|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
1-634 |
0e+00 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 1094.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 1 MRLTTKFSAFVTLLTGLTIFVTLLGCSLSFYNAIQYKFSHRVQAVATAIDTYLVSNDFSTLRPQITELMMSADIVRVDLL 80
Cdd:PRK11059 5 MRLTTKLSAFVTLLVALAMFVTLLGCTLSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLPELLQAANIVEVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 81 HGDKQVYTLARNGSYRPVGTNDLFRELSVPLIKHPGMSLRLVYQDPMGNYFHSLMTTAPLTGAIGFIILMLFLAVRWLQR 160
Cdd:PRK11059 85 QGDKPVYSFQRPASYRPQGSSSLYRELSLPLLKHPGMSLRLKYVDPFGNYFYSLYATASLTLAIGFIVLMLFLGVRWLRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 161 QLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLCEIQNAREQHSRLDTLIRSYAAQDMKTGLNNRLFFDN 240
Cdd:PRK11059 165 QLAGQELLEERARRILNGEREQAVAGSGYEWPRTASRALDHLLSELQDAREERSRFDTFIRSNAFQDAKTGLGNRLFFDN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 241 QLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMRYPGALLARYHRSDFAALLPHRTLKE 320
Cdd:PRK11059 245 QLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALLARYSRSDFAVLLPHRSLKE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 321 AESIASQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDTEQVMEHAESATRNAGLQGGNSWAIYDD-SLPEKGRGNVRW 399
Cdd:PRK11059 325 ADSLASQLLKAVDALPPPKMLDRDDFLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDKaQLPEKGRGSVRW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 400 RTLIEQMLSRGGPRLYQKPAVTREGRVHHRELMCRIFDGNEEVSSAE-YMPMVLQFGLSEEYDRLLISRLIPLLRYWPEE 478
Cdd:PRK11059 405 RTLLEQTLVRGGPRLYQQPAVTRDGKVHHRELFCRIRDGQGELLSAElFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 479 NLAIQVTVESLIRPRFQRWLRDTLMQCEKSQRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWI 558
Cdd:PRK11059 485 NLSINLSVDSLLSRAFQRWLRDTLLQCPRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYI 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447164221 559 KELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLD 634
Cdd:PRK11059 565 KELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
74-634 |
1.53e-62 |
|
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: 217.73 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 74 IVRVDLLHGDKQVYTLARNGSYRPVGTNDLFRELSVPLIKHPGMSLRLVYQDPMGNYFHSLMTTAPLTGAIGFIILMLFL 153
Cdd:COG2200 4 LLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 154 AVRWLQRQLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLCEIQNAREQHSRLDTLIRSYAAQDMKTGLN 233
Cdd:COG2200 84 ALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 234 NRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMRYPGALLARYHRSDFAALL 313
Cdd:COG2200 164 LRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 314 PHRTLKEAESIASQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDTEQVMEHAESATRNAGLQGGNSWAIYDDSLPEKG 393
Cdd:COG2200 244 LLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 394 RGNVRWRTLIEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFDGN-EEVSSAEYMPMVLQFGLSEEYDRLLISRLIPL 471
Cdd:COG2200 324 RRRLALESELREALEEGELRLYYQPIVdLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 472 LRYWPEEN----LAIQVTVESLIRPRFQRWLRDTLmQCEKSQRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQ 547
Cdd:COG2200 404 LARWPERGldlrLSVNLSARSLLDPDFLERLLELL-AEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 548 AGLTLVSTSWIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFF 627
Cdd:COG2200 483 FGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562
|
....*..
gi 447164221 628 ASSQPLD 634
Cdd:COG2200 563 GRPLPLE 569
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
401-635 |
8.03e-59 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 197.44 E-value: 8.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 401 TLIEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFDG-NEEVSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPE- 477
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVsLRTGRLVGVEALIRWQHPeGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 478 ----ENLAIQVTVESLIRPRFQRWLRDTLMqcEKSQR-RRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTL 552
Cdd:smart00052 82 gpppLLISINLSARQLISPDLVPRVLELLE--ETGLPpQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 553 VSTSWIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQP 632
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
...
gi 447164221 633 LDT 635
Cdd:smart00052 240 LDD 242
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
224-381 |
4.78e-41 |
|
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: 146.63 E-value: 4.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 224 AAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMRypGALLAR 303
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRR--SDLVAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 304 YHRSDFAALLPHRTLKEA---ESIASQLIKAVDTLPNNKMLDRDDMIHIGICAW-RSGQDTEQVMEHAESATRNAGLQGG 379
Cdd:pfam00990 79 LGGDEFAILLPETSLEGAqelAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGR 158
|
..
gi 447164221 380 NS 381
Cdd:pfam00990 159 NR 160
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
403-634 |
1.05e-33 |
|
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: 128.82 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 403 IEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFD-GNEEVSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPEEN- 479
Cdd:cd01948 3 LRRALERGEFELYYQPIVdLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 480 ---LAIQVTVESLIRPRFQRWLRDTLMQCEKSQRRrIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTS 556
Cdd:cd01948 83 dlrLSVNLSARQLRDPDFLDRLLELLAETGLPPRR-LVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447164221 557 WIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLD 634
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
223-380 |
1.69e-06 |
|
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: 48.49 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 223 YAAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTfMMRypGA-LL 301
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS-SVR--GSdVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 302 ARYHRSDFAALLPHRTLKEAESIASQLIKAVDTLPnnKMLDRDDMIH----IGICAWRSGQDT-EQVMEHAESATRNAGL 376
Cdd:TIGR00254 78 GRYGGEEFVVILPGTPLEDALSKAERLRDAINSKP--IEVAGSETLTvtvsIGVACYPGHGLTlEELLKRADEALYQAKK 155
|
....
gi 447164221 377 QGGN 380
Cdd:TIGR00254 156 AGRN 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
1-634 |
0e+00 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 1094.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 1 MRLTTKFSAFVTLLTGLTIFVTLLGCSLSFYNAIQYKFSHRVQAVATAIDTYLVSNDFSTLRPQITELMMSADIVRVDLL 80
Cdd:PRK11059 5 MRLTTKLSAFVTLLVALAMFVTLLGCTLSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLPELLQAANIVEVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 81 HGDKQVYTLARNGSYRPVGTNDLFRELSVPLIKHPGMSLRLVYQDPMGNYFHSLMTTAPLTGAIGFIILMLFLAVRWLQR 160
Cdd:PRK11059 85 QGDKPVYSFQRPASYRPQGSSSLYRELSLPLLKHPGMSLRLKYVDPFGNYFYSLYATASLTLAIGFIVLMLFLGVRWLRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 161 QLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLCEIQNAREQHSRLDTLIRSYAAQDMKTGLNNRLFFDN 240
Cdd:PRK11059 165 QLAGQELLEERARRILNGEREQAVAGSGYEWPRTASRALDHLLSELQDAREERSRFDTFIRSNAFQDAKTGLGNRLFFDN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 241 QLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMRYPGALLARYHRSDFAALLPHRTLKE 320
Cdd:PRK11059 245 QLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALLARYSRSDFAVLLPHRSLKE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 321 AESIASQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDTEQVMEHAESATRNAGLQGGNSWAIYDD-SLPEKGRGNVRW 399
Cdd:PRK11059 325 ADSLASQLLKAVDALPPPKMLDRDDFLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDKaQLPEKGRGSVRW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 400 RTLIEQMLSRGGPRLYQKPAVTREGRVHHRELMCRIFDGNEEVSSAE-YMPMVLQFGLSEEYDRLLISRLIPLLRYWPEE 478
Cdd:PRK11059 405 RTLLEQTLVRGGPRLYQQPAVTRDGKVHHRELFCRIRDGQGELLSAElFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 479 NLAIQVTVESLIRPRFQRWLRDTLMQCEKSQRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWI 558
Cdd:PRK11059 485 NLSINLSVDSLLSRAFQRWLRDTLLQCPRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYI 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447164221 559 KELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLD 634
Cdd:PRK11059 565 KELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
74-634 |
1.53e-62 |
|
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: 217.73 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 74 IVRVDLLHGDKQVYTLARNGSYRPVGTNDLFRELSVPLIKHPGMSLRLVYQDPMGNYFHSLMTTAPLTGAIGFIILMLFL 153
Cdd:COG2200 4 LLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 154 AVRWLQRQLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLCEIQNAREQHSRLDTLIRSYAAQDMKTGLN 233
Cdd:COG2200 84 ALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 234 NRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMRYPGALLARYHRSDFAALL 313
Cdd:COG2200 164 LRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 314 PHRTLKEAESIASQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDTEQVMEHAESATRNAGLQGGNSWAIYDDSLPEKG 393
Cdd:COG2200 244 LLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 394 RGNVRWRTLIEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFDGN-EEVSSAEYMPMVLQFGLSEEYDRLLISRLIPL 471
Cdd:COG2200 324 RRRLALESELREALEEGELRLYYQPIVdLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 472 LRYWPEEN----LAIQVTVESLIRPRFQRWLRDTLmQCEKSQRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQ 547
Cdd:COG2200 404 LARWPERGldlrLSVNLSARSLLDPDFLERLLELL-AEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 548 AGLTLVSTSWIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFF 627
Cdd:COG2200 483 FGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562
|
....*..
gi 447164221 628 ASSQPLD 634
Cdd:COG2200 563 GRPLPLE 569
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
401-635 |
8.03e-59 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 197.44 E-value: 8.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 401 TLIEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFDG-NEEVSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPE- 477
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVsLRTGRLVGVEALIRWQHPeGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 478 ----ENLAIQVTVESLIRPRFQRWLRDTLMqcEKSQR-RRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTL 552
Cdd:smart00052 82 gpppLLISINLSARQLISPDLVPRVLELLE--ETGLPpQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 553 VSTSWIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQP 632
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
...
gi 447164221 633 LDT 635
Cdd:smart00052 240 LDD 242
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
224-381 |
4.78e-41 |
|
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: 146.63 E-value: 4.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 224 AAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMRypGALLAR 303
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRR--SDLVAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 304 YHRSDFAALLPHRTLKEA---ESIASQLIKAVDTLPNNKMLDRDDMIHIGICAW-RSGQDTEQVMEHAESATRNAGLQGG 379
Cdd:pfam00990 79 LGGDEFAILLPETSLEGAqelAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGR 158
|
..
gi 447164221 380 NS 381
Cdd:pfam00990 159 NR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
223-385 |
2.00e-40 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 145.08 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 223 YAAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMryPGALLA 302
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLR--PGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 303 RYHRSDFAALLPHRTLKEAESIASQLIKAVDTLPNNKMLDRDDMIHIGICAW-RSGQDTEQVMEHAESATRNAGLQGGNS 381
Cdd:smart00267 80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 447164221 382 WAIY 385
Cdd:smart00267 160 VAVY 163
|
|
| GAPES4 |
pfam17157 |
Gammaproteobacterial periplasmic sensor domain; GAPES4 (GAmmaproteobacterial PEriplasmic ... |
33-130 |
6.49e-40 |
|
Gammaproteobacterial periplasmic sensor domain; GAPES4 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in various GGDEF- and EAL-containing proteins. In Escherichia coli, GAPES4 forms the N-terminal domain of the regulatory protein CsrD (YhdA), which contains enzymatically inactive GGDEF and EAL domains and controls CsrD) that controls the degradation of two non-coding RNAs, CsrB and CsrC. In Vibrio cholerae, GAPES4-containing protein MshH (Q9KUW1_VIBCH) inhibits biofilm formation, apparently acting through the glucose-specific enzyme IIA (Q9KTD8, pfam00358).
Pssm-ID: 435754 Cd Length: 98 Bit Score: 141.27 E-value: 6.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 33 AIQYKFSHRVQAVATAIDTYLVSNDFSTLRPQITELMMSADIVRVDLLHGDKQVYTLARNGSYRPVGTNDLFRELSVPLI 112
Cdd:pfam17157 1 LGQEKLEHRLQAVATSIDQALLTESPQELQRWLPELMQASGIVELELLSNDSTLYSFALPESYRPWGSASLYREVTLPLL 80
|
90
....*....|....*...
gi 447164221 113 KHPGMSLRLVYQDPMGNY 130
Cdd:pfam17157 81 HHPGMSLRFKYVDPLGNY 98
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
403-634 |
1.05e-33 |
|
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: 128.82 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 403 IEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFD-GNEEVSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPEEN- 479
Cdd:cd01948 3 LRRALERGEFELYYQPIVdLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 480 ---LAIQVTVESLIRPRFQRWLRDTLMQCEKSQRRrIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTS 556
Cdd:cd01948 83 dlrLSVNLSARQLRDPDFLDRLLELLAETGLPPRR-LVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447164221 557 WIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLD 634
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
403-628 |
1.05e-33 |
|
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: 128.97 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 403 IEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRIFDGNEE-VSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYW---PE 477
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVdLRTGRVVGYEALLRWQHPDGGlISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlgPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 478 ENLAIQVTVESLIRPRFQRWLRDTLMQcEKSQRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSW 557
Cdd:pfam00563 84 IKLSINLSPASLADPGFLELLRALLKQ-AGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447164221 558 IKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFA 628
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFS 233
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
127-634 |
1.37e-25 |
|
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: 112.18 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 127 MGNYFHSLMTTAPLTGAIGFIILMLFLAVRWLQRQLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLCEI 206
Cdd:COG5001 158 ARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 207 QNAREQHSRLDTLirsyAAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHS-------QVE 279
Cdd:COG5001 238 TERKRAEERLRHL----AYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAagdellrEVA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 280 EQffsLTNLLStfmmryPGALLARYHRSDFAALLPH-RTLKEAESIASQLIKAVDTlPnnkMLDRDDMIH----IGICAW 354
Cdd:COG5001 314 RR---LRACLR------EGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE-P---FELDGHELYvsasIGIALY 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 355 -RSGQDTEQVMEHAESATRNAGLQGGNSWAIYDDSLPEKGRGNVRWRTLIEQMLSRGGPRL-YQkPAV-TREGRV----- 426
Cdd:COG5001 381 pDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELhYQ-PQVdLATGRIvgaea 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 427 ----HHRELmcrifdgnEEVSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPEENL-----AIQVTVESLIRPRFQRW 497
Cdd:COG5001 460 llrwQHPER--------GLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLpdlrvAVNLSARQLRDPDLVDR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 498 LRDTLmqcEKSQ--RRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWIKELNVELLKLHPGLVRN 575
Cdd:COG5001 532 VRRAL---AETGlpPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRD 608
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 447164221 576 IEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFasSQPLD 634
Cdd:COG5001 609 LAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLF--SRPLP 665
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
119-385 |
6.51e-23 |
|
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: 98.90 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 119 LRLVYQDPMGNYFHSLMTTAPLTGAIGFIILMLFLAVRWLQRQLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSA 198
Cdd:COG2199 10 ALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 199 LDTLLCEIQNAREQHSRLDTLiRSYAAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQV 278
Cdd:COG2199 90 LLLLLLALEDITELRRLEERL-RRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 279 EEQFFSLTNLLSTFmMRyPGALLARYHRSDFAALLPHRTLKEAESIASQLIKAVDTLPnnkmLDRDDM-----IHIGICA 353
Cdd:COG2199 169 DEVLKEVARRLRAS-LR-ESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLP----FELEGKelrvtVSIGVAL 242
|
250 260 270
....*....|....*....|....*....|...
gi 447164221 354 WR-SGQDTEQVMEHAESATRNAGLQGGNSWAIY 385
Cdd:COG2199 243 YPeDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
206-635 |
2.37e-21 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 99.36 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 206 IQNAREQHSRLDTLIRSyAAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSL 285
Cdd:PRK09776 648 IQDVTESRKMLRQLSYS-ASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLREL 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 286 TNLLSTfMMRyPGALLARYHRSDFAALLPHRTLKEAESIASQLIKAVdtlpNNKMLDRDDMIH-----IGICAW-RSGQD 359
Cdd:PRK09776 727 ASLMLS-MLR-SSDVLARLGGDEFGLLLPDCNVESARFIATRIISAI----NDYHFPWEGRVYrvgasAGITLIdANNHQ 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 360 TEQVMEHAESATRNAGLQGGNSWAIY--DDSLPEKGRGNV----RWRTLIEQMLSRggprLYQKPAVTR-EGRVHHRELM 432
Cdd:PRK09776 801 ASEVMSQADIACYAAKNAGRGRVTVYepQQAAAHSEHRALslaeQWRMIKENQLMM----LAHGVASPRiPEARNHWLIS 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 433 CRIFDGNEE-VSSAEYMPMVLQFGLSEEYDRLLISRLiplLRYWPEE------NLAIQVTVESLIRPRFQRWLRDTLmqc 505
Cdd:PRK09776 877 LRLWDPEGEiIDEGAFRPAAEDPALMHALDRRVIHEF---FRQAAKAvaskglSIALPLSVAGLSSPTLLPFLLEQL--- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 506 EKS--QRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWIKELNVELLKLHPGLVRNIEKRTENQ 583
Cdd:PRK09776 951 ENSplPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDE 1030
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 447164221 584 LLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLDT 635
Cdd:PRK09776 1031 MLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDL 1082
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
227-383 |
2.95e-21 |
|
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: 90.69 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 227 DMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTFMMryPGALLARYHR 306
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLR--ESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447164221 307 SDFAALLPHRTLKEAESIASQLIKAVDTLPNNKMLDRDDMIHIGICAWRS-GQDTEQVMEHAESATRNAGLQGGNSWA 383
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
207-632 |
3.73e-15 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 78.83 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 207 QNAREQHSRLDTLIRSY---------AAQDM--------KTGLNNRLFFdnqlATLLEDQEKVGT---HGIVMMIRLPDF 266
Cdd:PRK11829 198 LPAHHQDDELGVLVRNYnrnqqlladAYADMgrishrfpVTELPNRSLF----ISLLEKEIASSTrtdHFHLLVIGIETL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 267 NMLSDTWGHSQVEEqffsltnLLSTFMMRY-----PGALLARYHRSDFAALL-----PHRTLKEAESIASQLIKAVdTLP 336
Cdd:PRK11829 274 QEVSGAMSEAQHQQ-------LLLTIVQRIeqcidDSDLLAQLSKTEFAVLArgtrrSFPAMQLARRIMSQVTQPL-FFD 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 337 NnkmLDRDDMIHIGICAWRSGQDT-EQVMEHAESATRNAGLQGGNSWAIYDDSLPEKGRGNVRWRTLIEQMLSRGGPRLY 415
Cdd:PRK11829 346 E---ITLRPSASIGITRYQAQQDTaESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLF 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 416 QKPAV-TREGRVHHRELMCRIF--DGNEEVSSaEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPEENLAIQVTVE----S 488
Cdd:PRK11829 423 LQPQWdMKRQQVIGAEALLRWCqpDGSYVLPS-GFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNisglQ 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 489 LIRPRFQRWLRdTLMQCEKSQRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWI---KELNVEL 565
Cdd:PRK11829 502 VQNKQFLPHLK-TLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHM 580
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447164221 566 LKLHPGLVRNIEKRTENQLLVQSLVEAcsgTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQP 632
Cdd:PRK11829 581 IKLDKSFVKNLPEDDAIARIISCVSDV---LKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
203-636 |
3.48e-13 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 72.88 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 203 LCEIQNAREQ-HSRLDTLIRSyaaqDMKTGLNNRLFFDNQLATLLEDQEKVgthgIVMMIRLPDFNMLSDTWGHSQVEEQ 281
Cdd:PRK11359 358 LAALALEQEKsRQHIEQLIQF----DPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 282 FFSLTNLLSTFMMryPGALLARYHRSDFAALLPHRTLKEAESIASQLIKAVdtlpnNKMLDRDDM-----IHIGIcAWRS 356
Cdd:PRK11359 430 LLEVVNRFREKLK--PDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVV-----SKPIMIDDKpfpltLSIGI-SYDV 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 357 GQDTEQVMEHAESATRNAGLQGGNSWAIYDDSLPEKGRGNVRWRTLIEQMLSRGGPRLYQKPAVTRE-GRVHHRELMCRI 435
Cdd:PRK11359 502 GKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAEtGELYGIEALARW 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 436 FD---GNeeVSSAEYMPMVLQFGLSEEYDRLLISRLIPLLRYWPEENLAIQVTVESLIRPRFQR-WLRDT---LMQCEKS 508
Cdd:PRK11359 582 HDplhGH--VPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSnQLPNQvsdAMQAWGI 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 509 QRRRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWIKELNVELLKLHPGLVrnieKRTENQLLVQS 588
Cdd:PRK11359 660 DGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFV----DRCLTEKRILA 735
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 447164221 589 LVEACSGT----STQVYATGVRSRSEWQTLIQRGVTGGQGDFFasSQPLDTN 636
Cdd:PRK11359 736 LLEAITSIgqslNLTVVAEGVETKEQFEMLRKIHCRVIQGYFF--SRPLPAE 785
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
224-380 |
4.71e-09 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 59.14 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 224 AAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEqffsltnLLSTFMMRYPGA---- 299
Cdd:PRK09581 292 AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDE-------VLREFAKRLRNNirgt 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 300 -LLARYHRSDFAALLPHRTLKEAESIASQLIKAVDTLP-----NNKMLDRddMIHIGICAWRSGQDT-EQVMEHAESATR 372
Cdd:PRK09581 365 dLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPfiisdGKERLNV--TVSIGVAELRPSGDTiEALIKRADKALY 442
|
....*...
gi 447164221 373 NAGLQGGN 380
Cdd:PRK09581 443 EAKNTGRN 450
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
297-644 |
9.81e-08 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 55.10 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 297 PGALLARYHRSDFAaLLPHRtLKE---AESIASQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDTEQVMEHAESATRN 373
Cdd:PRK13561 298 PRMVLAQISGYDFA-IIANG-VKEpwhAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 374 AGLQGGNSWAIYDDSLPEKGRGNVRWRTLIEQMLSRGGPRLYQKPAV-TREGRVHHRELMCRI--FDGNEE-----VSSA 445
Cdd:PRK13561 376 ARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVeMRSGKLVSAEALLRMqqPDGSWDlpeglIDRI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 446 EYMPMVLQFG--LSEEYDRLLISrlipllryWPEEN----LAIQVTVESLIRPRFQRWLRDtLMQCEKSQRRRIIIELAE 519
Cdd:PRK13561 456 ESCGLMVTVGhwVLEESCRLLAA--------WQERGimlpLSVNLSALQLMHPNMVADMLE-LLTRYRIQPGTLILEVTE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 520 A----DVGQHISRLQPvirLVNAlGVRVAVNQAGLTLVSTSWI---KELNVELLKLHPGLVRNIekrTENQLLVQSLVEA 592
Cdd:PRK13561 527 SrridDPHAAVAILRP---LRNA-GVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGL---PEDDSMVAAIIML 599
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 447164221 593 CSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLDtnvkKYSQRY 644
Cdd:PRK13561 600 AQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE----IFEERY 647
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
223-380 |
1.69e-06 |
|
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: 48.49 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 223 YAAQDMKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFSLTNLLSTfMMRypGA-LL 301
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS-SVR--GSdVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447164221 302 ARYHRSDFAALLPHRTLKEAESIASQLIKAVDTLPnnKMLDRDDMIH----IGICAWRSGQDT-EQVMEHAESATRNAGL 376
Cdd:TIGR00254 78 GRYGGEEFVVILPGTPLEDALSKAERLRDAINSKP--IEVAGSETLTvtvsIGVACYPGHGLTlEELLKRADEALYQAKK 155
|
....
gi 447164221 377 QGGN 380
Cdd:TIGR00254 156 AGRN 159
|
|
| |
