|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
86-749 |
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: 653.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 86 ALEAVRDGLWDWDLVTDRMFVSPGYAALIGLAPEELGDPIETWKKRLHPEEYATVLEAHRNHLQGLTDNLDHIYRLRHKD 165
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 166 GDYRWIHSRGRVLRDALGKPLHYTGVARDITLQRLKEDHLRQAAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSED 245
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 246 VLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSI----- 320
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARliter 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 321 KRSENELDFLAHHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQL 400
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 401 DERCLLSRLGGDEFAILVEN-DDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQ 479
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 480 AKDSGRNAYAFYTRVLTARARAHVQVESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVA 559
Cdd:COG5001 401 AKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 560 EECGLIAALDNWVLKRACRQMREWQQRGVELEFVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFE 639
Cdd:COG5001 481 EETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 640 QSLNLLCRLRILGVNLAIDDFGTGYSSLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEH 719
Cdd:COG5001 561 EALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVET 640
|
650 660 670
....*....|....*....|....*....|
gi 489174719 720 QDQALFLREHGCDFGQGYWYGRPQPAEALR 749
Cdd:COG5001 641 EEQLEFLRELGCDYAQGYLFSRPLPAEELE 670
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
316-748 |
3.78e-124 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 385.96 E-value: 3.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 316 DLSSIKRSENELDFLAHHDSLTGLPNRVLLRERIEQALENGKDRTVAgaLLLIDLDHFKHINDSLGHTTGDMLLKEVSKR 395
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVG--IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 396 LQHQLDERCLLSRLGGDEFAILVENDDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADA 475
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADT 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 476 ALFQAKDSGRNAYAFYTRVLTARARAHVQVESALRHALEHDELRVHYQPVHDLaSGRIVGVESLVRWQHPERGLVPPGEF 555
Cdd:PRK10060 380 AMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 556 VPVAEECGLIAALDNWVLKRACRQMREWQQRGVELEfVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVM 635
Cdd:PRK10060 459 ISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLR-VAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLI 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 636 EDFEQSLNLLCRLRILGVNLAIDDFGTGYSSLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAE 715
Cdd:PRK10060 538 ENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAE 617
|
410 420 430
....*....|....*....|....*....|...
gi 489174719 716 GIEHQDQALFLREHGCDFGQGYWYGRPQPAEAL 748
Cdd:PRK10060 618 GVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
191-749 |
5.27e-120 |
|
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: 372.58 E-value: 5.27e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 191 VARDITLQRLKEDHLRQAAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLA 270
Cdd:COG2200 15 LLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 271 LREQDVWSGEIWNRRKSGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENELDFLAHHDSLTGLPNRVLLRERIE 350
Cdd:COG2200 95 LLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 351 QALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLGGDEFAILV-ENDDPEAVARL 429
Cdd:COG2200 175 LLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLlLLAAAAAAAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 430 SQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRNAYAFYtRVLTARARAHVQVESAL 509
Cdd:COG2200 255 LRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFF-AAAEARARRRLALESEL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 510 RHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVLKRACRQMREWQQRGVE 589
Cdd:COG2200 334 REALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 590 LeFVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRLRILGVNLAIDDFGTGYSSLMR 669
Cdd:COG2200 414 L-RLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSY 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 670 LKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQPAEALR 749
Cdd:COG2200 493 LKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELE 572
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
507-747 |
4.06e-114 |
|
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: 344.91 E-value: 4.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 507 SALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVLKRACRQMREWQQR 586
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 587 GVELeFVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRLRILGVNLAIDDFGTGYSS 666
Cdd:cd01948 81 GPDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 667 LMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQPAE 746
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 489174719 747 A 747
Cdd:cd01948 240 E 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
506-747 |
2.39e-105 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 322.24 E-value: 2.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 506 ESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVLKRACRQMREWQQ 585
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 586 RGVELEFVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRLRILGVNLAIDDFGTGYS 665
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 666 SLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQPA 745
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 489174719 746 EA 747
Cdd:smart00052 241 DD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
161-753 |
4.11e-99 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 324.03 E-value: 4.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 161 LRHKDGDYRWIH-SRGRVlrDALGKpLHYTGVARDITLQRLKEDHLRQAAAVFDSTREGVLVTDAQAVIVHVNPSFERIT 239
Cdd:PRK11359 93 LEKKDGSKIWTRfALSKV--SAEGK-VYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQCNRAFTEMF 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 240 GYRSEDVLGKTPAILRSGRQDQA-----FYQRLWLALREQDVW------SGEIWNRRKSGEIYPQWLHIR---------- 298
Cdd:PRK11359 170 GYCISEASGMQPDTLLNIPEFPAdnrirLQQLLWKTARDQDEFllltrtGEKIWIKASISPVYDVLAHLQnlvmtfsdit 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 299 ---------------------------------------------AVRND------------------------------ 303
Cdd:PRK11359 250 eerqirqlegnilaamcssppfhemgeiicrniesvlneshvslfALRNGmpihwassshgaeyqnaqswsatirqrdga 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 304 -----------QGQLTHYVGVFSDLS------SIKRSEN--ELDFLAHHDSLTGLPNRVLLRERIEQALengkDRTVAGA 364
Cdd:PRK11359 330 pagtlqiktssGAETSAFIERVADISqhlaalALEQEKSrqHIEQLIQFDPLTGLPNRNNLHNYLDDLV----DKAVSPV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 365 LLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLGGDEFAILVENDDPEAVARLSQRILDGFNAPFDIH 444
Cdd:PRK11359 406 VYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMID 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 445 CQPIYISASLGVSLypEDASDVDHLMQHADAALFQAKDSGRNAYAFYTRVLTARARAHVQVESALRHALEHDELRVHYQP 524
Cdd:PRK11359 486 DKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQP 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 525 VHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVLKRACRQMREWQQRGVELEFVAVNVSSRLFNR 604
Cdd:PRK11359 564 QIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRS 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 605 GGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRLRILGVNLAIDDFGTGYSSLMRLKRLPVHKLKIDQGF 684
Cdd:PRK11359 644 NQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSF 723
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174719 685 VAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQPAEalrfDLP 753
Cdd:PRK11359 724 VDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAE----EIP 788
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
319-747 |
8.97e-89 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 292.77 E-value: 8.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 319 SIKRSENELDFLAHHDSLTGLPNRVLLRERIEQALEngkdRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQH 398
Cdd:PRK13561 219 LLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVA----RKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 399 QLDERCLLSRLGGDEFAILVEN-DDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASdVDHLMQHADAAL 477
Cdd:PRK13561 295 VLSPRMVLAQISGYDFAIIANGvKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLT-AEQLYSRAISAA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 478 FQAKDSGRNAYAFYTRVLTARARAHVQVESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVP 557
Cdd:PRK13561 374 FTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLID 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 558 VAEECGLIAALDNWVLKRACRQMREWQQRGVELEfVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMED 637
Cdd:PRK13561 454 RIESCGLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 638 FEQSLNLLCRLRILGVNLAIDDFGTGYSSLMRL---KRLPVHKLKIDQGFVAGLPgavDDAAIARAIVALAQSMGLRVVA 714
Cdd:PRK13561 533 PHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLP---EDDSMVAAIIMLAQSLNLQVIA 609
|
410 420 430
....*....|....*....|....*....|...
gi 489174719 715 EGIEHQDQALFLREHGCDFGQGYWYGRPQPAEA 747
Cdd:PRK13561 610 EGVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
57-748 |
3.21e-87 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 297.74 E-value: 3.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 57 LLYLYLVRQFRRKAQAY-------DELHGSEQRLNR-------ALEAVRDGLWDWDLVTD------RMFvspgyaALIGL 116
Cdd:PRK09776 372 LLAVSLVRDTDGTPLYFiaqiediNELKRTEQVNERlmeritlANEAGGIGIWEWDLKPNiiswdkRMF------ELYEI 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 117 APEELGDpIETWKKRLHPEEYATVLEAHRNHLQGLTdNLDHIYRLRHKDGdYRWIHSRGRVLRDALGKPLHYTGVARDIT 196
Cdd:PRK09776 446 PPHIKPT-WQVWYACLHPEDRQRVEKEIRDALQGRS-PFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMT 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 197 LQRLKEDHLRQAAA----VFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGK----------------TPAILRS 256
Cdd:PRK09776 523 EVRQLNEALFQEKErlhiTLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVplltvlhitfgdngplMENIYSC 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 257 GRQDQAFYQrlwlalrEQDVwsgeIWNRRKsGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENELDFLAHHDSL 336
Cdd:PRK09776 603 LTSRSAAYL-------EQDV----VLHCRS-GGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDAL 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 337 TGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLGGDEFAI 416
Cdd:PRK09776 671 THLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGL 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 417 LVENDDPEAVARLSQRILDGFNA-PFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRNAYAFYTRVL 495
Cdd:PRK09776 751 LLPDCNVESARFIATRIISAINDyHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQ 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 496 TARARAH--VQVESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVL 573
Cdd:PRK09776 831 AAAHSEHraLSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVI 910
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 574 KRACRQMRE-WQQRGVElefVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRLRILG 652
Cdd:PRK09776 911 HEFFRQAAKaVASKGLS---IALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAG 987
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 653 VNLAIDDFGTGYSSLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCD 732
Cdd:PRK09776 988 CRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVD 1067
|
730
....*....|....*.
gi 489174719 733 FGQGYWYGRPQPAEAL 748
Cdd:PRK09776 1068 LAYGYAIARPQPLDLL 1083
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
506-742 |
1.07e-80 |
|
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: 257.63 E-value: 1.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 506 ESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVLKRACRQMREWQQ 585
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 586 RGVELefVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRLRILGVNLAIDDFGTGYS 665
Cdd:pfam00563 81 GPDIK--LSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489174719 666 SLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRP 742
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
330-744 |
7.37e-74 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 252.94 E-value: 7.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 330 LAHHDSLTGLPNRVLLRERIEQALENgKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRL 409
Cdd:PRK11829 231 ISHRFPVTELPNRSLFISLLEKEIAS-STRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 410 GGDEFAILVEN-DDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRNAY 488
Cdd:PRK11829 310 SKTEFAVLARGtRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 489 AFYTRVLTARARAHVQVESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAAL 568
Cdd:PRK11829 390 MVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 569 DNWVLKRACRQMREWQQRGVELEfVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMEDFEQSLNLLCRL 648
Cdd:PRK11829 470 GNWVLEEACRILADWKARGVSLP-LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLREL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 649 RILGVNLAIDDFGTGYSSLMRL---KRLPVHKLKIDQGFVAGLPgavDDAAIARAIVALAQSMGLRVVAEGIEHQDQALF 725
Cdd:PRK11829 549 QGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQW 625
|
410
....*....|....*....
gi 489174719 726 LREHGCDFGQGYWYGRPQP 744
Cdd:PRK11829 626 LLEHGIQCGQGFLFSPPLP 644
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
506-749 |
6.74e-72 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 244.06 E-value: 6.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 506 ESALRHALEHDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVLKRACRQMREW-- 583
Cdd:COG4943 273 RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLla 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 584 QQRGVeleFVAVNVSSRLFNRGGLEERIANALEESGLEPRYLELEVTESAVMeDFEQSLNLLCRLRILGVNLAIDDFGTG 663
Cdd:COG4943 353 ADPDF---HISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFGTG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 664 YSSLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQ 743
Cdd:COG4943 429 YSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPL 508
|
....*.
gi 489174719 744 PAEALR 749
Cdd:COG4943 509 PAEEFI 514
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
332-489 |
4.74e-62 |
|
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: 205.10 E-value: 4.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 332 HHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLGG 411
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489174719 412 DEFAILVENDDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRNAYA 489
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
221-491 |
1.12e-58 |
|
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: 200.59 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 221 VTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYPQWLHIRAV 300
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 301 RNDQGQLTHYVGV---FSDLSSIKRSENELDFLAHHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHIN 377
Cdd:COG2199 81 LELLLLLLALLLLllaLEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 378 DSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLGGDEFAILVENDDPEAVARLSQRILDGFNA-PFDIHCQPIYISASLGV 456
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGV 240
|
250 260 270
....*....|....*....|....*....|....*
gi 489174719 457 SLYPEDASDVDHLMQHADAALFQAKDSGRNAYAFY 491
Cdd:COG2199 241 ALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
330-491 |
7.13e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 180.52 E-value: 7.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 330 LAHHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRL 409
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 410 GGDEFAILVENDDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRNAYA 489
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 489174719 490 FY 491
Cdd:smart00267 162 VY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
331-486 |
1.10e-50 |
|
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: 174.36 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 331 AHHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLG 410
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174719 411 GDEFAILVEN---DDPEAVARLSQRILDGFNAPFDIHCQPIYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRN 486
Cdd:pfam00990 81 GDEFAILLPEtslEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
494-748 |
1.77e-40 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 156.31 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 494 VLTARARAHVQVESALRHalehDELRVHYQPVHDLASGRIVGVESLVRWQHPERGLVPPGEFVPVAEECGLIAALDNWVL 573
Cdd:PRK10551 257 LLSLRMRPGKEILTGIKR----GQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLF 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 574 K---RACRQMREWQQRGVELefvAVNVSSRLFNRGGLEERIANALEEsgLEPRYLE--LEVTESAVMEDfEQSLNLLCRL 648
Cdd:PRK10551 333 EliaRDAAELQKVLPVGAKL---GINISPAHLHSDSFKADVQRLLAS--LPADHFQivLEITERDMVQE-EEATKLFAWL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 649 RILGVNLAIDDFGTGYSSLMRLKRLPVHKLKIDQGFVAGLPGAVDDAAIARAIVALAQSMGLRVVAEGIEHQDQALFLRE 728
Cdd:PRK10551 407 HSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRE 486
|
250 260
....*....|....*....|
gi 489174719 729 HGCDFGQGYWYGRPQPAEAL 748
Cdd:PRK10551 487 RGVNFLQGYWISRPLPLEDF 506
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
330-488 |
1.52e-37 |
|
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: 137.85 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 330 LAHHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRL 409
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 410 GGDEFAILVENDDPEAVARLSQRILDGFNA-PFDIHCQP-IYISASLGVSLYPEDASDVDHLMQHADAALFQAKDSGRNA 487
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 489174719 488 Y 488
Cdd:TIGR00254 161 V 161
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
71-327 |
2.87e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 134.77 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 71 QAYDELHGSEQRLNRALEAVRDGLWDWDLVTDRMFVSPGYAALIGLAPEELGDpiETWKKRLHPEEYATVLEAHRNHLQG 150
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELLRAALAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 151 lTDNLDHIYRLRHKDGDYRWIHSRGRVLRDALGKPLHYTGVARDITLQRLKEDHLRQAA----AVFDSTREGVLVTDAQA 226
Cdd:COG2202 79 -GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEerlrLLVENAPDGIFVLDLDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 227 VIVHVNPSFERITGYRSEDVLGKTPAILRSgRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYPQWLHIRAVRN-DQG 305
Cdd:COG2202 158 RILYVNPAAEELLGYSPEELLGKSLLDLLH-PEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLrDGG 236
|
250 260
....*....|....*....|..
gi 489174719 306 QLTHYVGVFSDLSSIKRSENEL 327
Cdd:COG2202 237 EVIGVLGIVRDITERKRAEEAL 258
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
196-419 |
5.57e-31 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 122.44 E-value: 5.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 196 TLQRLKEDHLRQAAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQD 275
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 276 VWSGEIWNRRKSGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENELDFLAHHDSLTGLPNRVLlrerIEQALEN 355
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDG----IFVLDLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 356 GKDRTVAGALLLI-----DLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRL-GGDEFAILVE 419
Cdd:COG2202 157 GRILYVNPAAEELlgyspEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLkDGDGRWVWVE 226
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
330-499 |
1.60e-27 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 116.54 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 330 LAHHDSLTGLPNR----VLLRERIEQALENGKDRtvagALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCL 405
Cdd:PRK09581 291 MAVTDGLTGLHNRryfdMHLKNLIERANERGKPL----SLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 406 LSRLGGDEFAILVENDDPEAVARLSQRILDGF-NAPFDIHCQ--PIYISASLGVSLYPEDASDVDHLMQHADAALFQAKD 482
Cdd:PRK09581 367 IARYGGEEFVVVMPDTDIEDAIAVAERIRRKIaEEPFIISDGkeRLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKN 446
|
170
....*....|....*..
gi 489174719 483 SGRNayafytRVLTARA 499
Cdd:PRK09581 447 TGRN------RVVALAA 457
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
325-486 |
1.39e-25 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 112.03 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 325 NELDFLAHHDSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERC 404
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 405 LLSRLGGDEFAILVEN---DDPEAVA-RLSQRILDgfnAPFDIHC-QPIYISASLGVSLYPEDAS-DVDHLMQHADAALF 478
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGaslAEAAQVAeRIRLRINE---KEILVAKsTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLY 548
|
....*...
gi 489174719 479 QAKDSGRN 486
Cdd:PRK15426 549 LAKQAGRN 556
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
331-481 |
4.36e-24 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 105.47 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 331 AHHDSLTGLPNRVLLRERIEQALENGKDRTvAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLG 410
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARK-TSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489174719 411 GDEFAILVENDDPEA-VARLSQRILDGFNAPFDIH-CQPIYISASLGVSLYPEDASdVDHLMQHADAALFQAK 481
Cdd:PRK09966 327 GDEFAMVLYDVQSESeVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHAS-AEKLQELADHNMYQAK 398
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
75-327 |
3.39e-22 |
|
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: 100.82 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 75 ELHGSEQRLNRALEAVRDGLWDWDLVTDRMFVSPGYAALIGLAPEELGDPieTWKKRLHPEEYATVLEAHRNHLQGLTDN 154
Cdd:COG5809 9 QLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGT--NILDFLHPDDEKELREILKLLKEGESRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 155 lDHIYRLRHKDGDYRWIHSRGRVLRDALGKPLHYTGVARDITLQRLKEDHLRQAAA----VFDSTREGVLVTDAQAVIVH 230
Cdd:COG5809 87 -ELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEkfrlIFNHSPDGIIVTDLDGRIIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 231 VNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYpqWLHIRAVR-NDQGQLTH 309
Cdd:COG5809 166 ANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWR--LLEASGAPiKKNGEVDG 243
|
250
....*....|....*...
gi 489174719 310 YVGVFSDLSSIKRSENEL 327
Cdd:COG5809 244 IVIIFRDITERKKLEELL 261
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
297-491 |
7.07e-22 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 96.67 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 297 IRAVRNDQGQLTHYVGVFSDL----SSIKRSENEL-DFLAHHDSLTGLPNRVLLRERIEQALENGKDRTVAgaLLLIDLD 371
Cdd:PRK09894 90 LLAIVEGHWQDAHFDAFQEGLlsftAALTDYKIYLlTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNLY--LALLDID 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 372 HFKHINDSLGHTTGDMLLKEVSKRLQHQLDERCLLSRLGGDEFAILVENDDPEAVARLSQRI-LDGFNAPFDIHCQPIYI 450
Cdd:PRK09894 168 RFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIrQLIANHAITHSDGRINI 247
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489174719 451 SASLGVSLYPEDASdVDHLMQHADAALFQAKDSGRNAYAFY 491
Cdd:PRK09894 248 TATFGVSRAFPEET-LDVVIGRADRAMYEGKQTGRNRVMFI 287
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
103-192 |
7.50e-22 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 90.48 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 103 RMFVSPGYAALIGLAPEELGDPIETWKKRLHPEEYATVLEAHRNHLQGLTDnLDHIYRLRHKDGDYRWIHSRGRVLRDAL 182
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEP-YSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
90
....*....|
gi 489174719 183 GKPLHYTGVA 192
Cdd:pfam08447 80 GKPVRVIGVA 89
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
201-327 |
4.58e-20 |
|
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: 86.58 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 201 KEDHLRqaaAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVW-SG 279
Cdd:TIGR00229 1 SEERYR---AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPvSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489174719 280 EIWNRRKSGEIYPQWLHIRAVRnDQGQLTHYVGVFSDLSSIKRSENEL 327
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
318-486 |
4.34e-19 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 89.89 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 318 SSIKRSENE--LDFLAHHDSLTGLPNR----VLLRERIEQALENGKDRTvagaLLLIDLDHFKHINDSLGHTTGDMLLKE 391
Cdd:PRK10245 190 TATKLAEHKrrLQVMSTRDGMTGVYNRrhweTLLRNEFDNCRRHHRDAT----LLIIDIDHFKSINDTWGHDVGDEAIVA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 392 VSKRLQHQLDERCLLSRLGGDEFAILVENDDPE-AVARLSqRILDGFNApFDIHCQP-IYISASLGVSLYPEDASDVDHL 469
Cdd:PRK10245 266 LTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAEsAITAMS-RVHEGLNT-LRLPNAPqVTLRISVGVAPLNPQMSHYREW 343
|
170
....*....|....*..
gi 489174719 470 MQHADAALFQAKDSGRN 486
Cdd:PRK10245 344 LKSADLALYKAKNAGRN 360
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
221-324 |
5.17e-19 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 91.12 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 221 VTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYPQWLHIRAV 300
Cdd:TIGR02938 19 ITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVAPV 98
|
90 100
....*....|....*....|....
gi 489174719 301 RNDQGQLTHYVGVFSDLSSIKRSE 324
Cdd:TIGR02938 99 LNEAGETTHFLGMHRDITELHRLE 122
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
334-745 |
3.31e-18 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 89.15 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 334 DSLTGLPNRVLLRERIEQALENGKDRTVAGALLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDER--CLLSRLGG 411
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYpgALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 412 DEFAILVenddP-----EAVARLSQ--RILDGFNAP-------FdIHcqpiyisasLGVSLYPEDASdVDHLMQHADAAL 477
Cdd:PRK11059 311 SDFAVLL----PhrslkEADSLASQllKAVDALPPPkmldrddF-LH---------IGICAYRSGQS-TEQVMEEAEMAL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 478 FQAKDSGRNAYAFYTR-VLTARARAHVQVESALRHALEHDELRVHYQPVhDLASGRIVGVESLVRWQHPERGLVPPGEFV 556
Cdd:PRK11059 376 RSAQLQGGNGWFVYDKaQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQPA-VTRDGKVHHRELFCRIRDGQGELLSAELFM 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 557 PVAEECGLIAALDNWVLKRACRQMREWQQrgvelEFVAVNVS-----SRLFNRgGLEERIanaLE-ESGLEPRyLELEVT 630
Cdd:PRK11059 455 PMVQQLGLSEQYDRQVIERVLPLLRYWPE-----ENLSINLSvdsllSRAFQR-WLRDTL---LQcPRSQRKR-LIFELA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 631 ESAVMEDFEQSLNLLCRLRILGVNLAIDDFG-----TGYsslmrLKRLPVHKLK--------ID-----QGFVAGLPGav 692
Cdd:PRK11059 525 EADVCQHISRLRPVLRMLRGLGCRLAVDQAGltvvsTSY-----IKELNVELIKlhpslvrnIHkrtenQLFVRSLVG-- 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489174719 693 ddaaiaraivALAQSmGLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQPA 745
Cdd:PRK11059 598 ----------ACAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
206-339 |
1.56e-16 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 81.82 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 206 RQAAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSgrQDQAFYQRLWLALRE-QDVWSGEIWNR 284
Cdd:COG3852 7 ELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALAEgQPVTEREVTLR 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489174719 285 RKSGEIYPQWLHIRAVRNDQGQlTHYVGVFSDLSSIKRSENELDFLAHHDSLTGL 339
Cdd:COG3852 85 RKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
210-316 |
1.65e-15 |
|
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: 73.22 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 210 AVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVW-SGEIWNRRKSG 288
Cdd:pfam00989 5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESrGFEVSFRVPDG 84
|
90 100 110
....*....|....*....|....*....|
gi 489174719 289 EIYpqWLHIRA--VRNDQGQLTHYVGVFSD 316
Cdd:pfam00989 85 RPR--HVEVRAspVRDAGGEILGFLGVLRD 112
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
228-318 |
8.09e-15 |
|
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: 70.57 E-value: 8.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 228 IVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREqdVWSGEIWNRRKSGEIYPQWLHIRAVRNDQGQL 307
Cdd:pfam13426 4 IIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKA--VREFEVVLYRKDGEPFPVLVSLAPIRDDGGEL 81
|
90
....*....|.
gi 489174719 308 THYVGVFSDLS 318
Cdd:pfam13426 82 VGIIAILRDIT 92
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
198-364 |
4.45e-14 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 76.03 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 198 QRLKEDHLRQAAAvfdstreGVLVTDAQA---VIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQ 274
Cdd:PRK13558 147 RRLKERALDEAPV-------GITIADATLpdePLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 275 DVWSGEIWNRRKSGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENEL--------DFLAHHDSLTGLPNRVLL- 345
Cdd:PRK13558 220 RPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALqrerrklqRLLERVEGLVNDVTSALVr 299
|
170 180
....*....|....*....|..
gi 489174719 346 ---RERIEQALengKDRTVAGA 364
Cdd:PRK13558 300 atdREEIEAAV---CDRVGAGG 318
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
69-327 |
3.62e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 73.17 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 69 KAQAYDELHGSEQRLnraLEAVRDGLWDWDLVTDRMFVSPGYA----ALIGLAPEELGDPIETWKKRLHPEEYATVLEAH 144
Cdd:PRK13560 59 EAEAQDCREQCERNL---KANIPGGMFLFALDGDGTFSFPSLLdangELAAIAKHDLMADKGLLAMLIGGDDGDFFFANP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 145 RNHLQGLTDNL------DHIYRLRHKDGdyRWIHSRGRVLRDALGKpLHYTGVARDITLQRLKEDHLRQA----AAVFDS 214
Cdd:PRK13560 136 FRSAETIAMALqsddwqEEEGHFRCGDG--RFIDCCLRFERHAHAD-DQVDGFAEDITERKRAEERIDEAlhflQQLLDN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 215 TREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYPQW 294
Cdd:PRK13560 213 IADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAAKFDADGSQIIEAEFQNKDGRTRPVD 292
|
250 260 270
....*....|....*....|....*....|....*
gi 489174719 295 LHIRAVRND--QGQLTHYVGVFSDLSSIKRSENEL 327
Cdd:PRK13560 293 VIFNHAEFDdkENHCAGLVGAITDISGRRAAEREL 327
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
215-317 |
4.10e-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. 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: 63.04 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 215 TREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSGEIYPQW 294
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 489174719 295 LHIRAVRNDQGQLTHYVGVFSDL 317
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
210-328 |
1.36e-11 |
|
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: 67.49 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 210 AVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRqdqafyqRLWLALREQDVWSGEIWNRRKSGE 289
Cdd:COG3829 15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS-------PLLEVLKTGKPVTGVIQKTGGKGK 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 489174719 290 iypQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENELD 328
Cdd:COG3829 88 ---TVIVTAIPIFEDGEVIGAVETFRDITELKRLERKLR 123
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
212-326 |
5.37e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 64.84 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 212 FDSTREGVLVTDAQAV---IVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRRKSG 288
Cdd:PRK13559 49 MEQTRMAMCITDPHQPdlpIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDG 128
|
90 100 110
....*....|....*....|....*....|....*...
gi 489174719 289 EIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENE 326
Cdd:PRK13559 129 EPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRAL 166
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
228-313 |
1.01e-10 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 58.50 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 228 IVHVNPSFERITGYRSEDVLGKTPAILRSGRQD--QAFYQRLWLALREQDVWSGEIWNRRKSGEIYpqWLHIRA--VRND 303
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDdrERVREALWEALKGGEPYSGEYRIRRKDGEYR--WVEARArpIRDE 78
|
90
....*....|
gi 489174719 304 QGQLTHYVGV 313
Cdd:pfam08447 79 NGKPVRVIGV 88
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
92-195 |
2.59e-10 |
|
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: 58.03 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 92 DGLWDWDLVTDRMFVSPGYAALIGLAPEELGDpiETWKKRLHPEEYATVLEAHRNHLQGLtDNLDHIYRLRHKDGDYRWI 171
Cdd:cd00130 3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIG--KSLLDLIHPEDREELRERLENLLSGG-EPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 489174719 172 HSRGRVLRDALGKPLHYTGVARDI 195
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
81-195 |
8.77e-10 |
|
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: 56.66 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 81 QRLNRALEAVRDGLWDWDLVTDRMFVSPGYAALIGLAPEEL-GDPIetwKKRLHPEEYATVLEAHRNHLQGLTDNLDHIY 159
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEViGKSL---LDLIPEEDDAEVAELLRQALLQGEESRGFEV 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 489174719 160 RLRHKDGDYRWIHSRGRVLRDALGKPLHYTGVARDI 195
Cdd:pfam00989 78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
79-196 |
3.17e-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: 55.37 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 79 SEQRLNRALEAVRDGLWdwdlVTDR----MFVSPGYAALIGLAPEELGDpiETWKKRLHPEEYATVLEAHRNHLQGLTDN 154
Cdd:TIGR00229 1 SEERYRAIFESSPDAII----VIDLegniLYVNPAFEEIFGYSAEELIG--RNVLELIPEEDREEVRERIERRLEGEPEP 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489174719 155 LDHIYRLRHKDGDYRWIHSRGRVLRDAlGKPLHYTGVARDIT 196
Cdd:TIGR00229 75 VSEERRVRRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDIT 115
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
156-196 |
5.10e-08 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 49.49 E-value: 5.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489174719 156 DHIYRLRHKDGDYRWIHSRGRVLRDALGKPLHYTGVARDIT 196
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
209-358 |
7.64e-08 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 55.83 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 209 AAVfDSTREGVLVTD---AQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIWNRR 285
Cdd:PRK13557 34 AAV-ETTRMPMIVTDpnqPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 286 KSGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSENEL------------------DF-------LAHHDSL-TGL 339
Cdd:PRK13557 113 KDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALrqaqkmealgqltggiahDFnnllqvmSGYLDVIqAAL 192
|
170
....*....|....*....
gi 489174719 340 PNRVLLRERIEQALENGKD 358
Cdd:PRK13557 193 SHPDADRGRMARSVENIRA 211
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
80-327 |
1.03e-07 |
|
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: 55.12 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 80 EQRLNRALEAVRDGLWDWDLVTDRMFVSPGYAALIGLAPEEL-GDPIETWkkrLHPEEYATVLEAHRNHLQGLtdNLDHI 158
Cdd:COG5805 33 TEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIiGKTIFDF---LEKEYHYRVKTRIERLQKGY--DVVMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 159 YRLRHKDGDYRWIHSRGRVLRDALGKPLHYTgvARDITLQRLKEDHLRQAA----AVFDSTREGVLVTDAQAVIVHVNPS 234
Cdd:COG5805 108 EQIYCKDGELIYVEVKLFPIYNQNGQAAILA--LRDITKKKKIEEILQEQEerlqTLIENSPDLICVIDTDGRILFINES 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 235 FERITGYRSEDVLGKTPAILRSGRQDQAFYQRLwlalreqdvwsGEIWNRRKSGEIYPQWLH-----------IRAVRND 303
Cdd:COG5805 186 IERLFGAPREELIGKNLLELLHPCDKEEFKERI-----------ESITEVWQEFIIEREIITkdgriryfeavIVPLIDT 254
|
250 260
....*....|....*....|....
gi 489174719 304 QGQLTHYVGVFSDLSSIKRSENEL 327
Cdd:COG5805 255 DGSVKGILVILRDITEKKEAEELM 278
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
206-272 |
1.73e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 48.93 E-value: 1.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489174719 206 RQAAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALR 272
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
386-481 |
3.45e-07 |
|
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: 51.06 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 386 DMLLKEVSKR-LQHQLDercLLSRLGGDEFAILVENDDPEAVARLSQRILDGFNAPFDIHcqpiyISASLGVSlypedas 464
Cdd:COG3706 100 DYLTKPFDPEeLLARVD---LVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLR-----VTVSIGVA------- 164
|
90
....*....|....*..
gi 489174719 465 dVDHLMQHADaALFQAK 481
Cdd:COG3706 165 -GDSLLKRAD-ALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
365-435 |
4.36e-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: 49.66 E-value: 4.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489174719 365 LLLIDLDHFKHINDSLGHTTGDMLLKEVSKRLQHQLDER-CLLSRLGGDEFAILVENDDPEAVARLSQRILD 435
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMRE 75
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
212-318 |
4.83e-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: 48.95 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 212 FDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTPAILRSGRQDQAFYQRLWLALREQDVWSGEIwNRRKSGEIY 291
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEER 79
|
90 100
....*....|....*....|....*..
gi 489174719 292 PQWLHIRAVRNDQGQLTHYVGVFSDLS 318
Cdd:pfam08448 80 HYELRLTPLRDPDGEVIGVLVISRDIT 106
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
634-747 |
5.97e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 52.50 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 634 VMEDFEQSLNLLCRLRIL---GVNLAIDDF--GTGYSSLMRLkrlpVHKLKIDqgfVAGLPGAVddaaiARAIVALAQSM 708
Cdd:COG3434 90 ILEDVEPDEELLEALKELkekGYRIALDDFvlDPEWDPLLPL----ADIIKID---VLALDLEE-----LAELVARLKRY 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 489174719 709 GLRVVAEGIEHQDQALFLREHGCDFGQGYWYGRPQPAEA 747
Cdd:COG3434 158 GIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
198-324 |
1.63e-06 |
|
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: 51.12 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 198 QRLKEDHLRQAAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSEDVLGKTpaiLRSGRQDQAFYQRLWLALREQdvW 277
Cdd:COG5000 82 REELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKP---LEELLPELDLAELLREALERG--W 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489174719 278 SGEIwnrrksgEIYPQWLHIRAVRNDQGQLTHYVGVFSDLSSIKRSE 324
Cdd:COG5000 157 QEEI-------ELTRDGRRTLLVRASPLRDDGYVIVFDDITELLRAE 196
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
164-327 |
2.53e-06 |
|
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: 50.89 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 164 KDGDYRWIHSRgrVLRDALgkplhytgvarditlqrLKEDHLrqaAAVFDSTREGVLVTDAQAVIVHVNPSFERITGYRS 243
Cdd:COG5805 14 KDGTPIWINNE--VLRMAI-----------------EITEEL---ETILENLPDAIIAVNREGKVIYINPAMEKLLGYTS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 244 EDVLGKT-PAILRSGRQDQAFYQRLWLALREQDVWSGEIWNrrKSGEIYPQWLHIRAVRNDQGQLTHYvgVFSDLSSIKR 322
Cdd:COG5805 72 EEIIGKTiFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYC--KDGELIYVEVKLFPIYNQNGQAAIL--ALRDITKKKK 147
|
....*
gi 489174719 323 SENEL 327
Cdd:COG5805 148 IEEIL 152
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
75-210 |
5.65e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 49.07 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 75 ELHGSEQRLNRALEAVRDGLwdwdLVTDR----MFVSPGYAALIGLAPEEL-GDPIETWkkRLHPEEYATVLEAHRNHLQ 149
Cdd:COG3852 1 ALRESEELLRAILDSLPDAV----IVLDAdgriTYVNPAAERLLGLSAEELlGRPLAEL--FPEDSPLRELLERALAEGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174719 150 GLTDnldHIYRLRHKDGDYRWIHSRGRVLRDALGKPlHYTGVARDITLQRLKEDHLRQAAA 210
Cdd:COG3852 75 PVTE---REVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRAEK 131
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
115-208 |
1.12e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 48.90 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174719 115 GLAPEELGDPIETWKKRLHPEEYATVLEAHRNHLQGLTDNLDHIYRLRHKDGDYRWIHSRGRVLRDALGKPLHYTGVARD 194
Cdd:PRK13560 508 GYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVID 587
|
90
....*....|....
gi 489174719 195 ITLQRLKEDHLRQA 208
Cdd:PRK13560 588 ISERKHAEEKIKAA 601
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
81-149 |
2.98e-05 |
|
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: 42.39 E-value: 2.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174719 81 QRLNRALEAVRDGLWDWDLVTDRMFVSPGYAALIGLAPEELGDpiETWKKRLHPEEYATVLEAHRNHLQ 149
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIG--KSLLELIHPEDRERVQEALQRLLS 67
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
210-245 |
1.30e-04 |
|
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: 40.61 E-value: 1.30e-04
10 20 30
....*....|....*....|....*....|....*.
gi 489174719 210 AVFDSTREGVLVTDAQAVIVHVNPSFERITGYRSED 245
Cdd:pfam13188 5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYELLG 40
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
278-318 |
3.47e-04 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 38.70 E-value: 3.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489174719 278 SGEIWNRRKSGEIYPQWLHIRAVRNDQGQLTHYVGVFSDLS 318
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
|
|
| |
