|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
239-901 |
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: 650.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 239 QGILGPDLSGVRLRVFDGLEQGDENLLFDNDPQADVGQAPLTAQRVLQVAGRPWTMSLALPPVVAATGLSQASTVLIGGL 318
Cdd:COG5001 6 ALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 319 VTTLLLAWVVFSLRTSEERAGRLAWEMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHN 398
Cdd:COG5001 86 LAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 399 VSRLMPERYRAQHDGYVARMETSASHRNLGMRREVVGLRSDGEEFPLWLAVNKIPTRGALEYVGMVSD---LTERKRIQA 475
Cdd:COG5001 166 LLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIarlITERKRAEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 476 ELQYTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDT 555
Cdd:COG5001 246 RLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 556 VVRMGGDEFVIVLPSVNGRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAG 635
Cdd:COG5001 326 VARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 636 RGNYKFFESHMLRTNQRRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGL 715
Cdd:COG5001 406 RNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 716 IGSIGDWVLISACQQAAKMQQELGQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQL 795
Cdd:COG5001 486 IVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALET 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 796 LHKIRSLGVSLAVDDFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYE 875
Cdd:COG5001 566 LRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLE 645
|
650 660
....*....|....*....|....*.
gi 1180039792 876 FLSQRQCDVAQGFYFGRPVTSTEFVD 901
Cdd:COG5001 646 FLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
367-899 |
1.95e-122 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 386.34 E-value: 1.95e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 367 ILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLmperyraqhdgYVARMETSASHRNlgmrreVVGLRSDGEEFP-- 444
Cdd:PRK10060 124 IVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKL-----------FMSRREAAASRRN------IRGFFRSGNAYEve 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 445 ----------LWLAVNKI--PTRGALEYVGMVS--DLTERKRIQAELQYTAHHDALTTLPNRAVLKDRLDQAIRHarREG 510
Cdd:PRK10060 187 rwiktrkgqrLFLFRNKFvhSGSGKNEIFLICSgtDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINA--ADN 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 511 NKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDEFvIVLPSVNGRDDVVPVVEKLIRILAQ 590
Cdd:PRK10060 265 NQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF-LVLASHTSQAALEAMASRILTRLRL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 591 PISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGNYKFFESHMlrtNQRRLE---TETALRRALDRD 667
Cdd:PRK10060 344 PFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEM---NQRVFEylwLDTNLRKALEND 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 668 EFSLRFQPQINIhSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLISACQQAAKMQQElGQPLQVAVN 747
Cdd:PRK10060 421 QLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDK-GINLRVAVN 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 748 ISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQLLHKIRSLGVSLAVDDFGTGYSSLSYLTRFPID 827
Cdd:PRK10060 499 VSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPID 578
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180039792 828 KLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPVTSTEF 899
Cdd:PRK10060 579 AIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
327-901 |
1.05e-115 |
|
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: 366.03 E-value: 1.05e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 327 VVFSLRTSEERAGRLAWEMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPER 406
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 407 YRAQHDGYVARMETSASHRNLGMRREVVGLRSDGEEFPLWLAVNKIPTRGALEYVGMVSDLTERKRIQAELQYTAHHDAL 486
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 487 TTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDEFVI 566
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 567 VLPSVNGRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGNYKFFESHM 646
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 647 LRTnQRRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLIS 726
Cdd:COG2200 321 ARA-RRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 727 ACQQAAKMQQElGQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQLLHKIRSLGVSL 806
Cdd:COG2200 400 ALRQLARWPER-GLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 807 AVDDFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQ 886
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|....*
gi 1180039792 887 GFYFGRPVTSTEFVD 901
Cdd:COG2200 559 GYLFGRPLPLEELEA 573
|
|
| CHASE1 |
COG3614 |
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms]; |
8-589 |
5.62e-113 |
|
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442832 [Multi-domain] Cd Length: 588 Bit Score: 359.00 E-value: 5.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 8 RKNLPLAITLVVGTLVTLGAWRFVQDVEHERSALAFSQRVDNTADAILDRFAAYQQVLHGGAALLHASRDVSRNEWRVYV 87
Cdd:COG3614 9 RRRLLPLLVLLLGLLLTALAWWAVRRAEEQRARARFERLADELASALEERLDAYEQVLRGLAGLFAASDDVTRAEFRRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 88 EHLMLEEMFPGIQGVGYAVNLGPDDLMAHERAVRADGFPDYRVHPQADRASRpsSAILYLEPFDVRNQRAFGYDMYSNAI 167
Cdd:COG3614 89 ASLDLLRRYPGIQGLGWAPRVPAAERAAFEAAARAEGFPDFRIRPAGERDEY--FPITYIEPLDARNRRALGFDMASEPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 168 RRAAMAKARDSGRPALSGRVTLLQEMDQdlQAGTLLYLPVYREDGPLETVAQRRAALLGWVYSPFRMNNLMQGILGP-DL 246
Cdd:COG3614 167 RRAAMERARDTGRPAASGPVTLVQETDG--QPGFLLYLPVYRGGAPPDTVAERRAALRGFVYAPFRMDDLLAGVLGRlAD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 247 SGVRLRVFDGLEQGDENLLFDNDPQADV-GQAPLTAQRVLQVAGRPWTMSL-ALPPVVAATGLSQASTVLIGGLVTTLLL 324
Cdd:COG3614 245 RDLDLRLYDGTDPGPPQLLYDSSPAAPAaAAPALSATRTLEVAGRTWTLEFrPTPAFEAALRSWLPWLVLLGGLLLSLLL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 325 AWVVFSLRTSEERAGRLAW--EMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRL 402
Cdd:COG3614 325 ALLLLSLARRRRRAEALAAarAALRALRAAELRLRALLRRALLALLRNALALALLLAALLLLLARLLLLLAALLLLLARA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 403 MPERYRAQHDGYVARMETSASHRNLGMRREVVGLRSDGEEFPLWLAvnkIPTRGALEYVGMVSDLTERKRIQAELQYTAH 482
Cdd:COG3614 405 LSAADLLLLQADLLLLRLLLLLRRRLLLVRDLRLGRGLGLGVVLLL---DAILLDLLALAELELAAARAEVALAEALLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 483 HDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGD 562
Cdd:COG3614 482 LVVLLLALLLALLRLLLALAELAATAAREAAGAALLLDREAALLDAALEALLDLLGLLVLLLLAELLLRLGALLLGRALL 561
|
570 580
....*....|....*....|....*..
gi 1180039792 563 EFVIVLPSVNGRDDVVPVVEKLIRILA 589
Cdd:COG3614 562 GGVGAGEGLVIIAELAALELELLRLEA 588
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
658-894 |
3.91e-105 |
|
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: 325.65 E-value: 3.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 658 TALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLISACQQAAKMQQe 737
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 738 LGQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQLLHKIRSLGVSLAVDDFGTGYSS 817
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180039792 818 LSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPV 894
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
470-898 |
1.61e-102 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 337.51 E-value: 1.61e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 470 RKRIQAELQYtahhDALTTLPNRAVLKDRLDQAIRHARregnKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEAS 549
Cdd:PRK11359 369 RQHIEQLIQF----DPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREK 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 550 VRDVDTVVRMGGDEFVIVLPSvNGRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLcpDDGQDERALLKHADTAMY 629
Cdd:PRK11359 441 LKPDQYLCRIEGTQFVLVSLE-NDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMD 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 630 QAKAAGRGNYKFFESHMLRTNQRRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPM 709
Cdd:PRK11359 518 YIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 710 AEEMGLIGSIGDWVLISACQQAAKMQQELGQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENS 789
Cdd:PRK11359 598 AEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHD 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 790 RETVQLLHKIRSLGVSLAVDDFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVE 869
Cdd:PRK11359 678 TEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVE 757
|
410 420
....*....|....*....|....*....
gi 1180039792 870 TLEQYEFLSQRQCDVAQGFYFGRPVTSTE 898
Cdd:PRK11359 758 TKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
657-894 |
9.33e-99 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 309.15 E-value: 9.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 657 ETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLISACQQAAKMQQ 736
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 737 ELGQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQLLHKIRSLGVSLAVDDFGTGYS 816
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180039792 817 SLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPV 894
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
659-893 |
1.93e-77 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 251.85 E-value: 1.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 659 ALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLISACQQAAkmQQEL 738
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA--QLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 739 GQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQLLHKIRSLGVSLAVDDFGTGYSSL 818
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180039792 819 SYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRP 893
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
647-905 |
2.29e-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: 256.38 E-value: 2.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 647 LRTNQRRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLis 726
Cdd:COG4943 263 LRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVI-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 727 acQQAAK-MQQELGQP--LQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITE--GVLLENSRETVQLLhkiRS 801
Cdd:COG4943 341 --EQVFRdLGDLLAADpdFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITErgFIDPAKARAVIAAL---RE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 802 LGVSLAVDDFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQ 881
Cdd:COG4943 416 AGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARG 495
|
250 260
....*....|....*....|....
gi 1180039792 882 CDVAQGFYFGRPVTSTEFVDSAQQ 905
Cdd:COG4943 496 VQYGQGWLFAKPLPAEEFIAWLAA 519
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
471-899 |
6.86e-71 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 247.70 E-value: 6.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 471 KRIQAELQYTAHHDALTTLPNRAVLKDRLDQAIrhARREgnKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASV 550
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVV--ARKQ--TTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 551 RDVDTVVRMGGDEFVIVLPSVNGRDDVVPVVEKLIRILAQPISVvgHEMIITP--SIGVCLCpDDGQDERALLKHADTAM 628
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPI--QRIQLRPscSIGIAMF-YGDLTAEQLYSRAISAA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 629 YQAKAAGRGNYKFFESHMLRTNQRRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQlGDVS-PGLFI 707
Cdd:PRK13561 374 FTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPD-GSWDlPEGLI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 708 PMAEEMGLIGSIGDWVLISACQQAAKMQQElGQPLQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLE 787
Cdd:PRK13561 453 DRIESCGLMVTVGHWVLEESCRLLAAWQER-GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRID 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 788 NSRETVQLLHKIRSLGVSLAVDDFGTGYSSLSYLTRF---PIDKLKIDQSFVRDITTdasDAAVASAIIAMAHSLKLAVV 864
Cdd:PRK13561 532 DPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVI 608
|
410 420 430
....*....|....*....|....*....|....*
gi 1180039792 865 AEGVETLEQYEFLSQRQCDVAQGFYFGRPVTSTEF 899
Cdd:PRK13561 609 AEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIF 643
|
|
| CHASE |
pfam03924 |
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ... |
77-266 |
4.48e-66 |
|
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 427591 Cd Length: 184 Bit Score: 219.08 E-value: 4.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 77 DVSRNEWRVYVEHLMLEEmfPGIQGVGYAVNLGPDDLMAHERAVRADGFPDYRVHPQADRASRpsSAILYLEPFDvRNQR 156
Cdd:pfam03924 2 SVDREEFRRYAASLLLRR--PGIQGLGWAPRVPAAERAAFEAAVRAEGFPDFTIRPAGDRDEY--FPIIYIEPLA-GNNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 157 AFGYDMYSNAIRRAAMAKARDSGRPALSGRVTLLQemDQDLQAGTLLYLPVYReDGPLETVAQRRAALLGWVYSPFRMNN 236
Cdd:pfam03924 77 ALGFDMASEPVRREAIERARDTGEPVLSGPVTLVQ--DGDGQPGFLLYLPVYR-GGPPDTVAERRAALLGFVYAPFRIDD 153
|
170 180 190
....*....|....*....|....*....|.
gi 1180039792 237 LMQ-GILGPDLSGVRLRVFDGLEQGDENLLF 266
Cdd:pfam03924 154 LLEaALLRLGEDGLDLALYDGTSASAPELLY 184
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
429-899 |
9.21e-65 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 230.60 E-value: 9.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 429 MRREvvgLRSDGEEFPLWLAVNKIPTRGALEYVGMVSDLTERKRIQAELQYT----AHHDALTTLPNRAVLKDRLDQAIR 504
Cdd:PRK11829 179 MAKE---LEDIGDHGVLHHQLTLPAHHQDDELGVLVRNYNRNQQLLADAYADmgriSHRFPVTELPNRSLFISLLEKEIA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 505 -HARREGNkvAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDEFVIVLPSVNGRDDVVPVVEK 583
Cdd:PRK11829 256 sSTRTDHF--HLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARR 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 584 LIRILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGNYKFFESHMLRTNQRRLETETALRRA 663
Cdd:PRK11829 334 IMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 664 LDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLISACQQAAKMQQElGQPLQ 743
Cdd:PRK11829 414 IENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKAR-GVSLP 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 744 VAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEITEGVLLENSRETVQLLHKIRSLGVSLAVDDFGTGYSSLSYL-- 821
Cdd:PRK11829 493 LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnh 572
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180039792 822 -TRFPIDKLKIDQSFVRDITtdaSDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPVTSTEF 899
Cdd:PRK11829 573 lKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEF 648
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
482-639 |
1.14e-61 |
|
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: 205.87 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 482 HHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGG 561
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180039792 562 DEFVIVLPSVNgRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGNY 639
Cdd:cd01949 81 DEFAILLPGTD-LEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
367-642 |
1.39e-61 |
|
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: 210.22 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 367 ILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMETSASHRNLGMRREVVGLRSDGEEFPLW 446
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 447 LAVNKIpTRGALEYVGMVSDLTERKRIQAELQYTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRI 526
Cdd:COG2199 81 LELLLL-LLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 527 NDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDEFVIVLPSVNgRDDVVPVVEKLIRILAQ-PISVVGHEMIITPSI 605
Cdd:COG2199 160 NDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTD-LEEAEALAERLREALEQlPFELEGKELRVTVSI 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 1180039792 606 GVCLCPDDGQDERALLKHADTAMYQAKAAGRGNYKFF 642
Cdd:COG2199 239 GVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
331-902 |
1.76e-61 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 227.25 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 331 LRTSEERAGRL---AWEMTD------ALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSR 401
Cdd:PRK09776 504 VLNKDGEVERLlgiNMDMTEvrqlneALFQEKERLHITLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLT 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 402 -----------LMPERYRAQhdgyvarmetsASHRNLGMRREVVGLRSDGEEFPLWLAVNKIPTRGAlEYVGMV---SDL 467
Cdd:PRK09776 584 vlhitfgdngpLMENIYSCL-----------TSRSAAYLEQDVVLHCRSGGSYDVHYSITPLSTLDG-ENIGSVlviQDV 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 468 TERKRIQAELQYTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLE 547
Cdd:PRK09776 652 TESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 548 ASVRDVDTVVRMGGDEFVIVLPSVNgRDDVVPVVEKLIR-ILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADT 626
Cdd:PRK09776 732 SMLRSSDVLARLGGDEFGLLLPDCN-VESARFIATRIISaINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADI 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 627 AMYQAKAAGRGNYKFFESHM--LRTNQRRLETETALRRALDRDEFSLRFQ---PQINIHSGQLigcEALVRWHHPQLGDV 701
Cdd:PRK09776 811 ACYAAKNAGRGRVTVYEPQQaaAHSEHRALSLAEQWRMIKENQLMMLAHGvasPRIPEARNHW---LISLRLWDPEGEII 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 702 SPGLFIPMAEEMGLIGSIGDWVLISACQQAAkmqQELGQP-LQVAVNISPQQFFRNDIISSINRALAMSGFPASQLEVEI 780
Cdd:PRK09776 888 DEGAFRPAAEDPALMHALDRRVIHEFFRQAA---KAVASKgLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEI 964
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 781 TEGVLLENSRETVQLLHKIRSLGVSLAVDDFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLK 860
Cdd:PRK09776 965 TETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLG 1044
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1180039792 861 LAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPVTSTEFVDS 902
Cdd:PRK09776 1045 MKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNS 1086
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
481-638 |
5.59e-61 |
|
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: 204.02 E-value: 5.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 481 AHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMG 560
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 561 GDEFVIVLPSVN--GRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGN 638
Cdd:pfam00990 81 GDEFAILLPETSleGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
479-642 |
2.39e-54 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 185.91 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 479 YTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVR 558
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 559 MGGDEFVIVLPSVNgRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGN 638
Cdd:smart00267 81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1180039792 639 YKFF 642
Cdd:smart00267 160 VAVY 163
|
|
| CHASE |
smart01079 |
This domain is found in the extracellular portion of receptor-like proteins - such as serine ... |
75-255 |
5.02e-53 |
|
This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.
Pssm-ID: 215015 Cd Length: 176 Bit Score: 182.53 E-value: 5.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 75 SRDVSRNEWRVYVEHLMLEEMFPGIQGVGYAVNLGPDDLMAHERAVRADGFPDYRVHPQADRASRPSSAILYLEPFDvRN 154
Cdd:smart01079 1 SESVSRAEFRRFALELQLNRRLPGIQGLGWAPRVPPAERAAFEAALRAGGPGLFNIRLAPDGERDEYFVITYIEPLA-GN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 155 QRAFGYDMYSNAIRRAAMAKARDSGRPALSGRVTLLQEMDQdlQAGTLLYLPVYREDGPLETvaqRRAALLGWVYSPFRM 234
Cdd:smart01079 80 EAALGLDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGD--GRGFLLRLPVYRGGPPTST---RREALWGFVSAVFRL 154
|
170 180
....*....|....*....|..
gi 1180039792 235 NNLMQGILGP-DLSGVRLRVFD 255
Cdd:smart01079 155 DDLLEGLLGAlDLPGLDLALYD 176
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
481-643 |
1.22e-44 |
|
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: 158.65 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 481 AHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMG 560
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 561 GDEFVIVLPSVNgRDDVVPVVEKLIR-ILAQPISVVGHEMI-ITPSIGVCLCPDDGQDERALLKHADTAMYQAKAAGRGN 638
Cdd:TIGR00254 82 GEEFVVILPGTP-LEDALSKAERLRDaINSKPIEVAGSETLtVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 1180039792 639 YKFFE 643
Cdd:TIGR00254 161 VVVAD 165
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
652-905 |
1.23e-44 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 169.40 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 652 RRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIGDWVLISACQQA 731
Cdd:PRK10551 260 LRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 732 AKMQQELGQPLQVAVNISPQQFFRNDIISSINRALAMsgFPASQLEV--EITEGVLLENSrETVQLLHKIRSLGVSLAVD 809
Cdd:PRK10551 340 AELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLAS--LPADHFQIvlEITERDMVQEE-EATKLFAWLHSQGIEIAID 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 810 DFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFY 889
Cdd:PRK10551 417 DFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYW 496
|
250
....*....|....*.
gi 1180039792 890 FGRPVTSTEFVDSAQQ 905
Cdd:PRK10551 497 ISRPLPLEDFVRWLKE 512
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
470-636 |
1.37e-32 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 132.33 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 470 RKRIQ----AELQYT---AHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISI 542
Cdd:PRK09581 274 RKRYQdalrNNLEQSiemAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 543 ALRLEASVRDVDTVVRMGGDEFVIVLPSVNgRDDVVPVVEKLIRILAQ-PISVV-GHEMI-ITPSIGVCLCPDDGQDERA 619
Cdd:PRK09581 354 AKRLRNNIRGTDLIARYGGEEFVVVMPDTD-IEDAIAVAERIRRKIAEePFIISdGKERLnVTVSIGVAELRPSGDTIEA 432
|
170
....*....|....*..
gi 1180039792 620 LLKHADTAMYQAKAAGR 636
Cdd:PRK09581 433 LIKRADKALYEAKNTGR 449
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
484-636 |
1.87e-30 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 122.10 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 484 DALTTLPNRAVLKDRLDQAIRhaRREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDE 563
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLR--NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180039792 564 FVIVLPSVNgRDDVVPVVEKLIR-ILAQPISVVGHEMIITPSIGVCLCpDDGQDERALLKHADTAMYQAKAAGR 636
Cdd:PRK09894 210 FIICLKAAT-DEEACRAGERIRQlIANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGR 281
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
352-477 |
1.15e-29 |
|
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: 114.31 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 352 SERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMETSASHrnlGMRR 431
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPE---PVSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1180039792 432 EVVGLRSDGEEFPLWLAVNKIPTRGALEYV-GMVSDLTERKRIQAEL 477
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEVSVSPIRTNGGELGVvGIVRDITERKEAEEAL 124
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
461-636 |
8.73e-28 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 119.35 E-value: 8.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 461 VGMVSDLTERkriQAELQYTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLI 540
Cdd:PRK15426 381 RRMVSNMFVL---QSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLS 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 541 SIALRLEASVRDVDTVVRMGGDEFVIVLPSVnGRDDVVPVVEKL-IRILAQPISVVGHEMI-ITPSIGV-CLCPDDGQDE 617
Cdd:PRK15426 458 HAAGLISSSLRAQDVAGRVGGEEFCVVLPGA-SLAEAAQVAERIrLRINEKEILVAKSTTIrISASLGVsSAEEDGDYDF 536
|
170
....*....|....*....
gi 1180039792 618 RALLKHADTAMYQAKAAGR 636
Cdd:PRK15426 537 EQLQSLADRRLYLAKQAGR 555
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
348-489 |
2.50e-24 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 105.70 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 348 ALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPEryraqHDGYVARMETSASHRNL 427
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPE-----DSPLRELLERALAEGQP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180039792 428 GMRREVVGLRSDGEEFPLWLAVNKIPTR-GALEYVGMVSDLTERKRIQAELQYTAHHDALTTL 489
Cdd:COG3852 76 VTEREVTLRRKDGEERPVDVSVSPLRDAeGEGGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
348-593 |
2.72e-23 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 100.10 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 348 ALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMETSASHRnl 427
Cdd:COG2202 5 ALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 428 gmRREVVGLRSDGEEFplWLAVNKIPTRGA----LEYVGMVSDLTERKRIQAELQYTAHHDALTTLPNR-AVLKDRLDQA 502
Cdd:COG2202 83 --RGELRNRRKDGSLF--WVELSISPVRDEdgeiTGFVGIARDITERKRAEEALRESEERLRLLVENAPdGIFVLDLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 503 IRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDEFVIVLPSVNGRDDVVPVVE 582
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGGEV 238
|
250
....*....|.
gi 1180039792 583 KLIRILAQPIS 593
Cdd:COG2202 239 IGVLGIVRDIT 249
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
467-637 |
6.11e-21 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 95.67 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 467 LTERKRiqaELQYTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRL 546
Cdd:PRK10245 194 LAEHKR---RLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 547 EASVRDVDTVVRMGGDEFVIVL---PSVNGRDDVVPVVEKL--IRILAQPisvvghEMIITPSIGVC-LCPDDGQdERAL 620
Cdd:PRK10245 271 QITLRGSDVIGRFGGDEFAVIMsgtPAESAITAMSRVHEGLntLRLPNAP------QVTLRISVGVApLNPQMSH-YREW 343
|
170
....*....|....*..
gi 1180039792 621 LKHADTAMYQAKAAGRG 637
Cdd:PRK10245 344 LKSADLALYKAKNAGRN 360
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
344-477 |
1.10e-20 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 92.78 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 344 EMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMetsas 423
Cdd:COG2202 127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRL----- 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1180039792 424 HRNLGMRREVVGLRSDGEEFPLWLAVNKIPTRGALE---YVGMVSDLTERKRIQAEL 477
Cdd:COG2202 202 LEGGRESYELELRLKDGDGRWVWVEASAVPLRDGGEvigVLGIVRDITERKRAEEAL 258
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
455-632 |
1.79e-20 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 95.07 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 455 RGALEYVGMVSDLTERK-RIQA---ELQYTAHHDALTTLPNRAVLKDRLDQAIRH--ARREGnkvAVLMLDLDHFKRIND 528
Cdd:PRK09966 218 RFALDFNSLLDEMEEWQlRLQAknaQLLRTALHDPLTGLANRAAFRSGINTLMNNsdARKTS---ALLFLDGDNFKYIND 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 529 TLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDEFVIVLPSVNGRDDVVPVVEKLIRILAQPISV-VGHEMIITPSIGV 607
Cdd:PRK09966 295 TWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGY 374
|
170 180
....*....|....*....|....*
gi 1180039792 608 CLCPDDGQDERaLLKHADTAMYQAK 632
Cdd:PRK09966 375 AMTIEHASAEK-LQELADHNMYQAK 398
|
|
| CHASE |
COG3452 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
8-806 |
1.14e-19 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442675 [Multi-domain] Cd Length: 785 Bit Score: 94.61 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 8 RKNLPLAITLVVGTLVTLGAWRFVQDVEHERSALAFSQRVDNTADAILDRFAAYQQVLHGGAALLHASRDVSRNEWRVYV 87
Cdd:COG3452 12 RPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEFERLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 88 EHLMleEMFPGIQGVGYAvnlgpddlmaheravradgfPDYR---VHPQAdrasrpssailylepfdvRNQRAFGYDMYS 164
Cdd:COG3452 92 RNLL--EDYPGIRNIALA--------------------PDGViryVYPLA------------------GNEAALGLDLRT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 165 NAIRRAAMAKARDSGRPALSGRVTLLQ-EMdqdlqaGTLLYLPVYREDGpletvaqrRAALLGWVYSPFRMNNLMQGILG 243
Cdd:COG3452 132 DPEQRAAALRARESGQLVLAGPVNLVQgGR------GLIGRLPVFLDGG--------DDRFWGFVSAVIDLDRLLDSAGL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 244 PDLSG---VRLRVFDGLeqGDENLLFDNDPQADvgqAPLTAQRVLQVAGRPWTMSlALPPVVAATGLSQASTVLIGGLVT 320
Cdd:COG3452 198 DDAQDgyqIALRGRDGD--GAEGEVFYGDAALF---DQDPVTLEVNLPGGSWQLA-AAPKGGWLASPRNALPLRLAGLLI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 321 TLLLAWVVFSLRTS--EERAGRLAWEMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADeviGHN 398
Cdd:COG3452 272 SLLLALLVYLLRQLllLRLLLLLLRLELIAAALLLLLLALDLLLELLLLLRLAEALLQERLRALALLAALEDLL---LLK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 399 VSRLMPERYRAQHDGYVARMETSASHRNLGMR-REVVGLRSDGEEFPLWLAVNKIPTRGALEYVGMVSDLTERKRIQAEL 477
Cdd:COG3452 349 FDRDLLDLLLLLELEAILALLLLLRRLLRSREaRGGLGGDLVRVGGVIDGRVAVILIIEALELAEARLAALDQERDASDV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 478 QYTAHHDALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVV 557
Cdd:COG3452 429 ALGAALVVLEALLIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLLGDALRERIRRALLRLQLLSLDLSALA 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 558 RMGGDEFVIVLpsVNGRDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVCLcpDDGQDERALLKHADTAMYQAKAAGRG 637
Cdd:COG3452 509 AVLGAESLAGL--LISVFIDARILEAERLELALVAGEVALEELLLRLLGEIL--LLRAELILALLDAKSGLSALELSGLL 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 638 NYKFFESHMLRTNQRRLETETALRRALDRDEFSLRFQPQINIHSGQLIGCEALVR----WHHPQLGDVSPGLFIPMAEEM 713
Cdd:COG3452 585 AGRAALDSLLLLLALALRQLDESALFILEELLLRLIIDLRIERLLLLLLGGEILLgelaLLLLLLVLIILILLSVEEAGL 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 714 GLIGSIGDWVLISACQQAAKMQQELGQPLQVAVNISPQQFFR---NDIISSINRALAMSGFPASQLEVEITEGVLLENSR 790
Cdd:COG3452 665 ILALSLLLALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGllaELVAEALRLALALAQLLLRLLLAELLQLLLLLLGL 744
|
810
....*....|....*.
gi 1180039792 791 ETVQLLHKIRSLGVSL 806
Cdd:COG3452 745 ILLELLLRLDGLLVEL 760
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
484-636 |
7.46e-19 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 90.79 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 484 DALTTLPNRAVLKDRLDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASVRDVDTVVRMGGDE 563
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180039792 564 FVIVLPsvngrDDVVPVVEKLIRILAQPISVVGHEMIITPSIGVC-LCPDDGQDEraLLKHADTAMYQAKAAGR 636
Cdd:NF040885 424 FCIILI-----DYEEAEAQNLIERIRQHLRTIDPDKRVSFSWGAYqMQPGDTLDD--AYKAADERLYLNKKQKH 490
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
309-489 |
1.13e-16 |
|
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: 83.87 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 309 QASTVLIGGLVTTLLLAWVVFSLRTSEERagrlaweMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFG 388
Cdd:COG5809 103 SSKLSPIFDQNGDIEGMLAISRDITERKR-------MEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 389 YSADEVIGHNVSRLMPERYRAQHDGYVARMETSASHRNLgmrrEVVGLRSDGEEFplWLAVNKIPTRGALE---YVGMVS 465
Cdd:COG5809 176 ISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQG----EVRFWTKDGRWR--LLEASGAPIKKNGEvdgIVIIFR 249
|
170 180
....*....|....*....|....
gi 1180039792 466 DLTERKRIQAELQYTahhDALTTL 489
Cdd:COG5809 250 DITERKKLEELLRKS---EKLSVV 270
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
423-894 |
2.62e-14 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 77.21 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 423 SHRNLGMRREVVgLRSDGEEFPLwlavnkiPTRGALEYvgMVSDLT----ERKRIQAELQYTAHHDALTTLPNRAVLKDR 498
Cdd:PRK11059 176 ARRILNGEREQA-VAGSGYEWPR-------TASRALDH--LLSELQdareERSRFDTFIRSNAFQDAKTGLGNRLFFDNQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 499 LDQAIRHARREGNKVAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASV-RDVDTVV-RMGGDEFVIVLPSVNGRdD 576
Cdd:PRK11059 246 LATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPGALLaRYSRSDFAVLLPHRSLK-E 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 577 VVPVVEKLIR-ILAQPISvvghEMIITPS---IGVClCPDDGQDERALLKHADTAMYQAKAAGRGNYKFFESHML----R 648
Cdd:PRK11059 325 ADSLASQLLKaVDALPPP----KMLDRDDflhIGIC-AYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDKAQLpekgR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 649 TNQR-RleteTALRRALDRDEFSLRFQPQINIHsGQLIGCEALVRWHHPQLGDVSPGLFIPMAEEMGLIGSIgDWVLISa 727
Cdd:PRK11059 400 GSVRwR----TLLEQTLVRGGPRLYQQPAVTRD-GKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQY-DRQVIE- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 728 cQQAAKMQQELGQPLqvAVNISpqqffrndIISSINRA---------LAMSGFPASQLEVEITEGVLLENSRETVQLLHK 798
Cdd:PRK11059 473 -RVLPLLRYWPEENL--SINLS--------VDSLLSRAfqrwlrdtlLQCPRSQRKRLIFELAEADVCQHISRLRPVLRM 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 799 IRSLGVSLAVDDFGTGYSSLSYLTRFPIDKLKIDQSFVRDITTDASDAAVASAIIAMAHSLKLAVVAEGVETLEQYEFLS 878
Cdd:PRK11059 542 LRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQ 621
|
490
....*....|....*.
gi 1180039792 879 QRQCDVAQGFYFGRPV 894
Cdd:PRK11059 622 ELGVSGGQGDFFAESQ 637
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
344-466 |
4.69e-14 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 76.35 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 344 EMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMETSAS 423
Cdd:PRK11359 2 KLTDADNAADGIFFPALEQNMMGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1180039792 424 HRNLGMRREVVGLRSDGEEFPLWLAVNKIPTRGALEYVGMVSD 466
Cdd:PRK11359 82 ARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRD 124
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
344-478 |
7.87e-14 |
|
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: 75.01 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 344 EMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMETSAS 423
Cdd:COG5809 5 KMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGES 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180039792 424 HRNLGMRRevvgLRSDGEEfpLWLAVNKIPTRGA----LEYVGMVSDLTERKRIQAELQ 478
Cdd:COG5809 85 RDELEFEL----RHKNGKR--LEFSSKLSPIFDQngdiEGMLAISRDITERKRMEEALR 137
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
354-466 |
8.08e-14 |
|
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: 68.60 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 354 RRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQ-HDGYVARMETSASHRNLGMRRE 432
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEvAELLRQALLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1180039792 433 VvglrSDGEefPLWLAVNKIPTRGA----LEYVGMVSD 466
Cdd:pfam00989 81 V----PDGR--PRHVEVRASPVRDAggeiLGFLGVLRD 112
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
349-514 |
6.82e-13 |
|
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: 71.73 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 349 LRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPER--YRAQHDGyvaRMETSASHRN 426
Cdd:COG3829 6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSplLEVLKTG---KPVTGVIQKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 427 LGMRREVVglrsdgeefplwlaVNKIPTRGALEYVGMVS---DLTERKRIQAELQytahhdaLTTLPNRAVLKDRLD--- 500
Cdd:COG3829 83 GGKGKTVI--------------VTAIPIFEDGEVIGAVEtfrDITELKRLERKLR-------EEELERGLSAKYTFDdii 141
|
170
....*....|....*..
gi 1180039792 501 ---QAIRHARREGNKVA 514
Cdd:COG3829 142 gksPAMKELLELAKRVA 158
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
354-417 |
7.70e-12 |
|
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: 61.26 E-value: 7.70e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180039792 354 RRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVAR 417
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
771-895 |
2.44e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 63.67 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 771 FPASQLEVEITEGVLLenSRETVQLLHKIRSLGVSLAVDDFGTGYSSLSYLTRfpIDKLKIDqsfVRDITtdasdAAVAS 850
Cdd:COG3434 81 LPPERVVLEILEDVEP--DEELLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID---VLALD-----LEELA 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1180039792 851 AIIAMAHSLKLAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPVT 895
Cdd:COG3434 149 ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
327-474 |
1.02e-09 |
|
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: 61.52 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 327 VVFSLRTSEErAGRLAW---EMTDALRAS-------ERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIG 396
Cdd:COG5000 54 VRLPVTGDDE-IGELARafnRMTDQLKEQreeleerRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIG 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180039792 397 HNVSRLMPERYRAQHDGYVARMETSASHRnlgmrrevvglRSDGEEFPLWLAVNKIPTRGaleYVGMVSDLTERKRIQ 474
Cdd:COG5000 133 KPLEELLPELDLAELLREALERGWQEEIE-----------LTRDGRRTLLVRASPLRDDG---YVIVFDDITELLRAE 196
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
348-477 |
2.89e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 60.52 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 348 ALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQhdgyVARMEtsASHRNL 427
Cdd:COG5805 151 ILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEE----FKERI--ESITEV 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1180039792 428 GMRREVVGLRSDGEEFPLWLAVNKIPTR----GALEYVGMVSDLTERKRIQAEL 477
Cdd:COG5805 225 WQEFIIEREIITKDGRIRYFEAVIVPLIdtdgSVKGILVILRDITEKKEAEELM 278
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
344-478 |
3.77e-09 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 60.37 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 344 EMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPEryRAQHDGYVAR-METSA 422
Cdd:PRK11360 252 NLAQALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPP--NTPFASPLLDtLEHGT 329
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 423 SHRNLgmrrEVVGLRSDGEefpLWLAVN----KIPTRGALEYVGMVSDLTERKRIQAELQ 478
Cdd:PRK11360 330 EHVDL----EISFPGRDRT---IELSVStsllHNTHGEMIGALVIFSDLTERKRLQRRVA 382
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
553-632 |
9.44e-09 |
|
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: 55.69 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 553 VDTVVRMGGDEFVIVLPSVNgRDDVVPVVEKLIRILAQPISVVghemiITPSIGVClcpddgqdERALLKHADtAMYQAK 632
Cdd:COG3706 115 VDLVARYGGEEFAILLPGTD-LEGALAVAERIREAVAELPSLR-----VTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
363-467 |
1.36e-08 |
|
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: 53.41 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 363 TADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARmetsASHRNLGMRREVVGLRSDGEE 442
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLEN----LLSGGEPVTLEVRLRRKDGSV 76
|
90 100
....*....|....*....|....*..
gi 1180039792 443 FPLWLAVNKIPTRGA--LEYVGMVSDL 467
Cdd:cd00130 77 IWVLVSLTPIRDEGGevIGLLGVVRDI 103
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
513-633 |
1.10e-07 |
|
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: 51.59 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 513 VAVLMLDLDHFKRINDTLGHHVGDDLLISIALRLEASV-RDVDTVVRMGGDEFVIVLPSVNGRdDVVPVVEKLIRILA-- 589
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPA-AAVAFAEDMREAVSal 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1180039792 590 QPISVVGHEMIITPSIGVCLCPDDGQDER-----ALLKHADTAMYQAKA 633
Cdd:cd07556 81 NQSEGNPVRVRIGIHTGPVVVGVIGSRPQydvwgALVNLASRMESQAKA 129
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
354-410 |
4.04e-07 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 47.93 E-value: 4.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1180039792 354 RRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQ 410
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDA 57
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
379-469 |
4.10e-07 |
|
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: 48.61 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 379 FNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVARMETSASHrnlgmrREVVGLRSDGEEFplWLAVNKIPTRGA- 457
Cdd:pfam13426 7 VNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVRE------FEVVLYRKDGEPF--PVLVSLAPIRDDg 78
|
90
....*....|....*
gi 1180039792 458 ---LEYVGMVSDLTE 469
Cdd:pfam13426 79 gelVGIIAILRDITE 93
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
360-472 |
8.95e-07 |
|
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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 48.18 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 360 LEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPERYRAQHDGYVAR-METSASHrnlgmRREVVGLRS 438
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRaLEGEEPI-----DFLEELLLN 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1180039792 439 DGEEfplWLAVNKIPTRGA----LEYVGMVSDLTERKR 472
Cdd:pfam08448 76 GEER---HYELRLTPLRDPdgevIGVLVISRDITERRR 110
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
332-515 |
1.92e-06 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 51.76 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 332 RTSEERAGRLAWEMTDALRASERRYRA---ILEHTADGILTIDER-------GIVRS-----------FNKAAEAIFGYS 390
Cdd:PRK13558 108 AVSDDATAAIAERIESAVPEHSRDTEArmpISDLTVESDRRLKERaldeapvGITIAdatlpdepliyINDAFERITGYS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 391 ADEVIGHNVSRLMPERYRAQHdgyVARMETSASHRNlGMRREVVGLRSDGEEFplWLAVNKIPTRG----ALEYVGMVSD 466
Cdd:PRK13558 188 PDEVLGRNCRFLQGEDTNEER---VAELREAIDEER-PTSVELRNYRKDGSTF--WNQVDIAPIRDedgtVTHYVGFQTD 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1180039792 467 LTERKRIQAELQytAHHDALTTLPNR--AVLKDRLDQAIRHARREGNKVAV 515
Cdd:PRK13558 262 VTERKEAELALQ--RERRKLQRLLERveGLVNDVTSALVRATDREEIEAAV 310
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
307-478 |
1.99e-05 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 47.92 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 307 LSQASTVLIGGLVTTLLLAWVVFSLRTSEERAGRLAWEMTDALRASERRYRAILEHTADGILTIDERGIVRSFNKAAEAI 386
Cdd:COG3290 37 LLLLLFLLFVIILLLLLLILLLILLLLLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 387 FGYsadEVIGHNVSRLMPERYRAqhdgyvarmetsashrnlGMRREVVGLRSdgeefpLWLAVNKIPTRGALEYVGMVS- 465
Cdd:COG3290 117 LGL---DAIGRPIDEVLAEVLET------------------GERDEEILLNG------RVLVVNRVPIRDDGRVVGAVAt 169
|
170
....*....|....*
gi 1180039792 466 --DLTERKRIQAELQ 478
Cdd:COG3290 170 frDRTELERLEEELE 184
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
753-894 |
8.07e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 45.38 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 753 FFRNDIISSIN----RALAMSGFPASQ--------LEVEITEGVLLenSRETVqlLHKIRSLGvSLAVDDFGTGYSSLSY 820
Cdd:PRK11596 95 FVRHGLLASVNidgpTLIALRQQPAILrlierlpwLRFELVEHIRL--PKDSP--FASMCEFG-PLWLDDFGTGMANFSA 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180039792 821 LTRFPIDKLKIDQS-FVRDITTDASDAAVASAIIAMAHSLKlAVVAEGVETLEQYEFLSQRQCDVAQGFYFGRPV 894
Cdd:PRK11596 170 LSEVRYDYIKVARElFIMLRQSEEGRNLFSQLLHLMNRYCR-GVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
341-477 |
1.72e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 42.35 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 341 LAWEMTDALRASERRYRA------ILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIGHNVSRLMPErYRAQhdgy 414
Cdd:PRK13560 185 FAEDITERKRAEERIDEAlhflqqLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPA-QPAD---- 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180039792 415 VARMETSASHRNLGMRREVVGLRS-DGEEFPLWLAVNKI----PTRGALEYVGMVSDLTERKRIQAEL 477
Cdd:PRK13560 260 DYQEADAAKFDADGSQIIEAEFQNkDGRTRPVDVIFNHAefddKENHCAGLVGAITDISGRRAAEREL 327
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
291-478 |
1.82e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 42.35 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 291 PWTMSLALPP-VVAATGLSQASTVLIGgLVTTLLLAWV----VFSLRTSEERAG-RLAWE--------------MTDALR 350
Cdd:PRK09776 194 PWPFTFIIVLlMWSAVRLPRMEAFLIF-LTTVMMVSLMmaadPSLLATPRTYLMsHMPWLpfllillpanimtmVMYAFR 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180039792 351 A-------SERRYRAILEHTADGILTIDERGIVRSFNKAAEAIFGYSADEVIG------------HNVSRLMPERYRAQH 411
Cdd:PRK09776 273 AerkhiseSETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGltfqqltwpedlNKDLQQVEKLLSGEI 352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180039792 412 DGYvaRMEtsashrnlgmRREvvgLRSDGEEFPLWLAVNKIPTRG--ALEYVGMVSDLTERKRIQAELQ 478
Cdd:PRK09776 353 NSY--SME----------KRY---YRRDGEVVWALLAVSLVRDTDgtPLYFIAQIEDINELKRTEQVNE 406
|
|
| |
