEQNVIN 294
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
440-624 |
3.75e-31 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 129.75 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 440 VVGMFGiarditTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGD 519
Cdd:PRK15426 380 IRRMVS------NMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGD 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 520 LLLIEVAKRLRSCLRSKDVVARQGGDEFTILLPDMYSEKSAAfIAEQI-LNILNKPFFI-QGEELSITPSIGIAMYPDYG 597
Cdd:PRK15426 454 RVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQ-VAERIrLRINEKEILVaKSTTIRISASLGVSSAEEDG 532
|
170 180
....*....|....*....|....*...
gi 446532590 598 T-DVTELMKNADMAMYRAKANGKNRFVF 624
Cdd:PRK15426 533 DyDFEQLQSLADRRLYLAKQAGRNRVCA 560
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
453-623 |
1.44e-26 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 113.18 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 453 LYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILN--TAQTSAndvAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLR 530
Cdd:PRK09966 237 LQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNnsDARKTS---ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 531 SCLRSKDVVARQGGDEFTILLPDMYSEKSAAFIAEQILNILNKPFFIQ-GEELSITPSIGIAMYPDYGTdVTELMKNADM 609
Cdd:PRK09966 314 EFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHAS-AEKLQELADH 392
|
170
....*....|....
gi 446532590 610 AMYRAKANGKNRFV 623
Cdd:PRK09966 393 NMYQAKHQRAEKLV 406
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
451-621 |
8.73e-26 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 110.30 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 451 TTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLR 530
Cdd:PRK10245 192 TKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 531 SCLRSKDVVARQGGDEFTILLPDMYSEKSAAFIA--EQILNILNKPFFIQgEELSItpSIGIA-MYPDYGtDVTELMKNA 607
Cdd:PRK10245 272 ITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSrvHEGLNTLRLPNAPQ-VTLRI--SVGVApLNPQMS-HYREWLKSA 347
|
170
....*....|....
gi 446532590 608 DMAMYRAKANGKNR 621
Cdd:PRK10245 348 DLALYKAKNAGRNR 361
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
464-878 |
9.55e-22 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 100.71 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 464 AFHDALTGLPNRRKFEKDLKNILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKD--VVAR 541
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPgaLLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 542 QGGDEFTILLPDMySEKSAAFIAEQILNILnkpffiqgeeLSITPS----------IGIAMYPDyGTDVTELMKNADMAM 611
Cdd:PRK11059 308 YSRSDFAVLLPHR-SLKEADSLASQLLKAV----------DALPPPkmldrddflhIGICAYRS-GQSTEQVMEEAEMAL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 612 YRAKANGKNRFVFFSKeisiaQNEIQFLEGE------LAKALQQNEFFLEYQPQVsTKTKQIIGFEALIRWKHPKLGIVS 685
Cdd:PRK11059 376 RSAQLQGGNGWFVYDK-----AQLPEKGRGSvrwrtlLEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGELLS 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 686 PAQFIPLAEETGFIIELGNWILRTACLEAKRWHNQGFShlkvgVNLSVVQFNHTNLIPTISKVLEETElKPEA--LDIEI 763
Cdd:PRK11059 450 AELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEENLS-----INLSVDSLLSRAFQRWLRDTLLQCP-RSQRkrLIFEL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 764 TESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAREFICGITTSPLEEAIISSIITLSKELN 843
Cdd:PRK11059 524 AEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTE 603
|
410 420 430
....*....|....*....|....*....|....*
gi 446532590 844 LEVIAEGVETEEQWKFLYEQNCDNIQGFFISKPVS 878
Cdd:PRK11059 604 TQVFATGVESREEWQTLQELGVSGGQGDFFAESQP 638
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
335-462 |
1.56e-13 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 73.86 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 335 ALSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFIDSKDHDLLKKAL-QLTKKGRPQTL 413
Cdd:COG5809 135 ALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIsQLLKDGGIAQG 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446532590 414 EVRTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEH 462
Cdd:COG5809 215 EVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLRK 263
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
335-606 |
2.18e-13 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 73.47 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 335 ALSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFIDSKDHDLLKKALQ-LTKKGRPQTL 413
Cdd:COG5809 9 QLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKlLKEGESRDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 414 EVRTKEKEGYYYYLHITLIPTFI-NKEVVGMFGIARDITTLYEKQKQVehlafhdaltglpnrRKFEKDLKNILNTAQ-- 490
Cdd:COG5809 89 EFELRHKNGKRLEFSSKLSPIFDqNGDIEGMLAISRDITERKRMEEAL---------------RESEEKFRLIFNHSPdg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 491 ----------TSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVArqggDEFTILLPDmyseksa 560
Cdd:COG5809 154 iivtdldgriIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQ----GEVRFWTKD------- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446532590 561 afiaeqilnilNKPFFIQGEELSITPSIGIAMYPDYGTDVTELMKN 606
Cdd:COG5809 223 -----------GRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKL 257
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
335-549 |
1.04e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 69.28 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 335 ALSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFIDSKDHDLLKKALQLT-KKGRPQTL 413
Cdd:COG2202 5 ALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAAlAGGGVWRG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 414 EVRTKEKEGYYYYLHITLIPTFI-NKEVVGMFGIARDITtlyeKQKQVEhlafhDALtglpnrRKFEKDLKNILNTAQ-- 490
Cdd:COG2202 85 ELRNRRKDGSLFWVELSISPVRDeDGEITGFVGIARDIT----ERKRAE-----EAL------RESEERLRLLVENAPdg 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446532590 491 ----------TSANDVAVMFLDLDRF----KKINDRLGHDVGDLLLIEVAKRLRSCLRSKDVVARQGGDEFTI 549
Cdd:COG2202 150 ifvldldgriLYVNPAAEELLGYSPEellgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRW 222
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
335-461 |
1.25e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 68.90 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 335 ALSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFIDSKDHDLLKKALQ--LTKKGRPQT 412
Cdd:COG2202 131 ALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRrlLEGGRESYE 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446532590 413 LEVRTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITtlyeKQKQVE 461
Cdd:COG2202 211 LELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDIT----ERKRAE 255
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
537-615 |
1.66e-10 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 60.69 E-value: 1.66e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446532590 537 DVVARQGGDEFTILLPDMySEKSAAFIAEQILNILNKPffiqgEELSITPSIGIAMypdygtdvTELMKNADmAMYRAK 615
Cdd:COG3706 116 DLVARYGGEEFAILLPGT-DLEGALAVAERIREAVAEL-----PSLRVTVSIGVAG--------DSLLKRAD-ALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
496-617 |
1.70e-10 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 59.68 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 496 VAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRS-CLRSKDVVARQGGDEFTILLPDMySEKSAAFIAEQILNILNKp 574
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSlIRRSGDLKIKTIGDEFMVVSGLD-HPAAAVAFAEDMREAVSA- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446532590 575 fFIQGEELSITPSIGIA----------MYPDYGTdVTELMKNADMAMYRAKAN 617
Cdd:cd07556 80 -LNQSEGNPVRVRIGIHtgpvvvgvigSRPQYDV-WGALVNLASRMESQAKAG 130
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
339-455 |
2.26e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 56.15 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 339 SEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFtAYYC-EVESYSLLHFIDSKDHDLLKKALQLTKKGRPQT--LEV 415
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIF-GYSAeELIGRNVLELIPEEDREEVRERIERRLEGEPEPvsEER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446532590 416 RTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYE 455
Cdd:TIGR00229 80 RVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKE 119
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
754-882 |
2.22e-08 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 57.50 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 754 LKPEALDIEITESIAINQnqSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKypINTLKIAreficgITTSPLEEaiIS 833
Cdd:COG3434 81 LPPERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID------VLALDLEE--LA 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446532590 834 SIITLSKELNLEVIAEGVETEEQWKFLYEQNCDNIQGFFISKP--VSSKDV 882
Cdd:COG3434 149 ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPeiLKGKKL 199
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
722-878 |
1.26e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 53.85 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 722 FSHLKVGVNLSVVQ------------FNHTNLIPTIS---KVLEETELKPEA---------LDIEITESIAINQNqSVVA 777
Cdd:PRK11596 69 FAEITVSHRLDVVKeqldllaqwadfFVRHGLLASVNidgPTLIALRQQPAIlrlierlpwLRFELVEHIRLPKD-SPFA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 778 KLEQLQNLGIqisiDDFGTG---YSSLAyLTKYpiNTLKIAREFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETE 854
Cdd:PRK11596 148 SMCEFGPLWL----DDFGTGmanFSALS-EVRY--DYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETP 220
|
170 180
....*....|....*....|....
gi 446532590 855 EQWKFLYEQNCDNIQGFFISKPVS 878
Cdd:PRK11596 221 EEWRDVQRSPAFAAQGYFLSRPAP 244
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
335-472 |
1.23e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 51.77 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 335 ALSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLF--TAYYCEVESYSLLHFIDSKDHDLLKKALQltkKGRPQT 412
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLglSAEELLGRPLAELFPEDSPLRELLERALA---EGQPVT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446532590 413 -LEVRTKEKEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEHLAFHDALTGL 472
Cdd:COG3852 78 eREVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
341-450 |
4.49e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 46.26 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 341 QRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFTAYYCEVESYSLLHFI----DSKDHDLLKKALQLTkkGRPQTLEVR 416
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIpeedDAEVAELLRQALLQG--EESRGFEVS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 446532590 417 TKEKEGYYYYLHITLIP-TFINKEVVGMFGIARDI 450
Cdd:pfam00989 79 FRVPDGRPRHVEVRASPvRDAGGEILGFLGVLRDI 113
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
336-499 |
3.52e-05 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 47.07 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 336 LSKSEQRYKSLFEDHPDAVFSLNMYGIFQQSNTACESLFtayycEVESYSLL--HFIDSKDHDLLKKALqltKKGRPQTL 413
Cdd:COG3829 6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERIL-----GLPREEVIgkNVTELIPNSPLLEVL---KTGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532590 414 EVRTKEKEGYYYYlhITLIPTFINKEVVGMFGIARDITTLYEKQKQVEHlafHDALTGLPNRRKFE------KDLKNILN 487
Cdd:COG3829 78 VIQKTGGKGKTVI--VTAIPIFEDGEVIGAVETFRDITELKRLERKLRE---EELERGLSAKYTFDdiigksPAMKELLE 152
|
170
....*....|...
gi 446532590 488 TAQTSAN-DVAVM 499
Cdd:COG3829 153 LAKRVAKsDSTVL 165
|
|
| |
