|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
372-878 |
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: 673.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 372 ASHSLLHFIDPKDHDLLKRALQITKEGRPQTLEVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVE 451
Cdd:COG5001 169 LLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLR 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 452 HLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVAR 531
Cdd:COG5001 249 HLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVAR 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 532 QGGDEFTILLPDMYSEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNR 611
Cdd:COG5001 329 LGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 612 FVFFSKEISIAQNEIQFLEGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIE 691
Cdd:COG5001 409 YRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVP 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 692 LGNWILRTACSEAKRWHNQGFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQ 771
Cdd:COG5001 489 LGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 772 LQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLY 851
Cdd:COG5001 569 LRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLR 648
|
490 500
....*....|....*....|....*..
gi 2283786088 852 EQNCDHIQGFFISKPVSSKDVWMLLHK 878
Cdd:COG5001 649 ELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| DUF4084 |
pfam13321 |
Domain of unknown function (DUF4084); This family of Firmicute proteins is frequently ... |
1-294 |
1.42e-151 |
|
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: 447.85 E-value: 1.42e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 1 VMMYIIVFSLWIFLIPNEWNIKEIGILFLFCFAAIFSCYCSYKAIKKMKRGDKLFWVLLLCTCLCGLAMEITLFLHSLSI 80
Cdd:pfam13321 11 VTMYIIIFSLWIFLIPKDLNIKEIGILFLFCFATLFSCYCLYKAIKKMKRGDKLFWVLVLCTCLCGLTMEITLFLHSLSI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 81 CDQVLFSYEALPFFIIQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIVIMNIYFTLTFILDLSSFHTLTKDTWVLIGYF 160
Cdd:pfam13321 91 YDQVIFSYKALPFFIVQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIVIMNIYFTLTFILDISSFRMLTTDTWVLIGYF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 161 IAQSLVIYAVISLYRREQYSSSRISLIIGFTIILVYGYIQLFQLNTGIKTSAEFSYLIHTASILLIGLSSILYILDKPMQ 240
Cdd:pfam13321 171 IAQSLVIYAVISLYRREEYSSSRISLIIGFTIILVYGYIHLFQLNAGIKPSSEVSYLIHTASILLIGLSSILYILDKPIQ 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2283786088 241 HETKTKYYRFDYVRFILPYFSIIMTFSFIIIQPWDDKFMLIGLVLSLILLFLRQ 294
Cdd:pfam13321 251 HETKTKYYRFDYVRFILPYFSIIITFSFIIFQPWDDKFMLIGLVLSLILLFLRQ 304
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
439-879 |
8.69e-120 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 378.26 E-value: 8.69e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 439 DITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILNTAqtSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKR 518
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 519 LRGCLRSKDIVARQGGDEFTILLPDMySEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNAD 598
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHT-SQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 599 MAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELSKALQQNEFFLEYQPQVSTkTKQIIGFEALIRWKHPKLGIVSPAQ 678
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 679 FIPLAEETGFIIELGNWILRTACSEAKRWHNQGFShLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIA 758
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 759 INQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIA 838
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2283786088 839 EGVETEEQWKFLYEQNCDHIQGFFISKPVSSKDV--WMLLHKK 879
Cdd:PRK10060 617 EGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFerWYKRYLK 659
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
631-868 |
3.56e-111 |
|
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: 340.68 E-value: 3.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 631 GELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWHnQ 710
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 711 GFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSS 790
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2283786088 791 LAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPVS 868
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
630-867 |
1.72e-101 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 315.31 E-value: 1.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 630 EGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWHN 709
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 710 QGFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYS 789
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2283786088 790 SLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPV 867
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
632-866 |
3.16e-77 |
|
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: 250.70 E-value: 3.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 632 ELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWhnQG 711
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 712 FSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSL 791
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2283786088 792 AYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKP 866
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
453-615 |
1.97e-48 |
|
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: 169.05 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 453 LAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQ 532
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 533 GGDEFTILLPDMYSEkSAAFIAEQILTILN-KPFFI-KDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKN 610
Cdd:TIGR00254 81 GGEEFVVILPGTPLE-DALSKAERLRDAINsKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 2283786088 611 RFVFF 615
Cdd:TIGR00254 160 RVVVA 164
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
331-393 |
7.59e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 38.53 E-value: 7.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2283786088 331 QRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRALQ 393
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQ 63
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
372-878 |
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: 673.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 372 ASHSLLHFIDPKDHDLLKRALQITKEGRPQTLEVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVE 451
Cdd:COG5001 169 LLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLR 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 452 HLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVAR 531
Cdd:COG5001 249 HLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVAR 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 532 QGGDEFTILLPDMYSEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNR 611
Cdd:COG5001 329 LGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 612 FVFFSKEISIAQNEIQFLEGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIE 691
Cdd:COG5001 409 YRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVP 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 692 LGNWILRTACSEAKRWHNQGFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQ 771
Cdd:COG5001 489 LGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 772 LQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLY 851
Cdd:COG5001 569 LRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLR 648
|
490 500
....*....|....*....|....*..
gi 2283786088 852 EQNCDHIQGFFISKPVSSKDVWMLLHK 878
Cdd:COG5001 649 ELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| DUF4084 |
pfam13321 |
Domain of unknown function (DUF4084); This family of Firmicute proteins is frequently ... |
1-294 |
1.42e-151 |
|
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: 447.85 E-value: 1.42e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 1 VMMYIIVFSLWIFLIPNEWNIKEIGILFLFCFAAIFSCYCSYKAIKKMKRGDKLFWVLLLCTCLCGLAMEITLFLHSLSI 80
Cdd:pfam13321 11 VTMYIIIFSLWIFLIPKDLNIKEIGILFLFCFATLFSCYCLYKAIKKMKRGDKLFWVLVLCTCLCGLTMEITLFLHSLSI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 81 CDQVLFSYEALPFFIIQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIVIMNIYFTLTFILDLSSFHTLTKDTWVLIGYF 160
Cdd:pfam13321 91 YDQVIFSYKALPFFIVQYILLFSGFAIKFIKHYSIRGLAQFSFDSIFIVIMNIYFTLTFILDISSFRMLTTDTWVLIGYF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 161 IAQSLVIYAVISLYRREQYSSSRISLIIGFTIILVYGYIQLFQLNTGIKTSAEFSYLIHTASILLIGLSSILYILDKPMQ 240
Cdd:pfam13321 171 IAQSLVIYAVISLYRREEYSSSRISLIIGFTIILVYGYIHLFQLNAGIKPSSEVSYLIHTASILLIGLSSILYILDKPIQ 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2283786088 241 HETKTKYYRFDYVRFILPYFSIIMTFSFIIIQPWDDKFMLIGLVLSLILLFLRQ 294
Cdd:pfam13321 251 HETKTKYYRFDYVRFILPYFSIIITFSFIIFQPWDDKFMLIGLVLSLILLFLRQ 304
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
376-877 |
1.31e-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: 382.98 E-value: 1.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 376 LLHFIDPKDHDLLKRALQITKEGRPQTLEVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEHLAF 455
Cdd:COG2200 76 LLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 456 HDALTGLPNRRKFEKDLKTILNTAQTSAND-VAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQGG 534
Cdd:COG2200 156 LDLLLLLLLRRLLLLLLLLLLLLLLALALLaLLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 535 DEFTILLPDMYSEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNRFVF 614
Cdd:COG2200 236 GGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 615 FSKEISIAQNEIQfLEGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGN 694
Cdd:COG2200 316 FAAAEARARRRLA-LESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 695 WILRTACSEAKRWHNQGFShLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQN 774
Cdd:COG2200 395 WVLERALRQLARWPERGLD-LRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 775 LGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQN 854
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
490 500
....*....|....*....|...
gi 2283786088 855 CDHIQGFFISKPVSSKDVWMLLH 877
Cdd:COG2200 554 CDYAQGYLFGRPLPLEELEALLR 576
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
439-879 |
8.69e-120 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 378.26 E-value: 8.69e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 439 DITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILNTAqtSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKR 518
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 519 LRGCLRSKDIVARQGGDEFTILLPDMySEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNAD 598
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHT-SQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 599 MAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELSKALQQNEFFLEYQPQVSTkTKQIIGFEALIRWKHPKLGIVSPAQ 678
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 679 FIPLAEETGFIIELGNWILRTACSEAKRWHNQGFShLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIA 758
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 759 INQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIA 838
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2283786088 839 EGVETEEQWKFLYEQNCDHIQGFFISKPVSSKDV--WMLLHKK 879
Cdd:PRK10060 617 EGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFerWYKRYLK 659
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
631-868 |
3.56e-111 |
|
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: 340.68 E-value: 3.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 631 GELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWHnQ 710
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 711 GFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSS 790
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2283786088 791 LAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPVS 868
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
445-874 |
1.40e-106 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 347.53 E-value: 1.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 445 EKQKQVEHLAFHDALTGLPNRRKFEKDLKTILNTAQtsanDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLR 524
Cdd:PRK11359 367 KSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 525 SKDIVARQGGDEFTILLPDMySEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMypDYGNDVTELMKNADMAMYRA 604
Cdd:PRK11359 443 PDQYLCRIEGTQFVLVSLEN-DVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 605 KANGKNRFVFFSKEISIAQNEIQFLEGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAE 684
Cdd:PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 685 ETGFIIELGNWILRTACSEAKRWHNQGFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQS 764
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTE 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 765 VVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETE 844
Cdd:PRK11359 680 IFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETK 759
|
410 420 430
....*....|....*....|....*....|..
gi 2283786088 845 EQWKFLYEQNCDHIQGFFISKPVSSKDV--WM 874
Cdd:PRK11359 760 EQFEMLRKIHCRVIQGYFFSRPLPAEEIpgWM 791
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
630-867 |
1.72e-101 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 315.31 E-value: 1.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 630 EGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWHN 709
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 710 QGFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYS 789
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2283786088 790 SLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPV 867
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
632-866 |
3.16e-77 |
|
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: 250.70 E-value: 3.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 632 ELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWhnQG 711
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 712 FSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSL 791
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2283786088 792 AYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKP 866
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
453-867 |
1.07e-76 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 262.73 E-value: 1.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 453 LAFHDALTGLPNRRKFEKDLKTILNTAQTSAndvaVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQ 532
Cdd:PRK13561 230 NATRFPVSDLPNKALLMALLEQVVARKQTTA----LMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 533 GGDEFTILLPDMYSEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYpdYGN-DVTELMKNADMAMYRAKANGKNR 611
Cdd:PRK13561 306 SGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF--YGDlTAEQLYSRAISAAFTARRKGKNQ 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 612 FVFFSKEISIAQNEIQFLEGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIE 691
Cdd:PRK13561 384 IQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVT 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 692 LGNWILRTACSEAKRWHNQGFShLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQ 771
Cdd:PRK13561 464 VGHWVLEESCRLLAAWQERGIM-LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRP 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 772 LQNLGIQISIDDFGTGYSSLAYLTKY---PINTLKIAQEFICGIttsPLEEAIISSIITLSKELNLEVIAEGVETEEQWK 848
Cdd:PRK13561 543 LRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRD 619
|
410
....*....|....*....
gi 2283786088 849 FLYEQNCDHIQGFFISKPV 867
Cdd:PRK13561 620 WLLKAGVGIAQGFLFARAL 638
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
399-871 |
3.31e-76 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 261.80 E-value: 3.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 399 RPQTLEVRTKEQEGYYYYlHITLIPTFINKEV-VGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILn 477
Cdd:PRK11829 177 RAMAKELEDIGDHGVLHH-QLTLPAHHQDDELgVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEI- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 478 TAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQGGDEFTILLPDMYSEKSAAFIAEQI 557
Cdd:PRK11829 255 ASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 558 LTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNRFVFFSKEISIAQNEIQFLEGELSKAL 637
Cdd:PRK11829 335 MSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 638 QQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWHNQGFShLKV 717
Cdd:PRK11829 415 ENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVS-LPL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 718 GVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYL--- 794
Cdd:PRK11829 494 SVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhl 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2283786088 795 TKYPINTLKIAQEFICGIttsPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPVSSKD 871
Cdd:PRK11829 574 KSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE 647
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
429-867 |
1.53e-74 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 265.00 E-value: 1.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 429 EVVGMFGIARDITTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVG 508
Cdd:PRK09776 640 ENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAG 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 509 DLLLIEVAKRLRGCLRSKDIVARQGGDEFTILLPDMySEKSAAFIAEQIL-TILNKPFFIKDEELSVTPSIGIAMYPDYG 587
Cdd:PRK09776 720 DALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDC-NVESARFIATRIIsAINDYHFPWEGRVYRVGASAGITLIDANN 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 588 NDVTELMKNADMAMYRAKANGKNRFVFFSKEisiaQNEIQFLEGELSKALQQ-----NEFFLEYQPQVSTKTKQIIGF-E 661
Cdd:PRK09776 799 HQASEVMSQADIACYAAKNAGRGRVTVYEPQ----QAAAHSEHRALSLAEQWrmikeNQLMMLAHGVASPRIPEARNHwL 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 662 ALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSE-AKRWHNQGFShlkVGVNLSVVQFNHTDLIPTISKVLK 740
Cdd:PRK09776 875 ISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQaAKAVASKGLS---IALPLSVAGLSSPTLLPFLLEQLE 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 741 ETELKPEALDIEITESIAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEA 820
Cdd:PRK09776 952 NSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEM 1031
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2283786088 821 IISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPV 867
Cdd:PRK09776 1032 LISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
370-615 |
1.48e-73 |
|
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: 242.58 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 370 EVASHSLLHFIDPKDHDLLKRALQITKEGRPQTLEVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQ 449
Cdd:COG2199 30 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 450 VEHLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIV 529
Cdd:COG2199 110 LRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 530 ARQGGDEFTILLPDMySEKSAAFIAEQILTILNK-PFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANG 608
Cdd:COG2199 190 ARLGGDEFAVLLPGT-DLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAG 268
|
....*..
gi 2283786088 609 KNRFVFF 615
Cdd:COG2199 269 RNRVVVY 275
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
629-871 |
4.95e-72 |
|
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: 246.75 E-value: 4.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 629 LEGELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWH 708
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 709 nQGFSHLKVGVNLSVVQFNHTDLIPTISKVLKETELKPEALDIEITESIAINQNQSVvAKLEQLQNLGIQISIDDFGTGY 788
Cdd:COG4943 352 -AADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAIDDFGTGY 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 789 SSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPVS 868
Cdd:COG4943 430 SSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLP 509
|
...
gi 2283786088 869 SKD 871
Cdd:COG4943 510 AEE 512
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
455-613 |
1.56e-71 |
|
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: 232.45 E-value: 1.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 455 FHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQGG 534
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2283786088 535 DEFTILLPDMySEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNRFV 613
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
454-611 |
1.85e-64 |
|
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: 213.27 E-value: 1.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 454 AFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQG 533
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 534 GDEFTILLPD--MYSEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNR 611
Cdd:pfam00990 81 GDEFAILLPEtsLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
452-615 |
6.13e-64 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 212.11 E-value: 6.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 452 HLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVAR 531
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 532 QGGDEFTILLPDMySEKSAAFIAEQILTILNKPFFIKDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKNR 611
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 2283786088 612 FVFF 615
Cdd:smart00267 160 VAVY 163
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
436-613 |
6.30e-49 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 180.10 E-value: 6.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 436 IARDITTLYEKQKQ------VEH---LAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHD 506
Cdd:PRK09581 265 LARVRTQIRRKRYQdalrnnLEQsieMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 507 VGDLLLIEVAKRLRGCLRSKDIVARQGGDEFTILLPDMYSEKsAAFIAEQI-LTILNKPFFI--KDEELSVTPSIGIAMY 583
Cdd:PRK09581 345 AGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIED-AIAVAERIrRKIAEEPFIIsdGKERLNVTVSIGVAEL 423
|
170 180 190
....*....|....*....|....*....|
gi 2283786088 584 PDYGNDVTELMKNADMAMYRAKANGKNRFV 613
Cdd:PRK09581 424 RPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
453-615 |
1.97e-48 |
|
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: 169.05 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 453 LAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQ 532
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 533 GGDEFTILLPDMYSEkSAAFIAEQILTILN-KPFFI-KDEELSVTPSIGIAMYPDYGNDVTELMKNADMAMYRAKANGKN 610
Cdd:TIGR00254 81 GGEEFVVILPGTPLE-DALSKAERLRDAINsKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 2283786088 611 RFVFF 615
Cdd:TIGR00254 160 RVVVA 164
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
632-881 |
2.12e-47 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 177.11 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 632 ELSKALQQNEFFLEYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIPLAEETGFIIELGNWILRTACSEAKRWHNQG 711
Cdd:PRK10551 267 EILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 712 FSHLKVGVNLSVVQFNHTDLIPTISKVLkeTELKPEALDI--EITESIAINQNQSVvAKLEQLQNLGIQISIDDFGTGYS 789
Cdd:PRK10551 347 PVGAKLGINISPAHLHSDSFKADVQRLL--ASLPADHFQIvlEITERDMVQEEEAT-KLFAWLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 790 SLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKPVSS 869
Cdd:PRK10551 424 ALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPL 503
|
250
....*....|..
gi 2283786088 870 KDVWMLLHKKTT 881
Cdd:PRK10551 504 EDFVRWLKEPYT 515
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
430-614 |
2.96e-32 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 132.83 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 430 VVGMFGiarditTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGD 509
Cdd:PRK15426 380 IRRMVS------NMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGD 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 510 LLLIEVAKRLRGCLRSKDIVARQGGDEFTILLPDMYSEKSAAfIAEQI-LTILNKPFFI-KDEELSVTPSIGIAMYPDYG 587
Cdd:PRK15426 454 RVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQ-VAERIrLRINEKEILVaKSTTIRISASLGVSSAEEDG 532
|
170 180
....*....|....*....|....*...
gi 2283786088 588 N-DVTELMKNADMAMYRAKANGKNRFVF 614
Cdd:PRK15426 533 DyDFEQLQSLADRRLYLAKQAGRNRVCA 560
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
457-622 |
7.05e-31 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 123.25 E-value: 7.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 457 DALTGLPNRRKFEKDLKTilNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQGGDE 536
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 537 FTILLPDmYSEKSAAFIAEQI-LTILNKPFFIKDEELSVTPSIGIAMYpDYGNDVTELMKNADMAMYRAKANGKNRFVFF 615
Cdd:PRK09894 210 FIICLKA-ATDEEACRAGERIrQLIANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRNRVMFI 287
|
....*..
gi 2283786088 616 SKEISIA 622
Cdd:PRK09894 288 DEQNVIN 294
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
443-613 |
3.18e-25 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 109.33 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 443 LYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILN--TAQTSAndvAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLR 520
Cdd:PRK09966 237 LQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNnsDARKTS---ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 521 GCLRSKDIVARQGGDEFTILLPDMYSEKSAAFIAEQILTILNKPFFIKDEEL-SVTPSIGIAMYPDYGNdVTELMKNADM 599
Cdd:PRK09966 314 EFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQtTMTLSIGYAMTIEHAS-AEKLQELADH 392
|
170
....*....|....
gi 2283786088 600 AMYRAKANGKNRFV 613
Cdd:PRK09966 393 NMYQAKHQRAEKLV 406
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
441-611 |
1.43e-23 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 103.37 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 441 TTLYEKQKQVEHLAFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLR 520
Cdd:PRK10245 192 TKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 521 GCLRSKDIVARQGGDEFTILLPDMYSEKSAAFIAE-----QILTILNKPffikdeELSVTPSIGIA-MYPDYGNdVTELM 594
Cdd:PRK10245 272 ITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRvheglNTLRLPNAP------QVTLRISVGVApLNPQMSH-YREWL 344
|
170
....*....|....*..
gi 2283786088 595 KNADMAMYRAKANGKNR 611
Cdd:PRK10245 345 KSADLALYKAKNAGRNR 361
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
454-868 |
2.85e-22 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 102.25 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 454 AFHDALTGLPNRRKFEKDLKTILNTAQTSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKD--IVAR 531
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPgaLLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 532 QGGDEFTILLPDMySEKSAAFIAEQILTILNK----PFFIKDEELsvtpSIGIAMYPDyGNDVTELMKNADMAMYRAKAN 607
Cdd:PRK11059 308 YSRSDFAVLLPHR-SLKEADSLASQLLKAVDAlpppKMLDRDDFL----HIGICAYRS-GQSTEQVMEEAEMALRSAQLQ 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 608 GKNRFVFFSKeisiaQNEIQFLEGE------LSKALQQNEFFLeYQPQVSTKTKQIIGFEALIRWKHPKLGIVSPAQFIP 681
Cdd:PRK11059 382 GGNGWFVYDK-----AQLPEKGRGSvrwrtlLEQTLVRGGPRL-YQQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 682 LAEETGFIIELGNWILRTACSEAKRWHNQGFShlkvgVNLSVVQFNHTDLIptisKVLKETEL---KPEA--LDIEITES 756
Cdd:PRK11059 456 MVQQLGLSEQYDRQVIERVLPLLRYWPEENLS-----INLSVDSLLSRAFQ----RWLRDTLLqcpRSQRkrLIFELAEA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 757 IAINQNQSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKYPINTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEV 836
Cdd:PRK11059 527 DVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQV 606
|
410 420 430
....*....|....*....|....*....|..
gi 2283786088 837 IAEGVETEEQWKFLYEQNCDHIQGFFISKPVS 868
Cdd:PRK11059 607 FATGVESREEWQTLQELGVSGGQGDFFAESQP 638
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
325-451 |
4.03e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 73.14 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 325 ALSKSEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRALQ--ITKEGRPQT 402
Cdd:COG2202 131 ALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRrlLEGGRESYE 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2283786088 403 LEVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITtlyeKQKQVE 451
Cdd:COG2202 211 LELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDIT----ERKRAE 255
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
325-539 |
5.34e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 325 ALSKSEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRAL-QITKEGRPQTL 403
Cdd:COG2202 5 ALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLrAALAGGGVWRG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 404 EVRTKEQEGYYYYLHITLIPTFI-NKEVVGMFGIARDITtlyeKQKQVEhlafhDALtglpnrRKFEKDLKTILNTAQ-- 480
Cdd:COG2202 85 ELRNRRKDGSLFWVELSISPVRDeDGEITGFVGIARDIT----ERKRAE-----EAL------RESEERLRLLVENAPdg 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2283786088 481 ----------TSANDVAVMFLDLDRF----KKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVARQGGDEFTI 539
Cdd:COG2202 150 ifvldldgriLYVNPAAEELLGYSPEellgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRW 222
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
325-452 |
8.29e-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: 71.54 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 325 ALSKSEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRAL-QITKEGRPQTL 403
Cdd:COG5809 135 ALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIsQLLKDGGIAQG 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2283786088 404 EVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEH 452
Cdd:COG5809 215 EVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLRK 263
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
325-543 |
2.13e-12 |
|
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: 70.39 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 325 ALSKSEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRALQITKEGR-PQTL 403
Cdd:COG5809 9 QLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGEsRDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 404 EVRTKEQEGYYYYLHITLIPTFI-NKEVVGMFGIARDITTLYEKQKQVehlafhdaltglpnrRKFEKDLKTILNTAQ-- 480
Cdd:COG5809 89 EFELRHKNGKRLEFSSKLSPIFDqNGDIEGMLAISRDITERKRMEEAL---------------RESEEKFRLIFNHSPdg 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2283786088 481 ----------TSANDVAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLRGCLRSKDIVArqggDEFTILLPD 543
Cdd:COG5809 154 iivtdldgriIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQ----GEVRFWTKD 222
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
527-605 |
1.04e-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: 61.46 E-value: 1.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2283786088 527 DIVARQGGDEFTILLPDMySEKSAAFIAEQILTILNKPffikdEELSVTPSIGIAMypdygndvTELMKNADmAMYRAK 605
Cdd:COG3706 116 DLVARYGGEEFAILLPGT-DLEGALAVAERIREAVAEL-----PSLRVTVSIGVAG--------DSLLKRAD-ALYQAR 179
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
329-445 |
8.39e-10 |
|
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: 57.30 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 329 SEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFtAYYC-EVASHSLLHFIDPKDHDLLKRALQ--ITKEGRPQTLEV 405
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIF-GYSAeELIGRNVLELIPEEDREEVRERIErrLEGEPEPVSEER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2283786088 406 RTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYE 445
Cdd:TIGR00229 80 RVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKE 119
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
486-581 |
1.00e-09 |
|
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: 57.37 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 486 VAVMFLDLDRFKKINDRLGHDVGDLLLIEVAKRLR-GCLRSKDIVARQGGDEFTILLPDMySEKSAAFIAEQILTILNKp 564
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDsLIRRSGDLKIKTIGDEFMVVSGLD-HPAAAVAFAEDMREAVSA- 79
|
90
....*....|....*...
gi 2283786088 565 ffIKDEELS-VTPSIGIA 581
Cdd:cd07556 80 --LNQSEGNpVRVRIGIH 95
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
744-872 |
4.92e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 59.43 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 744 LKPEALDIEITESIAINQnqSVVAKLEQLQNLGIQISIDDFGTGYSSLAYLTKypINTLKIAqeficgITTSPLEEaiIS 823
Cdd:COG3434 81 LPPERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID------VLALDLEE--LA 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2283786088 824 SIITLSKELNLEVIAEGVETEEQWKFLYEQNCDHIQGFFISKP--VSSKDV 872
Cdd:COG3434 149 ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPeiLKGKKL 199
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
325-462 |
1.53e-08 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 57.55 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 325 ALSKSEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIdPKDHDLLKRALQITKEGRPQT-L 403
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELF-PEDSPLRELLERALAEGQPVTeR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2283786088 404 EVRTKEQEGYYYYLHITLIPTFINKEVVGMFGIARDITTLYEKQKQVEHLAFHDALTGL 462
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
712-868 |
1.04e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 51.16 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 712 FSHLKVGVNLSVVQ------------FNHTDLIPTIS---KVLKETELKPEA---------LDIEITESIAINQNqSVVA 767
Cdd:PRK11596 69 FAEITVSHRLDVVKeqldllaqwadfFVRHGLLASVNidgPTLIALRQQPAIlrlierlpwLRFELVEHIRLPKD-SPFA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 768 KLEQLQNLGIqisiDDFGTG---YSSLAyLTKYpiNTLKIAQEFICGITTSPLEEAIISSIITLSKELNLEVIAEGVETE 844
Cdd:PRK11596 148 SMCEFGPLWL----DDFGTGmanFSALS-EVRY--DYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETP 220
|
170 180
....*....|....*....|....
gi 2283786088 845 EQWKFLYEQNCDHIQGFFISKPVS 868
Cdd:PRK11596 221 EEWRDVQRSPAFAAQGYFLSRPAP 244
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
331-440 |
1.75e-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: 47.41 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 331 QRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRALQITKEGR--PQTLEVRTK 408
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGeeSRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|...
gi 2283786088 409 EQEGYYYYLHITLIP-TFINKEVVGMFGIARDI 440
Cdd:pfam00989 81 VPDGRPRHVEVRASPvRDAGGEILGFLGVLRDI 113
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
326-452 |
3.44e-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: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 326 LSKSEQRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDpkdHDLLKRALqitKEGRPQTLEV 405
Cdd:COG3829 6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP---NSPLLEVL---KTGKPVTGVI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2283786088 406 RTKEQEGYYYYlhITLIPTFINKEVVGMFGIARDITTLYEKQKQVEH 452
Cdd:COG3829 80 QKTGGKGKTVI--VTAIPIFEDGEVIGAVETFRDITELKRLERKLRE 124
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
331-393 |
7.59e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 38.53 E-value: 7.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2283786088 331 QRYKSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIDPKDHDLLKRALQ 393
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQ 63
|
|
| TyrR |
COG3283 |
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ... |
329-422 |
9.66e-03 |
|
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];
Pssm-ID: 442513 [Multi-domain] Cd Length: 514 Bit Score: 39.40 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283786088 329 SEQRY---KSLFEDHPDAVFSLNMHGIFQQSNTACESLFTAYYCEVASHSLLHFIdpKDHDLLkRALQiTKEGRPQTLEV 405
Cdd:COG3283 75 SEREHlelDALLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQPLSELL--KGFNFS-RWLE-SNEPRPQSERV 150
|
90
....*....|....*..
gi 2283786088 406 RTKEQEgyyYYLHITLI 422
Cdd:COG3283 151 VINGQD---YLADILPI 164
|
|
| |
