|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-587 |
2.47e-110 |
|
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: 344.84 E-value: 2.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 1 MATPPYPEDEHSRQAYVDQLGLLEEGADEVFEEILAAATSYFQTPIALISILDHQRQWFRASIGLDIRQTPRRDSFCAYA 80
Cdd:COG5001 76 ALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 81 ILGKGVFEVADATLDPRFRDNPYVQGEPRIRFYAGAPLATAEGLNLGSLCVIDREPRGPLAERDVAMLEHFARLVMARIH 160
Cdd:COG5001 156 ALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIAR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 161 TLRSTN----------YIDEPTGLYNRLRLQEDVSLRLQR----DGALTVIaadllplallntII---------RTLGYP 217
Cdd:COG5001 236 LITERKraeerlrhlaYHDPLTGLPNRRLFLDRLEQALARarrsGRRLALL------------FIdldrfkeinDTLGHA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 218 FSNDLMLEARDRIRAELPDF-TLYKISPTRFGLLLPR-QQQEETESVCLRLLRAFESPVVCRG--IPIKANVGLGVLPla 293
Cdd:COG5001 304 AGDELLREVARRLRACLREGdTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGheLYVSASIGIALYP-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 294 DDPLDGDQdwlrlVVSAAD----DARDRGVG-WARYNPPLDQAQQRAFTLLTSLSQAIGTEEgFHLVYQPKIDLPTGRCT 368
Cdd:COG5001 382 DDGADAEE-----LLRNADlamyRAKAAGRNrYRFFDPEMDERARERLELEADLRRALERGE-LELHYQPQVDLATGRIV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 369 GVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNI-PLRLAINVSASDMEDSSFLEEAVRL 447
Cdd:COG5001 456 GAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLpDLRVAVNLSARQLRDPDLVDRVRRA 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 448 AKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKA 527
Cdd:COG5001 536 LAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDD 615
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 528 QSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQLEDWLRR 587
Cdd:COG5001 616 AAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
340-580 |
2.99e-101 |
|
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: 306.39 E-value: 2.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 340 TSLSQAIGTEEgFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNA 419
Cdd:cd01948 1 ADLRRALERGE-FELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 420 RNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSN 499
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 500 WTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPE 579
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 489193161 580 Q 580
Cdd:cd01948 240 E 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
342-580 |
1.02e-87 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 271.78 E-value: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 342 LSQAIgTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARN 421
Cdd:smart00052 4 LRQAL-ENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 422 I-PLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNW 500
Cdd:smart00052 83 PpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 501 TYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQ 580
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
341-575 |
2.62e-76 |
|
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: 241.84 E-value: 2.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 341 SLSQAIGTEEgFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWnAR 420
Cdd:pfam00563 3 ALRRALENGE-FVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 421 NIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNW 500
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489193161 501 TYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQP 575
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
215-587 |
1.50e-68 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 234.19 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 215 GYPFSNDLMLEARDRIRAELP-DFTLYKISPTRFGLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVlplA 293
Cdd:PRK10060 285 GHMFGDQLLQDVSLAILSCLEeDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGI---A 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 294 DDPLDGDQdwLRLVVSAADDA----RDRGVGWARYNPPldQAQQRAFTLL---TSLSQAIgTEEGFHLVYQPKIDLpTGR 366
Cdd:PRK10060 362 LAPEHGDD--SESLIRSADTAmytaKEGGRGQFCVFSP--EMNQRVFEYLwldTNLRKAL-ENDQLVIHYQPKITW-RGE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 367 CTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVR 446
Cdd:PRK10060 436 VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 447 LAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPK 526
Cdd:PRK10060 516 ALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPV 595
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489193161 527 AQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQLEDWLRR 587
Cdd:PRK10060 596 SQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-587 |
2.47e-110 |
|
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: 344.84 E-value: 2.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 1 MATPPYPEDEHSRQAYVDQLGLLEEGADEVFEEILAAATSYFQTPIALISILDHQRQWFRASIGLDIRQTPRRDSFCAYA 80
Cdd:COG5001 76 ALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 81 ILGKGVFEVADATLDPRFRDNPYVQGEPRIRFYAGAPLATAEGLNLGSLCVIDREPRGPLAERDVAMLEHFARLVMARIH 160
Cdd:COG5001 156 ALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIAR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 161 TLRSTN----------YIDEPTGLYNRLRLQEDVSLRLQR----DGALTVIaadllplallntII---------RTLGYP 217
Cdd:COG5001 236 LITERKraeerlrhlaYHDPLTGLPNRRLFLDRLEQALARarrsGRRLALL------------FIdldrfkeinDTLGHA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 218 FSNDLMLEARDRIRAELPDF-TLYKISPTRFGLLLPR-QQQEETESVCLRLLRAFESPVVCRG--IPIKANVGLGVLPla 293
Cdd:COG5001 304 AGDELLREVARRLRACLREGdTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGheLYVSASIGIALYP-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 294 DDPLDGDQdwlrlVVSAAD----DARDRGVG-WARYNPPLDQAQQRAFTLLTSLSQAIGTEEgFHLVYQPKIDLPTGRCT 368
Cdd:COG5001 382 DDGADAEE-----LLRNADlamyRAKAAGRNrYRFFDPEMDERARERLELEADLRRALERGE-LELHYQPQVDLATGRIV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 369 GVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNI-PLRLAINVSASDMEDSSFLEEAVRL 447
Cdd:COG5001 456 GAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLpDLRVAVNLSARQLRDPDLVDRVRRA 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 448 AKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKA 527
Cdd:COG5001 536 LAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDD 615
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 528 QSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQLEDWLRR 587
Cdd:COG5001 616 AAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
340-580 |
2.99e-101 |
|
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: 306.39 E-value: 2.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 340 TSLSQAIGTEEgFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNA 419
Cdd:cd01948 1 ADLRRALERGE-FELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 420 RNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSN 499
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 500 WTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPE 579
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 489193161 580 Q 580
Cdd:cd01948 240 E 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
10-586 |
4.43e-101 |
|
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: 317.88 E-value: 4.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 10 EHSRQAYVDQLGLLEEGADEVFEEILAAATSYFQTPIALISILDHQRQWFRASIGLDIRQTPRRDSFCAYAILGKGVFEV 89
Cdd:COG2200 2 LLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 90 ADATLDPRFRDNPYVQGEPRIRFYAGAPLATAEGLNLGSLCVIDREPRGPLAERDVAMLEHFARLVMARIHTLRSTNYID 169
Cdd:COG2200 82 LLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 170 EPTGLYNRLRLQEDVSLRLQRDGALTVIAADLLPLALLNTIIRTLGYPFSNDLMLEARDRIRAELPDFTLYKISPTRFGL 249
Cdd:COG2200 162 LLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 250 LLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVLPLADDPLDGDQDWLRLVVSAADDARDRGVGWARYNPPLD 329
Cdd:COG2200 242 LLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 330 QAQQRaFTLLTSLSQAIgTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRH 409
Cdd:COG2200 322 RARRR-LALESELREAL-EEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 410 AMAQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIA 489
Cdd:COG2200 400 ALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 490 VDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQG 569
Cdd:COG2200 480 LDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQG 559
|
570
....*....|....*..
gi 489193161 570 YLIAQPMLPEQLEDWLR 586
Cdd:COG2200 560 YLFGRPLPLEELEALLR 576
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
342-580 |
1.02e-87 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 271.78 E-value: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 342 LSQAIgTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARN 421
Cdd:smart00052 4 LRQAL-ENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 422 I-PLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNW 500
Cdd:smart00052 83 PpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 501 TYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQ 580
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
341-575 |
2.62e-76 |
|
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: 241.84 E-value: 2.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 341 SLSQAIGTEEgFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWnAR 420
Cdd:pfam00563 3 ALRRALENGE-FVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 421 NIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNW 500
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489193161 501 TYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQP 575
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
332-587 |
1.49e-73 |
|
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: 244.44 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 332 QQRAFTLLTSLSQAIgTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAM 411
Cdd:COG4943 266 LRRRLSPRRRLRRAI-KRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 412 AQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIrDASAVGSVLLRARELGMGIAVD 491
Cdd:COG4943 345 RDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 492 DFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYL 571
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|....*.
gi 489193161 572 IAQPMLPEQLEDWLRR 587
Cdd:COG4943 504 FAKPLPAEEFIAWLAA 519
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
215-587 |
1.50e-68 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 234.19 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 215 GYPFSNDLMLEARDRIRAELP-DFTLYKISPTRFGLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVlplA 293
Cdd:PRK10060 285 GHMFGDQLLQDVSLAILSCLEeDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGI---A 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 294 DDPLDGDQdwLRLVVSAADDA----RDRGVGWARYNPPldQAQQRAFTLL---TSLSQAIgTEEGFHLVYQPKIDLpTGR 366
Cdd:PRK10060 362 LAPEHGDD--SESLIRSADTAmytaKEGGRGQFCVFSP--EMNQRVFEYLwldTNLRKAL-ENDQLVIHYQPKITW-RGE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 367 CTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVR 446
Cdd:PRK10060 436 VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 447 LAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPK 526
Cdd:PRK10060 516 ALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPV 595
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489193161 527 AQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQLEDWLRR 587
Cdd:PRK10060 596 SQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
169-586 |
2.68e-60 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 214.25 E-value: 2.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 169 DEPTGLYNRLRLQEDVSLRLQRDGALTVIAADLLPLallNTIIRTLGYPFSNDLMLEARDRIRAEL-PDFTLYKISPTRF 247
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHF---QDVIDSLGYAWADQALLEVVNRFREKLkPDQYLCRIEGTQF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 248 GLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVlplaDDPLDGDQDWLrlvVSAADDARDR-----GVGWA 322
Cdd:PRK11359 456 VLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGI----SYDVGKNRDYL---LSTAHNAMDYirkngGNGWQ 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 323 RYNPPLDQAQQRAFTLLTSLSQAIgTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPL 402
Cdd:PRK11359 529 FFSPAMNEMVKERLVLGAALKEAI-SNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENI 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 403 SDWVLRHAMAQLAQWNAR--NIPLrLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLR 480
Cdd:PRK11359 608 GRWVIAEACRQLAEWRSQniHIPA-LSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQI 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 481 ARELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQ 560
Cdd:PRK11359 687 LRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLR 766
|
410 420
....*....|....*....|....*.
gi 489193161 561 AWGCHEGQGYLIAQPMLPEQLEDWLR 586
Cdd:PRK11359 767 KIHCRVIQGYFFSRPLPAEEIPGWMS 792
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
222-586 |
1.51e-55 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 198.78 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 222 LMLEARDRIRAELPDFT-LYKISPTRFGLLLPRQQQEEtESVCL--RLLRAFESPVVCRGIPIKANVGLGVLPLaddplD 298
Cdd:PRK13561 284 LLLTLVEKLKSVLSPRMvLAQISGYDFAIIANGVKEPW-HAITLgqQVLTIINERLPIQRIQLRPSCSIGIAMF-----Y 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 299 GDQ---DWLRLVVSAADDARDRGVGW-ARYNPPLDQAQQRAFTLLTSLSQAIgTEEGFHLVYQPKIDLPTGRCTGVEALL 374
Cdd:PRK13561 358 GDLtaeQLYSRAISAAFTARRKGKNQiQFFDPQQMEAAQKRLTEESDILNAL-ENHQFAIWLQPQVEMRSGKLVSAEALL 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 375 RWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDID 454
Cdd:PRK13561 437 RMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 455 LSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYL---RDLPITAIKLDQSFtrdLAGSPKAQSVT 531
Cdd:PRK13561 517 PGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMF---VDGLPEDDSMV 593
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489193161 532 QAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQLED-WLR 586
Cdd:PRK13561 594 AAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEErYLE 649
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
324-576 |
3.08e-46 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 172.82 E-value: 3.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 324 YNPPLDQAQQRAFTLLTSLSQAIGTEEgFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLS 403
Cdd:PRK11829 392 FEPHLIEKTHKRLTQENDLLQAIENHD-FTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLG 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 404 DWVLRHAMAQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARE 483
Cdd:PRK11829 471 NWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 484 LGMGIAVDDFGTGYSNWTYLR---DLPITAIKLDQSFTRDLagsPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQ 560
Cdd:PRK11829 551 LGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLL 627
|
250
....*....|....*.
gi 489193161 561 AWGCHEGQGYLIAQPM 576
Cdd:PRK11829 628 EHGIQCGQGFLFSPPL 643
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
344-585 |
2.75e-35 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 139.36 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 344 QAIGTEEgFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSdwvlRH---AMAQLAQWNAR 420
Cdd:PRK10551 270 TGIKRGQ-FYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLT----QHlfeLIARDAAELQK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 421 NIP--LRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVgSVLLRARELGMGIAVDDFGTGYS 498
Cdd:PRK10551 345 VLPvgAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT-KLFAWLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 499 NWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLP 578
Cdd:PRK10551 424 ALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPL 503
|
....*..
gi 489193161 579 EQLEDWL 585
Cdd:PRK10551 504 EDFVRWL 510
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
113-576 |
2.74e-27 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 117.47 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 113 YAGAPLATAEGLNLGSLCVIdreprgplaeRDV----AMLEHFARLVMariHtlrstnyiDEPTGLYNR----LRLQE-- 182
Cdd:PRK09776 629 YSITPLSTLDGENIGSVLVI----------QDVtesrKMLRQLSYSAS---H--------DALTHLANRasfeKQLRRll 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 183 -DVSLRLQRdGALTVIAADLLPL-------ALLNTIIRTLGYpfsndLMleaRDRIRaelPDFTLYKISPTRFGLLLPRQ 254
Cdd:PRK09776 688 qTVNSTHQR-HALVFIDLDRFKAvndsaghAAGDALLRELAS-----LM---LSMLR---SSDVLARLGGDEFGLLLPDC 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 255 QQEETESVCLRLLRAFES---PVVCRGIPIKANVGLGVLPlADDPLDGDqdwlrlVVSAADDA------RDRGVgWARYN 325
Cdd:PRK09776 756 NVESARFIATRIISAINDyhfPWEGRVYRVGASAGITLID-ANNHQASE------VMSQADIAcyaaknAGRGR-VTVYE 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 326 PPLDQAQ-QRAFTLLTSLSQAIGTEEGFHLVYQ---PKIDLptgRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRP 401
Cdd:PRK09776 828 PQQAAAHsEHRALSLAEQWRMIKENQLMMLAHGvasPRIPE---ARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHA 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 402 LSDWVLRHAMAQLAQWNARNiPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRA 481
Cdd:PRK09776 905 LDRRVIHEFFRQAAKAVASK-GLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKL 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 482 RELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQA 561
Cdd:PRK09776 984 RLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSG 1063
|
490
....*....|....*
gi 489193161 562 WGCHEGQGYLIAQPM 576
Cdd:PRK09776 1064 IGVDLAYGYAIARPQ 1078
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
151-575 |
2.58e-12 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 69.51 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 151 FARLVMARIHTL-RSTNYIDEPTGLYNRL----RL------QEDVSLRlqrdGALTVIAADLLplallNTIIRTLGYPFS 219
Cdd:PRK11059 212 DAREERSRFDTFiRSNAFQDAKTGLGNRLffdnQLatlledQEMVGAH----GVVMLIRLPDF-----DLLQEEWGESQV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 220 NDLMLEARDRIRAEL---PDFTLYKISPTRFGLLLPRQQQEETESVCLRLLRAFESpvvcrgipikanvglgvLPLADdP 296
Cdd:PRK11059 283 EELLFELINLLSTFVmryPGALLARYSRSDFAVLLPHRSLKEADSLASQLLKAVDA-----------------LPPPK-M 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 297 LDGDqDWLRLVVSA-------------ADDA-RD----RGVGWARYnpplDQAQQ--------RAFTLL-TSLSQaigte 349
Cdd:PRK11059 345 LDRD-DFLHIGICAyrsgqsteqvmeeAEMAlRSaqlqGGNGWFVY----DKAQLpekgrgsvRWRTLLeQTLVR----- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 350 EGFHLVYQPKIDLpTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNiplrLAIN 429
Cdd:PRK11059 415 GGPRLYQQPAVTR-DGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEEN----LSIN 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 430 VSASDMEDSSFL----EEAVRLAKTYdidLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYLRD 505
Cdd:PRK11059 490 LSVDSLLSRAFQrwlrDTLLQCPRSQ---RKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKE 566
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 506 LPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQP 575
Cdd:PRK11059 567 LNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
28-159 |
8.31e-11 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 59.80 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 28 DEVFEEILAAATSYFQTPIALISILD--------HQRQWFRASIGLDIRQTPrrdsfcAYAILGKGVFEVADATLDPRFR 99
Cdd:pfam01590 3 EEILQTILEELRELLGADRCALYLPDadgleylpPGARWLKAAGLEIPPGTG------VTVLRTGRPLVVPDAAGDPRFL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 100 DNPYVQGEPRIRFYAGAPLaTAEGLNLGSLCVIDrePRGPLAERDVAMLEHFARLVMARI 159
Cdd:pfam01590 77 DPLLLLRNFGIRSLLAVPI-IDDGELLGVLVLHH--PRPPFTEEELELLEVLADQVAIAL 133
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
28-489 |
3.15e-08 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 56.74 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 28 DEVFEEILAAATSYFQTPIALISILDHQRQ--WFRASIGLD---IRQTPRRDSFCAYAILGKGVFEVADATLDPRFRDNP 102
Cdd:COG2203 209 EELLQRILELAGELLGADRGAILLVDEDGGelELVAAPGLPeeeLGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 103 Y-VQGEPRIRFYAGAPLaTAEGLNLGSLCVIDREPRgPLAERDVAMLEHFARLVMARIHTLRSTNYIDEptglYNRLRLQ 181
Cdd:COG2203 289 ReLLLALGIRSLLCVPL-LVDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEA----ALAALLQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 182 EDVSLRLQRDGALTVIAADLLPLALLNTIIRTLGYPFSNDLMLEARDRIRAELPDFTLYKISPTRFGLLLPRQQQEETES 261
Cdd:COG2203 363 ELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 262 VCLRLLRAFESPVVCRGIPIKANVGLGVLPLADDPLDGDQDWLRLVVSAADDARDRGVGWARYNPPLDQAQQRAFTLLTS 341
Cdd:COG2203 443 RRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 342 LSQAIGTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARN 421
Cdd:COG2203 523 LLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLL 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489193161 422 IPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIA 489
Cdd:COG2203 603 LERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELDLILDS 670
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
460-575 |
4.01e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 52.50 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 460 LEFTESVLIRDAsavgsVLLRAREL---GMGIAVDDFgTGYSNWTYLRDLpITAIKLDqsftrdLAGSPKAQsvTQAVIG 536
Cdd:COG3434 88 LEILEDVEPDEE-----LLEALKELkekGYRIALDDF-VLDPEWDPLLPL-ADIIKID------VLALDLEE--LAELVA 152
|
90 100 110
....*....|....*....|....*....|....*....
gi 489193161 537 LASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQP 575
Cdd:COG3434 153 RLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
27-163 |
2.69e-06 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 47.97 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 27 ADEVFEEILAAATSYFQTPIALISILDHQRQ--WFRASIGLD---IRQT--PRRDSFCAYAILGKGVFEVADATLDPRFR 99
Cdd:COG3605 19 LDEALDRIVRRIAEALGVDVCSIYLLDPDGGrlELRATEGLNpeaVGKVrlPLGEGLVGLVAERGEPLNLADAASHPRFK 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489193161 100 DNPYVqGEPRIRFYAGAPLaTAEGLNLGSLCVIDREPRgPLAERDVAMLEHFARLVMARIHTLR 163
Cdd:COG3605 99 YFPET-GEEGFRSFLGVPI-IRRGRVLGVLVVQSREPR-EFTEEEVEFLVTLAAQLAEAIANAE 159
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
78-314 |
6.12e-06 |
|
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: 48.05 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 78 AYAILGKGVFEVADATLDPRFRDNPYVQGEPRIRFYAGAPLATAEGLNLGSLCVIDREPRGPLAERDVAMLEHFARLVMA 157
Cdd:COG2199 13 LLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 158 RIHTLRSTN-------------YIDEPTGLYNRLRLQEDVSLRLQR----DGALTVIaadllplallntIIR-------- 212
Cdd:COG2199 93 LLLALEDITelrrleerlrrlaTHDPLTGLPNRRAFEERLERELARarreGRPLALL------------LIDldhfkrin 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 213 -TLGYPFSNDLMLEARDRIRAELPDF-TLYKISPTRFGLLLPRQQQEETESVCLRLLRAFES-PVVCRGIPIKANVGLGV 289
Cdd:COG2199 161 dTYGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGV 240
|
250 260
....*....|....*....|....*
gi 489193161 290 LPLADDPLDGDQdwlrlVVSAADDA 314
Cdd:COG2199 241 ALYPEDGDSAEE-----LLRRADLA 260
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
28-163 |
8.49e-06 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 45.84 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 28 DEVFEEILAAATSYFQTPIALISILD---HQRQWFRASIGLDIRQTPRR----DSFCAYAILGKGVFEVADATLDPRFRD 100
Cdd:smart00065 3 EELLQTILEELRQLLGADRVLIYLVDendRGELVLVAADGLTLPTLGIRfpldEGLAGRVAETGRPLNIPDVEADPLFAE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489193161 101 NPYvQGEPRIRFYAGAPLATAEGLnLGSLCVIDREPRGPLAERDVAMLEHFARLVMARIHTLR 163
Cdd:smart00065 83 DLL-GRYQGVRSFLAVPLVADGEL-VGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQ 143
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
167-314 |
1.60e-05 |
|
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: 45.24 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 167 YIDEPTGLYNRLRLQEDVSLRLQR----DGALTVIaadllplallntIIR---------TLGYPFSNDLMLEARDRIRAE 233
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARarrsGRPLALL------------LIDidhfkqindTYGHAAGDEVLKEVAERLRSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 234 LPD-FTLYKISPTRFGLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVLPLADDPLDGDQdwlrlVVSAAD 312
Cdd:cd01949 69 LREsDLVARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEE-----LLRRAD 143
|
..
gi 489193161 313 DA 314
Cdd:cd01949 144 EA 145
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
491-583 |
5.48e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 44.99 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 491 DDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGY 570
Cdd:PRK11596 158 DDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGY 237
|
90
....*....|...
gi 489193161 571 LIAQPMLPEQLED 583
Cdd:PRK11596 238 FLSRPAPFETLET 250
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
166-318 |
8.54e-05 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 43.39 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 166 NYIDEPTGLYNRLRLQEDVSLRLQR------DGALTVIAADLLplallNTIIRTLGYPFSNDLMLEARDRIRAELPDF-T 238
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRaqrqgsPFALLLIDLDNF-----KDINDTYGHAVGDELLQEVAQRLSSCLRPGdL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 239 LYKISPTRFGLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVLPLADDPLDGDqDWLRLVVSAADDARDRG 318
Cdd:smart00267 78 LARLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAE-DLLKRADTALYQAKKAG 156
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
28-155 |
7.33e-04 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 40.14 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193161 28 DEVFEEILAAATSYFQTPIALISILDHQRQ---WFRASIGLDIRQTPR-RDSFCAYAILGKGVFEVADATLDPRFRDNPy 103
Cdd:pfam13185 5 EELLDAVLEAAVELGASAVGFILLVDDDGRlaaWGGAADELSAALDDPpGEGLVGEALRTGRPVIVNDLAADPAKKGLP- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489193161 104 vQGEPRIRFYAGAPLaTAEGLNLGSLCVIDREPrGPLAERDVAMLEHFARLV 155
Cdd:pfam13185 84 -AGHAGLRSFLSVPL-VSGGRVVGVLALGSNRP-GAFDEEDLELLELLAEQA 132
|
|
| |
