|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
135-552 |
2.77e-140 |
|
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: 421.49 E-value: 2.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 135 FDSITGTWNREQFEHRMNYLIKEKIYKN--GAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGD 212
Cdd:COG5001 253 HDPLTGLPNRRLFLDRLEQALARARRSGrrLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGD 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 213 EFAFFYPMCTK-ETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFF 291
Cdd:COG5001 333 EFAVLLPDLDDpEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 292 SQELYENKLKVISMQQKLRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVG 371
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERG--ELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLG 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 372 KWIIKEAVKQCKEWHKI-NPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLK 450
Cdd:COG5001 491 EWVLREACRQLAAWQDAgLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALR 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 451 GIGVYIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSL 530
Cdd:COG5001 571 ALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLREL 650
|
410 420
....*....|....*....|..
gi 544960489 531 GVDIIQGFLFGRPVSASEFYKF 552
Cdd:COG5001 651 GCDYAQGYLFSRPLPAEELEAL 672
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
309-548 |
4.39e-96 |
|
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: 292.14 E-value: 4.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 309 LRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEWHKI 388
Cdd:cd01948 3 LRRALERG--EFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 389 NPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGYSSL 468
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 469 NYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSASE 548
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
136-549 |
8.98e-89 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 287.35 E-value: 8.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKEKIYKNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGDEFA 215
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 216 FFYPMCTKETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFFSQEL 295
Cdd:PRK10060 320 VLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEM 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 296 YENKLKVISMQQKLRECVENNfnDFELFFQPQVNaITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWII 375
Cdd:PRK10060 400 NQRVFEYLWLDTNLRKALEND--QLVIHYQPKIT-WRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVM 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 376 KEAVKQCKEWHKINPDFKISVNVSYIQLKED-FFRDFIvECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGV 454
Cdd:PRK10060 477 LDVVRQVAKWRDKGINLRVAVNVSARQLADQtIFTALK-QALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGA 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 455 YIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDI 534
Cdd:PRK10060 556 QVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE 635
|
410
....*....|....*
gi 544960489 535 IQGFLFGRPVSASEF 549
Cdd:PRK10060 636 RQGFLFAKPMPAVAF 650
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
309-546 |
3.35e-82 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 256.76 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 309 LRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEW-HK 387
Cdd:smart00052 4 LRQALENG--QFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 388 INPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGYSS 467
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544960489 468 LNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSA 546
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
306-543 |
7.06e-73 |
|
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: 232.21 E-value: 7.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 306 QQKLRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEW 385
Cdd:pfam00563 1 ARALRRALENG--EFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 386 hKINPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGY 465
Cdd:pfam00563 79 -QLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544960489 466 SSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRP 543
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
136-291 |
1.55e-24 |
|
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: 100.10 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKE-KIY-KNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIAtevlEYLPKDVR----LYRL 209
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRaRRFqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVA----RILQSSVRgsdvVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 210 DGDEFAFFYPMCTKETIEKIYEKIHMYTNTQhEIE---SNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKN 286
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSK-PIEvagSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 544960489 287 RIKFF 291
Cdd:TIGR00254 160 RVVVA 164
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
62-124 |
2.23e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 45.79 E-value: 2.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544960489 62 WSKIVYPDDVQIWKDDIQELLDGKKgEHNLEYRLINKYEEIVWISCRGKVYVSDDPKTILLVG 124
Cdd:pfam08447 26 WLDLVHPDDRERVREALWEALKGGE-PYSGEYRIRRKDGEYRWVEARARPIRDENGKPVRVIG 87
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
14-131 |
7.38e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 44.63 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 14 EIFFELLSQSTEDYIFFWDINRNKFKISSAIFDEFNLSKEieSDLVNCWSKIVYPDDVQIWKDDIQELLDGKKGEHNLEY 93
Cdd:COG2202 136 EERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPE--ELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELEL 213
|
90 100 110
....*....|....*....|....*....|....*...
gi 544960489 94 RLINKYEEIVWISCRGkVYVSDDPKTILLVGRIKNIGE 131
Cdd:COG2202 214 RLKDGDGRWVWVEASA-VPLRDGGEVIGVLGIVRDITE 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
135-552 |
2.77e-140 |
|
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: 421.49 E-value: 2.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 135 FDSITGTWNREQFEHRMNYLIKEKIYKN--GAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGD 212
Cdd:COG5001 253 HDPLTGLPNRRLFLDRLEQALARARRSGrrLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGD 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 213 EFAFFYPMCTK-ETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFF 291
Cdd:COG5001 333 EFAVLLPDLDDpEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 292 SQELYENKLKVISMQQKLRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVG 371
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERG--ELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLG 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 372 KWIIKEAVKQCKEWHKI-NPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLK 450
Cdd:COG5001 491 EWVLREACRQLAAWQDAgLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALR 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 451 GIGVYIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSL 530
Cdd:COG5001 571 ALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLREL 650
|
410 420
....*....|....*....|..
gi 544960489 531 GVDIIQGFLFGRPVSASEFYKF 552
Cdd:COG5001 651 GCDYAQGYLFSRPLPAEELEAL 672
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
164-552 |
7.47e-107 |
|
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: 331.75 E-value: 7.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 164 AMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGDEFAFFYPMCTKETIEKIYEKIHMYTNTQ-HE 242
Cdd:COG2200 188 LLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEpLL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 243 IESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFFSQElYENKLKVISMQQKLRECVENNfnDFEL 322
Cdd:COG2200 268 LGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAA-EARARRRLALESELREALEEG--ELRL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 323 FFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEWHKINPDFKISVNVSYIQ 402
Cdd:COG2200 345 YYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNLSARS 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 403 LKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGYSSLNYLKELSVNIIKIE 482
Cdd:COG2200 425 LLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKID 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 483 RSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSASEFYKF 552
Cdd:COG2200 505 RSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
309-548 |
4.39e-96 |
|
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: 292.14 E-value: 4.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 309 LRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEWHKI 388
Cdd:cd01948 3 LRRALERG--EFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 389 NPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGYSSL 468
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 469 NYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSASE 548
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
136-549 |
8.98e-89 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 287.35 E-value: 8.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKEKIYKNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGDEFA 215
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 216 FFYPMCTKETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFFSQEL 295
Cdd:PRK10060 320 VLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEM 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 296 YENKLKVISMQQKLRECVENNfnDFELFFQPQVNaITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWII 375
Cdd:PRK10060 400 NQRVFEYLWLDTNLRKALEND--QLVIHYQPKIT-WRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVM 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 376 KEAVKQCKEWHKINPDFKISVNVSYIQLKED-FFRDFIvECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGV 454
Cdd:PRK10060 477 LDVVRQVAKWRDKGINLRVAVNVSARQLADQtIFTALK-QALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGA 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 455 YIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDI 534
Cdd:PRK10060 556 QVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE 635
|
410
....*....|....*
gi 544960489 535 IQGFLFGRPVSASEF 549
Cdd:PRK10060 636 RQGFLFAKPMPAVAF 650
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
309-546 |
3.35e-82 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 256.76 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 309 LRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEW-HK 387
Cdd:smart00052 4 LRQALENG--QFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 388 INPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGYSS 467
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544960489 468 LNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSA 546
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
304-552 |
4.21e-75 |
|
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: 247.52 E-value: 4.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 304 SMQQKLRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCK 383
Cdd:COG4943 271 SPRRRLRRAIKRR--EFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 384 EWHKINPDFKISVNVSyiqlKEDF----FRDFIVECLVEYQLRPEFLILELTENCWIpDINLLNDKFISLKGIGVYIAID 459
Cdd:COG4943 349 DLLAADPDFHISINLS----ASDLlsprFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 460 DFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFL 539
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|...
gi 544960489 540 FGRPVSASEFYKF 552
Cdd:COG4943 504 FAKPLPAEEFIAW 516
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
306-543 |
7.06e-73 |
|
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: 232.21 E-value: 7.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 306 QQKLRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEW 385
Cdd:pfam00563 1 ARALRRALENG--EFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 386 hKINPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGY 465
Cdd:pfam00563 79 -QLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544960489 466 SSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRP 543
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
134-548 |
7.18e-68 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 234.28 E-value: 7.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 134 KFDSITGTWNREQFEHRMNYLIKEKIykNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGDE 213
Cdd:PRK11359 377 QFDPLTGLPNRNNLHNYLDDLVDKAV--SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 214 FAFFYPMCTKETIEKIYEkiHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFFSQ 293
Cdd:PRK11359 455 FVLVSLENDVSNITQIAD--ELRNVVSKPIMIDDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSP 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 294 ELYENKLKVISMQQKLRECVENNfnDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKW 373
Cdd:PRK11359 533 AMNEMVKERLVLGAALKEAISNN--QLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRW 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 374 IIKEAVKQCKEWHKINPDFK-ISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPdinlLNDKFIS---- 448
Cdd:PRK11359 611 VIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMME----HDTEIFKriqi 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 449 LKGIGVYIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVK 528
Cdd:PRK11359 687 LRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLR 766
|
410 420
....*....|....*....|
gi 544960489 529 SLGVDIIQGFLFGRPVSASE 548
Cdd:PRK11359 767 KIHCRVIQGYFFSRPLPAEE 786
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
251-549 |
1.50e-61 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 214.42 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 251 TITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFFSQELYENKLKVISMQQKLRECVENNfnDFELFFQPQVNA 330
Cdd:PRK11829 352 SASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENH--DFTLFLQPQWDM 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 331 ITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEWHKINPDFKISVNVSYIQLKEDFFRD 410
Cdd:PRK11829 430 KRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLP 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 411 FIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFISLKGIGVYIAIDDFGTGYSSLNYL---KELSVNIIKIERSFVK 487
Cdd:PRK11829 510 HLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVK 589
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544960489 488 NITYNSyeyTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSASEF 549
Cdd:PRK11829 590 NLPEDD---AIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEF 648
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
249-549 |
5.16e-59 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 207.26 E-value: 5.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 249 YCTItaGVAMYpEDGDNYLDLFKHADIALDIAKISGKNRIKFFSQELYENKLKVISMQQKLRECVENNfnDFELFFQPQV 328
Cdd:PRK13561 348 SCSI--GIAMF-YGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENH--QFAIWLQPQV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 329 NAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVGKWIIKEAVKQCKEWHKINPDFKISVNVSYIQLKEDFF 408
Cdd:PRK13561 423 EMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNM 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 409 RDFIVECLVEYQLRPEFLILELTENCWIPD----INLLNDkfisLKGIGVYIAIDDFGTGYSSLNYL---KELSVNIIKI 481
Cdd:PRK13561 503 VADMLELLTRYRIQPGTLILEVTESRRIDDphaaVAILRP----LRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKI 578
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544960489 482 ERSFVKNITYNSyeyTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSASEF 549
Cdd:PRK13561 579 DKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIF 643
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
136-549 |
3.34e-43 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 165.62 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKEKI--YKNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYL-PKDVrLYRLDGD 212
Cdd:PRK09776 668 DALTHLANRASFEKQLRRLLQTVNstHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLrSSDV-LARLGGD 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 213 EFAFFYPMCTKETIEKIYEK-IHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKF- 290
Cdd:PRK09776 747 EFGLLLPDCNVESARFIATRiISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVy 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 291 -FSQELYENKLKVISMQQKLRECVENNFndFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIP 369
Cdd:PRK09776 827 ePQQAAAHSEHRALSLAEQWRMIKENQL--MMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHA 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 370 VGKWIIKEAVKQCKEwhKI-NPDFKISVNVSYIQLKEDFFRDFIVECLVEYQLRPEFLILELTENCWIPDINLLNDKFIS 448
Cdd:PRK09776 905 LDRRVIHEFFRQAAK--AVaSKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQK 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 449 LKGIGVYIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVK 528
Cdd:PRK09776 983 LRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLS 1062
|
410 420
....*....|....*....|.
gi 544960489 529 SLGVDIIQGFLFGRPVSASEF 549
Cdd:PRK09776 1063 GIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
135-288 |
6.97e-43 |
|
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: 150.40 E-value: 6.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 135 FDSITGTWNREQFEHRMNYLIKEKIYKNG--AMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGD 212
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544960489 213 EFAFFYPMCTKETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRI 288
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
135-291 |
4.98e-40 |
|
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: 146.66 E-value: 4.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 135 FDSITGTWNREQFEHRMNYLIKEKIYKNG--AMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGD 212
Cdd:COG2199 116 HDPLTGLPNRRAFEERLERELARARREGRplALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 213 EFAFFYPMCTKETIEKIYEKIHMY-TNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFF 291
Cdd:COG2199 196 EFAVLLPGTDLEEAEALAERLREAlEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
135-287 |
1.76e-33 |
|
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: 125.06 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 135 FDSITGTWNREQFEHRMNYLIK--EKIYKNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYL-PKDVrLYRLDG 211
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQraLREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLrRSDL-VARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544960489 212 DEFAFFYPMCTKETIEKIYEKIHMYTNTQ---HEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNR 287
Cdd:pfam00990 82 DEFAILLPETSLEGAQELAERIRRLLAKLkipHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
135-291 |
2.42e-32 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 121.97 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 135 FDSITGTWNREQFEHRMNYLIKEKI-YKNGAMFIM-DVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGD 212
Cdd:smart00267 5 RDPLTGLPNRRYFEEELEQELQRAQrQGSPFALLLiDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544960489 213 EFAFFYPMCTKETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNRIKFF 291
Cdd:smart00267 85 EFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVAVY 163
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
318-552 |
8.24e-32 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 128.96 E-value: 8.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 318 NDFELFFQPQVNAITKEVIGAEVLLRWHSSTYGEVSPVEFIPILEQSNLIIPVG----KWIIKEAVKQCkewHKINPDFK 393
Cdd:PRK10551 275 GQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTqhlfELIARDAAELQ---KVLPVGAK 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 394 ISVNVSYIQLKEDFFRDFIVECLVeyQLRPEF--LILELTENCWIPDiNLLNDKFISLKGIGVYIAIDDFGTGYSSLNYL 471
Cdd:PRK10551 352 LGINISPAHLHSDSFKADVQRLLA--SLPADHfqIVLEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFGTGHSALIYL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 472 KELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPVSASEFYK 551
Cdd:PRK10551 429 ERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVR 508
|
.
gi 544960489 552 F 552
Cdd:PRK10551 509 W 509
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
136-291 |
1.55e-24 |
|
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: 100.10 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKE-KIY-KNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIAtevlEYLPKDVR----LYRL 209
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRaRRFqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVA----RILQSSVRgsdvVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 210 DGDEFAFFYPMCTKETIEKIYEKIHMYTNTQhEIE---SNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKN 286
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSK-PIEvagSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 544960489 287 RIKFF 291
Cdd:TIGR00254 160 RVVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
136-288 |
9.30e-18 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 86.11 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKEKIYKNGAMFIM--DVDNFKNINEKYGHSYGDKVLRAIATEvleyLPKDVR----LYRL 209
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMmiDIDHFKKVNDTYGHDAGDEVLREFAKR----LRNNIRgtdlIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 210 DGDEFAFFYPMCTKETIEKIYEKIHM---YTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKN 286
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERIRRkiaEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRN 450
|
..
gi 544960489 287 RI 288
Cdd:PRK09581 451 RV 452
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
136-546 |
1.25e-15 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 79.91 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLI--KEKIYKNGAMFIMDVDNFKNINEKYGHSYGDKVLRA----IATEVLEYlpKDVRLYRL 209
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLedQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFElinlLSTFVMRY--PGALLARY 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 210 DGDEFAFFYPMCTKETIEKIYEKIHMYTNTQH--EIESNKYYCTItaGVAMYPEdGDNYLDLFKHADIALDIAKISGKNr 287
Cdd:PRK11059 309 SRSDFAVLLPHRSLKEADSLASQLLKAVDALPppKMLDRDDFLHI--GICAYRS-GQSTEQVMEEAEMALRSAQLQGGN- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 288 ikffSQELYENKlkviSMQQKLRECV------ENNFND--FELFFQPQVNAiTKEVIGAEVLLRWHSSTYGEVSPVEFIP 359
Cdd:PRK11059 385 ----GWFVYDKA----QLPEKGRGSVrwrtllEQTLVRggPRLYQQPAVTR-DGKVHHRELFCRIRDGQGELLSAELFMP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 360 ILEQSNLIIPVGKWIIKEAVKQCKEWhkinPDFKISVNVSYIQL-KEDFFR---DFIVEClvEYQLRPEfLILELTENCW 435
Cdd:PRK11059 456 MVQQLGLSEQYDRQVIERVLPLLRYW----PEENLSINLSVDSLlSRAFQRwlrDTLLQC--PRSQRKR-LIFELAEADV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 436 IPDINLLNDKFISLKGIGVYIAIDDFGTGYSSLNYLKELSVNIIKIERSFVKNITYNSYEYTFLEYIIKLAHIINLKVCV 515
Cdd:PRK11059 529 CQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFA 608
|
410 420 430
....*....|....*....|....*....|.
gi 544960489 516 EGIESYEEYDIVKSLGVDIIQGFLFGRPVSA 546
Cdd:PRK11059 609 TGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
136-292 |
5.04e-13 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 69.71 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNR----EQFEHRMNYLIKEKIYKngAMFimDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDG 211
Cdd:PRK09894 132 DVLTGLPGRrvldESFDHQLRNREPQNLYL--ALL--DIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 212 DEFAFFYPMCTKETIEKIYEKIHMYTNTQH-EIESNKYYCTITAGVAMYPEdGDNYLDLFKHADIALDIAKISGKNRIKF 290
Cdd:PRK09894 208 EEFIICLKAATDEEACRAGERIRQLIANHAiTHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTGRNRVMF 286
|
..
gi 544960489 291 FS 292
Cdd:PRK09894 287 ID 288
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
136-288 |
2.36e-12 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 69.27 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKEKiYKNGAMF--IM-DVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGD 212
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRC-QRDQQPFsvIQlDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 213 EFAFFYPMCTKETIEKIYEKIHMYTNTQhEIESNK---YYCTITAGVAMYPEDGDNYLD-LFKHADIALDIAKISGKNRI 288
Cdd:PRK15426 480 EFCVVLPGASLAEAAQVAERIRLRINEK-EILVAKsttIRISASLGVSSAEEDGDYDFEqLQSLADRRLYLAKQAGRNRV 558
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
136-287 |
2.90e-12 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 68.32 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEH--RMNYLIKEKIYKNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGDE 213
Cdd:PRK10245 208 DGMTGVYNRRHWETllRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544960489 214 FAFFYPMCTKETIEKIYEKIHMYTNTQHEIESNKYYCTITAGVAMYPEDGDNYLDLFKHADIALDIAKISGKNR 287
Cdd:PRK10245 288 FAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNR 361
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
136-229 |
8.45e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 67.34 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 136 DSITGTWNREQFEHRMNYLIKEK-IYKNGAMFIMDVDNFKNINEKYGHSYGDKVLRAIATEVLEYLPKDVRLYRLDGDEF 214
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMNNSdARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEF 330
|
90
....*....|....*.
gi 544960489 215 AF-FYPMCTKETIEKI 229
Cdd:PRK09966 331 AMvLYDVQSESEVQQI 346
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
409-544 |
2.49e-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: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 409 RDFIVECLVEyQLRPEFLILELTENCwIPDINLLnDKFISLKGIGVYIAIDDFGTGYSSLNYLKElsVNIIKIErsfvkn 488
Cdd:COG3434 70 EELLLSDLPE-LLPPERVVLEILEDV-EPDEELL-EALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID------ 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 544960489 489 itYNSYEYTFLEYIIKLAHIINLKVCVEGIESYEEYDIVKSLGVDIIQGFLFGRPV 544
Cdd:COG3434 139 --VLALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPE 192
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
62-124 |
2.23e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 45.79 E-value: 2.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544960489 62 WSKIVYPDDVQIWKDDIQELLDGKKgEHNLEYRLINKYEEIVWISCRGKVYVSDDPKTILLVG 124
Cdd:pfam08447 26 WLDLVHPDDRERVREALWEALKGGE-PYSGEYRIRRKDGEYRWVEARARPIRDENGKPVRVIG 87
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
374-545 |
2.89e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 45.76 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 374 IIKEAVKQCKEWHK--INPDFKISVNV---SYIQLKEDF-FRDFIVEClveyqlrPeFLILELTENCWIPdinlLNDKFI 447
Cdd:PRK11596 80 VVKEQLDLLAQWADffVRHGLLASVNIdgpTLIALRQQPaILRLIERL-------P-WLRFELVEHIRLP----KDSPFA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 448 SLKGIGVyIAIDDFGTGYSSLNYLKELSVNIIKIERS-FVknITYNSYEYTFLeyIIKLAHIINL---KVCVEGIESYEE 523
Cdd:PRK11596 148 SMCEFGP-LWLDDFGTGMANFSALSEVRYDYIKVARElFI--MLRQSEEGRNL--FSQLLHLMNRycrGVIVEGVETPEE 222
|
170 180
....*....|....*....|..
gi 544960489 524 YDIVKSLGVDIIQGFLFGRPVS 545
Cdd:PRK11596 223 WRDVQRSPAFAAQGYFLSRPAP 244
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
14-131 |
7.38e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 44.63 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 14 EIFFELLSQSTEDYIFFWDINRNKFKISSAIFDEFNLSKEieSDLVNCWSKIVYPDDVQIWKDDIQELLDGKKGEHNLEY 93
Cdd:COG2202 136 EERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPE--ELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELEL 213
|
90 100 110
....*....|....*....|....*....|....*...
gi 544960489 94 RLINKYEEIVWISCRGkVYVSDDPKTILLVGRIKNIGE 131
Cdd:COG2202 214 RLKDGDGRWVWVEASA-VPLRDGGEVIGVLGIVRDITE 250
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
186-281 |
7.63e-03 |
|
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: 37.58 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960489 186 DKVLRAIATEVLEYLPKDVR----------LYRLDGDEFAFFYPMCTKETIEKIYEKIhmytntQHEIESNKY-YCTITA 254
Cdd:COG3706 88 EDRARALEAGADDYLTKPFDpeellarvdlVARYGGEEFAILLPGTDLEGALAVAERI------REAVAELPSlRVTVSI 161
|
90 100
....*....|....*....|....*..
gi 544960489 255 GVAmypedgdnYLDLFKHADiALDIAK 281
Cdd:COG3706 162 GVA--------GDSLLKRAD-ALYQAR 179
|
|
| |
