|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
1-662 |
0e+00 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 1445.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 1 MDDLEQNLLFRYMGTHSPWWRLTADSNALHLSTSENADVTQVIALNDEQAALIRQLTVITSSISMTLSLYGEDVPVHLVG 80
Cdd:PRK10060 2 KDVRESQTLYNFLGTHSPYWRLTEDSNALELSATEETETNVAVALSPEQAARIREMTVITSSLMLTLTLDGEPLSVHLVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 81 RKITRNEWAGTASAWHDTPSVARDLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFM 160
Cdd:PRK10060 82 RKINKREWAGTASAWHDTPSVARDLSHGLSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 161 TRSEAAASRRNIAGFFRNGSSYEVERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERLRVLANTDT 240
Cdd:PRK10060 162 SRREAAASRRNIRGFFRSGNAYEVERWIKTRKGQRLFLFRNKFVHSGSGKNEIFLICSGTDITEERRAQERLRILANTDS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 241 ITGLPNRNAIHELISDAIATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLGGDEFIVM 320
Cdd:PRK10060 242 ITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 321 ATDTSQGSLEAMASRILSRLRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGKFCVFSPEMNQ 400
Cdd:PRK10060 322 ASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 401 RVFEYLWLDTNLRKALDNDQLLIHYQPKMTWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVR 480
Cdd:PRK10060 402 RVFEYLWLDTNLRKALENDQLVIHYQPKITWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 481 QVAKWRDKGINLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQIHLDD 560
Cdd:PRK10060 482 QVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 561 FGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLF 640
Cdd:PRK10060 562 FGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLF 641
|
650 660
....*....|....*....|..
gi 1279591189 641 AKPMPAAVFERWLKRYQSRKMR 662
Cdd:PRK10060 642 AKPMPAVAFERWYKRYLKRKLI 663
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-658 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 576.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 1 MDDLEQNLLFRYMGTHSPWWRLTADSNALHLSTSENADVTQVIALNDEQAALIRQLTVITSSISMTLSLYGEDVPVHLVG 80
Cdd:COG5001 13 ALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 81 RKITRNEWAGTASAWHDTPSVARDLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFM 160
Cdd:COG5001 93 LLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 161 TRSEAAASRRNIAGFFRNGSSYEVERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLIC---SGTDITEERRAQERLRVLAN 237
Cdd:COG5001 173 LLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAvlaIARLITERKRAEERLRHLAY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 238 TDTITGLPNRNAIHELISDAIAT--RGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLGGD 315
Cdd:COG5001 253 HDPLTGLPNRRLFLDRLEQALARarRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 316 EFIVMATD-TSQGSLEAMASRILSRLRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGKFCVF 394
Cdd:COG5001 333 EFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 395 SPEMNQRVFEYLWLDTNLRKALDNDQLLIHYQPKMTWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRW 473
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERGELELHYQPQVDLAtGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEW 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 474 VMLDVVRQVAKWRDKGI-NLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQL 552
Cdd:COG5001 493 VLREACRQLAAWQDAGLpDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRAL 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 553 GAQIHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGV 632
Cdd:COG5001 573 GVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGC 652
|
650 660
....*....|....*....|....*.
gi 1279591189 633 NERQGFLFAKPMPAAVFERWLKRYQS 658
Cdd:COG5001 653 DYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
102-654 |
3.57e-112 |
|
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: 349.08 E-value: 3.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 102 ARDLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFMTRSEAAASRRNIAGFFRNGSS 181
Cdd:COG2200 22 EALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 182 YEVERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERLRVLANTDTITGLPNRNAIHELISDAIATR 261
Cdd:COG2200 102 LLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 262 GDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLGGDE--FIVMATDTSQGSLEAMASRILSR 339
Cdd:COG2200 182 LALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGgfLLLLLLLAAAAAAAAALRLLLLL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 340 LRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGKFCVFSPEMNQRVFEYLWLdTNLRKALDND 419
Cdd:COG2200 262 LLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALE-SELREALEEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 420 QLLIHYQPKMTWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNV 498
Cdd:COG2200 341 ELRLYYQPIVDLRtGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 499 SARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQIHLDDFGTGYSSLSQLARFPIDA 578
Cdd:COG2200 421 SARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDY 500
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279591189 579 IKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPAAVFERWLK 654
Cdd:COG2200 501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
410-647 |
1.13e-100 |
|
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: 307.16 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 410 TNLRKALDNDQLLIHYQPKM-TWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDK 488
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVdLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 489 GINLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQIHLDDFGTGYSSL 568
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279591189 569 SQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPAA 647
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
409-647 |
5.87e-100 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 305.68 E-value: 5.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 409 DTNLRKALDNDQLLIHYQPKMTWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRD 487
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRtGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 488 KGI-NLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQIHLDDFGTGYS 566
Cdd:smart00052 81 QGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 567 SLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPA 646
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
.
gi 1279591189 647 A 647
Cdd:smart00052 241 D 241
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
224-657 |
5.04e-93 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 305.16 E-value: 5.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 224 EERRAQERLRVLANTDTITGLPNRNAIHELISDAIATrgDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCL 303
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDK--AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 304 DEGQVLARLGGDEFIVMATDTSQGSLEAMASRILSRLRQPFRIGLIEIYTGCSLGIALapQHGNDRESVIRNADTAMYTA 383
Cdd:PRK11359 442 KPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 384 KENGRGKFCVFSPEMNQRVFEYLWLDTNLRKALDNDQLLIHYQPKM-TWRGEVRSLEALVRWQSPERGLIPPLEFISYAE 462
Cdd:PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIfAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 463 ESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSARQLADqtifSDLKQALKDLNFEYC----PIDVELTESCLIE 537
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQNIHIpALSVNLSALHFRS----NQLPNQVSDAMQAWGidghQLTVEITESMMME 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 538 NEELALSVIQQFSQLGAQIHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEG 617
Cdd:PRK11359 676 HDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEG 755
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1279591189 618 VESAKEDAFLTKNGVNERQGFLFAKPMPAAVFERWLKRYQ 657
Cdd:PRK11359 756 VETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVL 795
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
227-654 |
1.99e-80 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 267.74 E-value: 1.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 227 RAQERLRVLANTDTITGLPNRNAIHELISDAIATRGDTQVGVVYLDldnfkKVNDAYGHMFGDQ---LLQAVALAILSCL 303
Cdd:PRK13561 222 RQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQTTALMIITCE-----TLRDTAGVLKEAQreiLLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 304 DEGQVLARLGGDEFIVMAtDTSQGSLEAM--ASRILSRLRQPFRIGLIEIYTGCSLGIALapQHGN-DRESVIRNADTAM 380
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIA-NGVKEPWHAItlGQQVLTIINERLPIQRIQLRPSCSIGIAM--FYGDlTAEQLYSRAISAA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 381 YTAKENGRGKFCVFSPEMNQRVFEYLWLDTNLRKALDNDQLLIHYQPKMTWR-GEVRSLEALVRWQSPERGLIPPLEFIS 459
Cdd:PRK13561 374 FTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRsGKLVSAEALLRMQQPDGSWDLPEGLID 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 460 YAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFSDLKQALKdlNFEYCP--IDVELTESCLIE 537
Cdd:PRK13561 454 RIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLT--RYRIQPgtLILEVTESRRID 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 538 NEELALSVIQQFSQLGAQIHLDDFGTGYSSLSQLARF---PIDAIKLDQSFVRDIHKQSisqSLVRAIVAVAQALNLQVI 614
Cdd:PRK13561 532 DPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVI 608
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1279591189 615 AEGVESAKEDAFLTKNGVNERQGFLFAKPMPAAVFE-RWLK 654
Cdd:PRK13561 609 AEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEeRYLE 649
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
412-643 |
8.95e-70 |
|
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: 226.82 E-value: 8.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 412 LRKALDNDQLLIHYQPKM-TWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWrDKGI 490
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVdLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-QLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 491 NLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQIHLDDFGTGYSSLSQ 570
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279591189 571 LARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKP 643
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
412-659 |
1.08e-69 |
|
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: 235.97 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 412 LRKALDNDQLLIHYQPKMTWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW--RDK 488
Cdd:COG4943 276 LRRAIKRREFYVHYQPIVDLKtGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLlaADP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 489 GinLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALsVIQQFSQLGAQIHLDDFGTGYSSL 568
Cdd:COG4943 356 D--FHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKARA-VIAALREAGHRIAIDDFGTGYSSL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 569 SQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPAAV 648
Cdd:COG4943 433 SYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEE 512
|
250
....*....|.
gi 1279591189 649 FERWLKRYQSR 659
Cdd:COG4943 513 FIAWLAAQRAP 523
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
241-650 |
3.54e-69 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 237.92 E-value: 3.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 241 ITGLPNRNAIHELISDAIATRGDTQ-VGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLGGDEFIV 319
Cdd:PRK11829 237 VTELPNRSLFISLLEKEIASSTRTDhFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 320 MATDTSQGSlEAM--ASRILSRLRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGKFCVFSPE 397
Cdd:PRK11829 317 LARGTRRSF-PAMqlARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPH 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 398 MNQRVFEYLWLDTNLRKALDNDQLLIHYQPKMTWRGE-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVML 476
Cdd:PRK11829 396 LIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQqVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 477 DVVRQVAKWRDKGINLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQI 556
Cdd:PRK11829 476 EACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 557 HLDDFGTGYSSLS---QLARFPIDAIKLDQSFVRDIhkqSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVN 633
Cdd:PRK11829 556 ALDDFGIGYSSLRylnHLKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQ 632
|
410
....*....|....*..
gi 1279591189 634 ERQGFLFAKPMPAAVFE 650
Cdd:PRK11829 633 CGQGFLFSPPLPRAEFE 649
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
221-649 |
1.53e-62 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 225.32 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 221 DITEERRAQERLRVLANTDTITGLPNR----NAIHELISDAIATRgdTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVA 296
Cdd:PRK09776 650 DVTESRKMLRQLSYSASHDALTHLANRasfeKQLRRLLQTVNSTH--QRHALVFIDLDRFKAVNDSAGHAAGDALLRELA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 297 LAILSCLDEGQVLARLGGDEFIVMATDTSQGSLEAMASRILSRLRQ---PFRIGLIEIytGCSLGIALAPQHGNDRESVI 373
Cdd:PRK09776 728 SLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDyhfPWEGRVYRV--GASAGITLIDANNHQASEVM 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 374 RNADTAMYTAKENGRGKFCVFSPEMNQ--RVFEYLWLDTNLRKALDNDQLLIHYQ---PKMTWRGEVrsLEALVRWQSPE 448
Cdd:PRK09776 806 SQADIACYAAKNAGRGRVTVYEPQQAAahSEHRALSLAEQWRMIKENQLMMLAHGvasPRIPEARNH--WLISLRLWDPE 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 449 RGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAK-WRDKGinLRVAVNVSARQLADQTIFSDLKQALKDLNFEYCPID 527
Cdd:PRK09776 884 GEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKaVASKG--LSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLH 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 528 VELTESCLIENEELALSVIQQFSQLGAQIHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQ 607
Cdd:PRK09776 962 LEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQ 1041
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1279591189 608 ALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPAAVF 649
Cdd:PRK09776 1042 RLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
237-392 |
3.05e-58 |
|
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: 193.16 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 237 NTDTITGLPNRNAIHELISDAI--ATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLGG 314
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279591189 315 DEFIVMATDTSQGSLEAMASRILSRLRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGKFC 392
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
221-394 |
2.78e-56 |
|
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: 192.50 E-value: 2.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 221 DITEERRAQERLRVLANTDTITGLPNRNAIHELISDAI--ATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALA 298
Cdd:COG2199 99 DITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELarARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 299 ILSCLDEGQVLARLGGDEFIVMATDTSQGSLEAMASRILSRLRQ-PFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNAD 377
Cdd:COG2199 179 LRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRAD 258
|
170
....*....|....*..
gi 1279591189 378 TAMYTAKENGRGKFCVF 394
Cdd:COG2199 259 LALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
235-394 |
7.05e-56 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 187.07 E-value: 7.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 235 LANTDTITGLPNRNAIHELISDAI--ATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARL 312
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELqrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 313 GGDEFIVMATDTSQGSLEAMASRILSRLRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGKFC 392
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 1279591189 393 VF 394
Cdd:smart00267 162 VY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
236-390 |
6.44e-52 |
|
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: 176.29 E-value: 6.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 236 ANTDTITGLPNRNAIHELISDAI--ATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLG 313
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 314 GDEFIVMATDTSQGS---LEAMASRILSRLRQPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRNADTAMYTAKENGRGK 390
Cdd:pfam00990 81 GDEFAILLPETSLEGaqeLAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
415-654 |
8.45e-44 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 164.78 E-value: 8.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 415 ALDNDQLLIHYQPKM-TWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRD---KGI 490
Cdd:PRK10551 271 GIKRGQFYVEYQPVVdTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKvlpVGA 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 491 NLrvAVNVSARQLADQTIFSDLKQALKDLNFEYCPIDVELTESCLIENEElALSVIQQFSQLGAQIHLDDFGTGYSSLSQ 570
Cdd:PRK10551 351 KL--GINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEE-ATKLFAWLHSQGIEIAIDDFGTGHSALIY 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 571 LARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPAAVFE 650
Cdd:PRK10551 428 LERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFV 507
|
....
gi 1279591189 651 RWLK 654
Cdd:PRK10551 508 RWLK 511
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
235-394 |
1.27e-32 |
|
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: 123.60 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 235 LANTDTITGLPNRNAIHELISD--AIATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARL 312
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSelKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 313 GGDEFIVMATDTSQGSleamASRILSRLRQPFRIGLIEIYTG------CSLGIALAPQHGNDRESVIRNADTAMYTAKEN 386
Cdd:TIGR00254 81 GGEEFVVILPGTPLED----ALSKAERLRDAINSKPIEVAGSetltvtVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
....*...
gi 1279591189 387 GRGKFCVF 394
Cdd:TIGR00254 157 GRNRVVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
226-390 |
1.38e-26 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 113.46 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 226 RRAQERLRV-------LANTDTITGLPNR----NAIHELISDAIAtRGDTqVGVVYLDLDNFKKVNDAYGHMFGDQLLQA 294
Cdd:PRK09581 275 KRYQDALRNnleqsieMAVTDGLTGLHNRryfdMHLKNLIERANE-RGKP-LSLMMIDIDHFKKVNDTYGHDAGDEVLRE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 295 VALAILSCLDEGQVLARLGGDEFIVMATDTSQgsleAMASRILSRLRQ-----PFRI--GLIEIYTGCSLGIALAPQHGN 367
Cdd:PRK09581 353 FAKRLRNNIRGTDLIARYGGEEFVVVMPDTDI----EDAIAVAERIRRkiaeePFIIsdGKERLNVTVSIGVAELRPSGD 428
|
170 180
....*....|....*....|...
gi 1279591189 368 DRESVIRNADTAMYTAKENGRGK 390
Cdd:PRK09581 429 TIEALIKRADKALYEAKNTGRNR 451
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
232-400 |
5.29e-25 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 105.53 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 232 LRVLANTDTITGLPNRNAIHELISDAIATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLAR 311
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 312 LGGDEFIVMATDTsqgSLEAmASRILSRLR-----QPFRIGLIEIYTGCSLGIALAPQHGNDRESVIRnADTAMYTAKEN 386
Cdd:PRK09894 205 YGGEEFIICLKAA---TDEE-ACRAGERIRqlianHAITHSDGRINITATFGVSRAFPEETLDVVIGR-ADRAMYEGKQT 279
|
170
....*....|....
gi 1279591189 387 GRGKfCVFSPEMNQ 400
Cdd:PRK09894 280 GRNR-VMFIDEQNV 292
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
228-392 |
2.30e-24 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 107.79 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 228 AQERLRVLANTDTITGLPNRNAIHELISDAIATRGDTQ--VGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDE 305
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQqpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 306 GQVLARLGGDEFIVMATDTSQgsleAMASRILSRLRQpfRIGLIEIYTGC--------SLGIALAPQHGN-DRESVIRNA 376
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASL----AEAAQVAERIRL--RINEKEILVAKsttirisaSLGVSSAEEDGDyDFEQLQSLA 543
|
170
....*....|....*.
gi 1279591189 377 DTAMYTAKENGRGKFC 392
Cdd:PRK15426 544 DRRLYLAKQAGRNRVC 559
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
229-646 |
1.57e-18 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 89.54 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 229 QERLRV----LANT--DTITGLPNR----NAIHELISDA--IATRGdtqvgVVYL-DLDNFKKVNDAYGHMFGDQLLQAV 295
Cdd:PRK11059 215 EERSRFdtfiRSNAfqDAKTGLGNRlffdNQLATLLEDQemVGAHG-----VVMLiRLPDFDLLQEEWGESQVEELLFEL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 296 ALAILSCLDE--GQVLARLGGDEFIVMATDTSQGSLEAMASRIL-SRLRQPFrIGLIEIYTGCSLGIAlAPQHGNDRESV 372
Cdd:PRK11059 290 INLLSTFVMRypGALLARYSRSDFAVLLPHRSLKEADSLASQLLkAVDALPP-PKMLDRDDFLHIGIC-AYRSGQSTEQV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 373 IRNADTAMYTAKENGRGKFCVFS----PEM---NQRvfeylWlDTNLRKALDNDQLLIHYQPKMTWRGEVRSLEALVRWQ 445
Cdd:PRK11059 368 MEEAEMALRSAQLQGGNGWFVYDkaqlPEKgrgSVR-----W-RTLLEQTLVRGGPRLYQQPAVTRDGKVHHRELFCRIR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 446 SPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKginlRVAVNVSARQLADQTIFSDLKQALKDLNFEYCP 525
Cdd:PRK11059 442 DGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE----NLSINLSVDSLLSRAFQRWLRDTLLQCPRSQRK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 526 -IDVELTESCLIENEELALSVIQQFSQLGAQIHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVA 604
Cdd:PRK11059 518 rLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVG 597
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1279591189 605 VAQALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMPA 646
Cdd:PRK11059 598 ACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
218-390 |
2.19e-18 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 87.19 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 218 SGTDITEERRaqeRLRVLANTDTITGLPNRNAIHELISDAI--ATRGDTQVGVVYLDLDNFKKVNDAYGHMFGDQLLQAV 295
Cdd:PRK10245 190 TATKLAEHKR---RLQVMSTRDGMTGVYNRRHWETLLRNEFdnCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 296 ALAILSCLDEGQVLARLGGDEFIVMATDTSQGSLEAMASRILSRLRQPFRIGLIEIYTGCSLGIA-LAPQHGNDRESvIR 374
Cdd:PRK10245 267 TRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVApLNPQMSHYREW-LK 345
|
170
....*....|....*.
gi 1279591189 375 NADTAMYTAKENGRGK 390
Cdd:PRK10245 346 SADLALYKAKNAGRNR 361
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
102-312 |
1.17e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 74.29 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 102 ARDLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFkLFMTRSEAAASRRNIAGFFRNGSS 181
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLR-DLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 182 YEVERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERLRvlantdtitglpNRNAIHELISDAIatr 261
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALR------------ESEERLRLLVENA--- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279591189 262 gdtQVGVVYLDLD-NFKKVNDAYGHMFG---DQLLQAVALAILSCLDEGQVLARL 312
Cdd:COG2202 147 ---PDGIFVLDLDgRILYVNPAAEELLGyspEELLGKSLLDLLHPEDRERLLELL 198
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
239-384 |
3.14e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 68.88 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 239 DTITGLPNR----NAIHELISDAIATRGDtqvGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVLARLGG 314
Cdd:PRK09966 251 DPLTGLANRaafrSGINTLMNNSDARKTS---ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGG 327
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279591189 315 DEFIVMATDTSQgslEAMASRILSRLRQPFRIGLiEIYTG------CSLGIALAPQHGNdRESVIRNADTAMYTAK 384
Cdd:PRK09966 328 DEFAMVLYDVQS---ESEVQQICSALTQIFNLPF-DLHNGhqttmtLSIGYAMTIEHAS-AEKLQELADHNMYQAK 398
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
113-232 |
1.20e-09 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 59.65 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 113 EQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFkLFMTRSEAAASRRNIAGFFRNG-SSYEVERWVKTR 191
Cdd:COG2202 140 RLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLL-DLLHPEDRERLLELLRRLLEGGrESYELELRLKDG 218
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1279591189 192 KGqRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERL 232
Cdd:COG2202 219 DG-RWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
265-386 |
4.81e-09 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 55.05 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 265 QVGVVYLDLDNFKKVNDAYGHMFGDQLLQAVALAILSCLDEGQVL-ARLGGDEFIVMATDTSQGSLEAMASRI---LSRL 340
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkIKTIGDEFMVVSGLDHPAAAVAFAEDMreaVSAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1279591189 341 RQP------FRIGlieIYTGCSLGIALAPQHGNDR-ESVIRNADTAMYTAKEN 386
Cdd:cd07556 81 NQSegnpvrVRIG---IHTGPVVVGVIGSRPQYDVwGALVNLASRMESQAKAG 130
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
104-244 |
5.37e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 58.32 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 104 DLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFmtrSEAAASRRNIAGFFRNGSSYE 183
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELF---PEDSPLRELLERALAEGQPVT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279591189 184 VERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERLRVLANTDTITGL 244
Cdd:COG3852 78 EREVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
123-232 |
6.71e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 54.22 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 123 IVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLfMTRSEAAASRRNIAGFFRNGSS-YEVERWVKTRKGQRLFLFRN 201
Cdd:TIGR00229 16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLEL-IPEEDREEVRERIERRLEGEPEpVSEERRVRRKDGSEIWVEVS 94
|
90 100 110
....*....|....*....|....*....|.
gi 1279591189 202 KFVHSGSGkNEIYLICSGTDITEERRAQERL 232
Cdd:TIGR00229 95 VSPIRTNG-GELGVVGIVRDITERKEAEEAL 124
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
308-384 |
4.84e-08 |
|
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: 53.37 E-value: 4.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279591189 308 VLARLGGDEFIVMATDTSQGSLEAMASRILSRLRQpfrigLIEIYTGCSLGIAlapqhgndRESVIRNADtAMYTAK 384
Cdd:COG3706 117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVAE-----LPSLRVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
528-645 |
1.00e-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: 54.81 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 528 VELTESCLIeNEELaLSVIQQFSQLGAQIHLDDFgTGYSSLSQLARFpIDAIKLDqsfVRDIHKQSIsqslvRAIVAVAQ 607
Cdd:COG3434 88 LEILEDVEP-DEEL-LEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID---VLALDLEEL-----AELVARLK 155
|
90 100 110
....*....|....*....|....*....|....*...
gi 1279591189 608 ALNLQVIAEGVESAKEDAFLTKNGVNERQGFLFAKPMP 645
Cdd:COG3434 156 RYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
123-222 |
1.40e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 49.94 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 123 IVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFMTRSEAAASRRNIAGfFRNGSSYEVERWVKTRKGQRLFLFRNK 202
Cdd:cd00130 5 VIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENL-LSGGEPVTLEVRLRRKDGSVIWVLVSL 83
|
90 100
....*....|....*....|
gi 1279591189 203 FVHSGSGKNEIYLICSGTDI 222
Cdd:cd00130 84 TPIRDEGGEVIGLLGVVRDI 103
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
103-312 |
7.44e-07 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 52.28 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 103 RDLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKlFMTRSEAAASRRNIAGFFRNGSSY 182
Cdd:COG5809 8 LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILD-FLHPDDEKELREILKLLKEGESRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 183 EVERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERLRVLANTdtitglpnrnaiHELISDaiatrg 262
Cdd:COG5809 87 ELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEK------------FRLIFN------ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279591189 263 DTQVGVVYLDLD-NFKKVNDAYGHMFG---DQLLQAVALAILSCLDEGQVLARL 312
Cdd:COG5809 149 HSPDGIIVTDLDgRIIYANPAACKLLGisiEELIGKSILELIHSDDQENVAAFI 202
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
123-233 |
3.83e-06 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 49.97 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 123 IVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFmtRSEAaasRRNIAGFFRN----GSSYEVERWVKTRKGQRLFL 198
Cdd:COG5809 154 IIVTDLDGRIIYANPAACKLLGISIEELIGKSILELI--HSDD---QENVAAFISQllkdGGIAQGEVRFWTKDGRWRLL 228
|
90 100 110
....*....|....*....|....*....|....*
gi 1279591189 199 FRNKFVHSGSGKNEIYLICsGTDITEERRAQERLR 233
Cdd:COG5809 229 EASGAPIKKNGEVDGIVII-FRDITERKKLEELLR 262
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
123-233 |
3.90e-06 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 49.77 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 123 IVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFMTRSEAAAsrrniagfFRNGSSYEVERWVKTRKGQRLFLFRNK 202
Cdd:COG3829 24 IIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEV--------LKTGKPVTGVIQKTGGKGKTVIVTAIP 95
|
90 100 110
....*....|....*....|....*....|.
gi 1279591189 203 FVHSGsgkNEIYLICSGTDITEERRAQERLR 233
Cdd:COG3829 96 IFEDG---EVIGAVETFRDITELKRLERKLR 123
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
129-224 |
2.42e-05 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 43.22 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 129 NGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFMtrseAAASRRNIAGFFRNGSSYEVERWVKTRKGQRLFLFRnkfVHS-- 206
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA----EPEDSERLREALREGKAVREFEVVLYRKDGEPFPVL---VSLap 73
|
90 100
....*....|....*....|
gi 1279591189 207 --GSGKNEIYLICSGTDITE 224
Cdd:pfam13426 74 irDDGGELVGIIAILRDITE 93
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
476-651 |
3.85e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 45.76 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 476 LDVV----RQVAKWRDKGI--NLRVAVNVSARQLADQTIFSDLKQALkdlnfEYCP-IDVELTESCLIENEelalSVIQQ 548
Cdd:PRK11596 78 LDVVkeqlDLLAQWADFFVrhGLLASVNIDGPTLIALRQQPAILRLI-----ERLPwLRFELVEHIRLPKD----SPFAS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 549 FSQLGaQIHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQSISQSLVRAIVAVAQALNLQVIAEGVESAKEDAFLT 628
Cdd:PRK11596 149 MCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQ 227
|
170 180
....*....|....*....|...
gi 1279591189 629 KNGVNERQGFLFAKPMPaavFER 651
Cdd:PRK11596 228 RSPAFAAQGYFLSRPAP---FET 247
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
103-230 |
2.35e-04 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 44.18 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 103 RDLAQGLSFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFMTRSEAAAsrrnIAGFFRNGSSY 182
Cdd:COG5000 83 EELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAEL----LREALERGWQE 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1279591189 183 EVERwvkTRKGQRLFLfrnkfVHSGSGKNEIYLIcSGTDITEERRAQE 230
Cdd:COG5000 159 EIEL---TRDGRRTLL-----VRASPLRDDGYVI-VFDDITELLRAER 197
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
110-159 |
2.38e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 39.69 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1279591189 110 SFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLF 159
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
104-233 |
2.54e-03 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 41.11 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 104 DLAQGL----SFAEQVVSEANSVIVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLFMTRSEAAASRRNIagfFRNG 179
Cdd:PRK11360 252 NLAQALretrSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLDT---LEHG 328
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1279591189 180 SSYEVERWVKTRKGQRLFLFRNKFVHSGSGKNEIYLICSGTDITEERRAQERLR 233
Cdd:PRK11360 329 TEHVDLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVA 382
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
123-222 |
2.56e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 38.17 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279591189 123 IVILDQNGNIQRFNRLSEEYTGLKEHEVIGQNVFKLF---MTRSEAAASRRNIAGfFRNGSSYEVeRWVKTRKGQRLFLF 199
Cdd:pfam00989 14 IFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIpeeDDAEVAELLRQALLQ-GEESRGFEV-SFRVPDGRPRHVEV 91
|
90 100
....*....|....*....|...
gi 1279591189 200 RNKFVHSGSGkNEIYLICSGTDI 222
Cdd:pfam00989 92 RASPVRDAGG-EILGFLGVLRDI 113
|
|
| |
