|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
771-1406 |
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: 698.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 771 QLGRLNGLLRRVRHAIGDRQKLAELRENPGQHLFALDCLRADGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQRRAER 850
Cdd:COG5001 44 LLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 851 ELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLASLQHSGSWEGEILQ 930
Cdd:COG5001 124 LAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 931 KRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHRLAYYDALTHLPNRTLFQDRLHTALQQAERNGQWV 1010
Cdd:COG5001 204 RLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1011 VLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLLPSQGDREialkRAIQVAELILGRLA 1090
Cdd:COG5001 284 ALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPE----DAEAVAERILAALA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1091 RPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKNNFQFYQAEMNARALERLELESDLRRALELGEF 1170
Cdd:COG5001 360 EPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGEL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1171 VLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQLRSWHKAKVRVPKVSVNLS 1250
Cdd:COG5001 440 ELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLS 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1251 ARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYSSLNYLKQFPIDVL 1330
Cdd:COG5001 520 ARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTL 599
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599797 1331 KIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPAEQFGMLYAS 1406
Cdd:COG5001 600 KIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
838-1406 |
6.72e-136 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 433.34 E-value: 6.72e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 838 IARDISQqrraerELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLAS 917
Cdd:PRK10060 102 VARDLSH------GLSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 918 LQHSG-SWEGEILQKRKTGE---LYPS-WVGITAVRDEegdlVSFVCFFSDISERKASERRIHRLAYYDALTHLPNRTLF 992
Cdd:PRK10060 176 FFRSGnAYEVERWIKTRKGQrlfLFRNkFVHSGSGKNE----IFLICSGTDITEERRAQERLRILANTDSITGLPNRNAI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 993 QDRLHTALQQAERNGqwVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFtLLLPSQGDRE 1072
Cdd:PRK10060 252 QELIDHAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF-LVLASHTSQA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1073 iALKRaiqVAELILGRLARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKNNFQFYQAEMNARAL 1152
Cdd:PRK10060 329 -ALEA---MASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVF 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1153 ERLELESDLRRALELGEFVLHYQPQFTGDGrRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQL 1232
Cdd:PRK10060 405 EYLWLDTNLRKALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1233 RSWHKAKVRVpKVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVDDF 1312
Cdd:PRK10060 484 AKWRDKGINL-RVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDF 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1313 GTGYSSLNYLKQFPIDVLKIDRSFVDGLpHGEQDAQ-IARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLF 1391
Cdd:PRK10060 563 GTGYSSLSQLARFPIDAIKLDQSFVRDI-HKQPVSQsLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLF 641
|
570
....*....|....*
gi 15599797 1392 GRPMPAEQFGMLYAS 1406
Cdd:PRK10060 642 AKPMPAVAFERWYKR 656
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
831-1400 |
6.07e-119 |
|
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: 384.52 E-value: 6.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 831 RFEGLLGIARDISQQRRAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQ 910
Cdd:COG2200 8 LRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 911 LKHVLASLQHSGSWEGEILQKRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHRLAYYDALTHLPNRT 990
Cdd:COG2200 88 LLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 991 LFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLLPSQGD 1070
Cdd:COG2200 168 LLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1071 REIALKRAIQVAELilgrLARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKNNFQFYQAEMnAR 1150
Cdd:COG2200 248 AAAAAAALRLLLLL----LLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE-AR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1151 ALERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACK 1230
Cdd:COG2200 323 ARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1231 QLRSWHKAKVRVPkVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVD 1310
Cdd:COG2200 403 QLARWPERGLDLR-LSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1311 DFGTGYSSLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYL 1390
Cdd:COG2200 482 DFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYL 561
|
570
....*....|
gi 15599797 1391 FGRPMPAEQF 1400
Cdd:COG2200 562 FGRPLPLEEL 571
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1159-1399 |
7.95e-112 |
|
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: 351.85 E-value: 7.95e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1159 SDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQLRSWHKA 1238
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1239 KvRVPKVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYSS 1318
Cdd:cd01948 81 G-PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1319 LNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPAE 1398
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 15599797 1399 Q 1399
Cdd:cd01948 240 E 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
836-1398 |
2.57e-110 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 367.94 E-value: 2.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 836 LGIARDISQQRRAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQP-RLLTADRQEANQLKHV 914
Cdd:PRK11359 119 LALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPdTLLNIPEFPADNRIRL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 915 LASLQHSGSWEGEILQKRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISE---------------------------- 966
Cdd:PRK11359 199 QQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEerqirqlegnilaamcssppfhemgeii 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 --------------------------------------------------------------------------------
Cdd:PRK11359 279 crniesvlneshvslfalrngmpihwassshgaeyqnaqswsatirqrdgapagtlqiktssgaetsafiervadisqhl 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 967 ------RKASERRIHRLAYYDALTHLPNRTLFQDRLHTALQqaerNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVA 1040
Cdd:PRK11359 359 aalaleQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVD----KAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVV 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1041 TRLSACVSQDDTVARMGGDEFTLLLPsqgdrEIALKRAIQVAELILGRLARPFTLEGREFFVTASIGValSPQDGAELSL 1120
Cdd:PRK11359 435 NRFREKLKPDQYLCRIEGTQFVLVSL-----ENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGI--SYDVGKNRDY 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1121 LMKNADTAMYHAKEMGKNNFQFYQAEMNARALERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRG 1200
Cdd:PRK11359 508 LLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHG 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1201 LVPPSEFIPVLEEIGLVAQVGDWLLAEACKQLRSWHKAKVRVPKVSVNLSARQFADGQLGERIAAILYETGIPPACLELE 1280
Cdd:PRK11359 588 HVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVE 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1281 LTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYSSLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSL 1360
Cdd:PRK11359 668 ITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSL 747
|
650 660 670
....*....|....*....|....*....|....*...
gi 15599797 1361 NLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPAE 1398
Cdd:PRK11359 748 NLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
1158-1399 |
7.89e-102 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 324.56 E-value: 7.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1158 ESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQLRSWHK 1237
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1238 AKVRVPKVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYS 1317
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1318 SLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPA 1397
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 15599797 1398 EQ 1399
Cdd:smart00052 241 DD 242
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
611-1400 |
2.10e-87 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 309.68 E-value: 2.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 611 NHHLGQQLGYNQEELARMGenfWETLLHPDDQEY-YWRIRNLQHvvGDGLLLDSQLRWRHRDGRWHWFDIreqAFS--RD 687
Cdd:PRK09776 309 NKALCQFLGYSQEELRGLT---FQQLTWPEDLNKdLQQVEKLLS--GEINSYSMEKRYYRRDGEVVWALL---AVSlvRD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 688 RSGRVARLIGVAKDITFTVEANNALRENGRRYRMLAE---------NISDVIFSTDAELNASYVSPsvqhvFGYSPEWAL 758
Cdd:PRK09776 381 TDGTPLYFIAQIEDINELKRTEQVNERLMERITLANEaggigiwewDLKPNIISWDKRMFELYEIP-----PHIKPTWQV 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 759 LnglhQTATNPRQLGRLNGLLRRvrhAIGDRQKL-AELRenpgqhlfaldCLRADG-RKIPIELRIVLmwDEHDRFEGLL 836
Cdd:PRK09776 456 W----YACLHPEDRQRVEKEIRD---ALQGRSPFkLEFR-----------IVVKDGvRHIRALANRVL--NKDGEVERLL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 837 GIARDISQQRRAEREL-----RMAATVFEHSTAAImVTDPAGYIVQVNDSFSRLTGYSPADVLDqQPRLLT---ADRQEA 908
Cdd:PRK09776 516 GINMDMTEVRQLNEALfqekeRLHITLDSIGEAVV-CTDMAMKVTFMNPVAEKMTGWTQEEALG-VPLLTVlhiTFGDNG 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 909 NQLKHVLASLQHSGSW---EGEILQKRkTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHRLAYYDALTH 985
Cdd:PRK09776 594 PLMENIYSCLTSRSAAyleQDVVLHCR-SGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTH 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 986 LPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLL 1065
Cdd:PRK09776 673 LANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLL 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1066 PsqgdrEIALKRAIQVAELILGRL-ARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKNNFQFYQ 1144
Cdd:PRK09776 753 P-----DCNVESARFIATRIISAInDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYE 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1145 AEMNA--RALERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGD 1222
Cdd:PRK09776 828 PQQAAahSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDR 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1223 WLLAEACKQlrswHKAKVRVPKVSV--NLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGL 1300
Cdd:PRK09776 908 RVIHEFFRQ----AAKAVASKGLSIalPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKL 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1301 KRLGLAIAVDDFGTGYSSLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLRE 1380
Cdd:PRK09776 984 RLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSG 1063
|
810 820
....*....|....*....|
gi 15599797 1381 HGCDEVQGYLFGRPMPAEQF 1400
Cdd:PRK09776 1064 IGVDLAYGYAIARPQPLDLL 1083
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
976-1400 |
2.67e-86 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 295.85 E-value: 2.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 976 RLAYYDALTHLPNRTLFQdrlhTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVAR 1055
Cdd:PRK13561 229 RNATRFPVSDLPNKALLM----ALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1056 MGGDEFTLLLPSQGDREialkRAIQVAELILGRLARPFTLEGREFFVTASIGVALSPQD-GAELslLMKNADTAMYHAKE 1134
Cdd:PRK13561 305 ISGYDFAIIANGVKEPW----HAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDlTAEQ--LYSRAISAAFTARR 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1135 MGKNNFQFYQAEMNARALERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEI 1214
Cdd:PRK13561 379 KGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESC 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1215 GLVAQVGDWLLAEACKQLRSWHKAKVRVPkVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAM 1294
Cdd:PRK13561 459 GLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAV 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1295 QILSGLKRLGLAIAVDDFGTGYSSLNYLKQF---PIDVLKIDRSFVDGLPhgeQDAQIARAIIAMAHSLNLMVIAEGVES 1371
Cdd:PRK13561 538 AILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLP---EDDSMVAAIIMLAQSLNLQVIAEGVET 614
|
410 420
....*....|....*....|....*....
gi 15599797 1372 QAQLDFLREHGCDEVQGYLFGRPMPAEQF 1400
Cdd:PRK13561 615 EAQRDWLLKAGVGIAQGFLFARALPIEIF 643
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1158-1394 |
7.37e-82 |
|
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: 268.42 E-value: 7.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1158 ESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQLRSWHK 1237
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1238 AkvRVPKVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYS 1317
Cdd:pfam00563 81 G--PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599797 1318 SLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRP 1394
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1153-1405 |
1.20e-81 |
|
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: 278.72 E-value: 1.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1153 ERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQL 1232
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1233 RSWHKAKVRVpKVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMsDVAEAMQILSGLKRLGLAIAVDDF 1312
Cdd:COG4943 348 GDLLAADPDF-HISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDF 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1313 GTGYSSLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFG 1392
Cdd:COG4943 426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
|
250
....*....|...
gi 15599797 1393 RPMPAEQFGMLYA 1405
Cdd:COG4943 506 KPLPAEEFIAWLA 518
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
976-1406 |
1.90e-80 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 279.52 E-value: 1.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 976 RLAYYDALTHLPNRTLFQDRLHTALQ-QAERNGQWVvlMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVA 1054
Cdd:PRK11829 230 RISHRFPVTELPNRSLFISLLEKEIAsSTRTDHFHL--LVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1055 RMGGDEFTLLLpsqgdREIALKR-AIQVAELILGRLARPFTLEGREFFVTASIGVAL--SPQDGAELslLMKNADTAMYH 1131
Cdd:PRK11829 308 QLSKTEFAVLA-----RGTRRSFpAMQLARRIMSQVTQPLFFDEITLRPSASIGITRyqAQQDTAES--MMRNASTAMMA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1132 AKEMGKNNFQFYQAEMNARALERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVL 1211
Cdd:PRK11829 381 AHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1212 EEIGLVAQVGDWLLAEACKQLRSWHKAKVRVPkVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVA 1291
Cdd:PRK11829 461 EEEGMMVPLGNWVLEEACRILADWKARGVSLP-LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLD 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1292 EAMQILSGLKRLGLAIAVDDFGTGYSSLNYL---KQFPIDVLKIDRSFVDGLPhgeQDAQIARAIIAMAHSLNLMVIAEG 1368
Cdd:PRK11829 540 EALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEG 616
|
410 420 430
....*....|....*....|....*....|....*...
gi 15599797 1369 VESQAQLDFLREHGCDEVQGYLFGRPMPAEQFGMLYAS 1406
Cdd:PRK11829 617 VETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEAQYFS 654
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
940-1143 |
4.48e-62 |
|
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: 213.69 E-value: 4.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 940 SWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHRLAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDR 1019
Cdd:COG2199 76 LLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1020 FKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLLPsqgdrEIALKRAIQVAELILGRLAR-PFTLEGR 1098
Cdd:COG2199 156 FKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLP-----GTDLEEAEALAERLREALEQlPFELEGK 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599797 1099 EFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKNNFQFY 1143
Cdd:COG2199 231 ELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
979-1141 |
8.14e-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: 208.18 E-value: 8.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 979 YYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGG 1058
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1059 DEFTLLLPsqgdrEIALKRAIQVAELILGRLARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKN 1138
Cdd:cd01949 81 DEFAILLP-----GTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
...
gi 15599797 1139 NFQ 1141
Cdd:cd01949 156 RVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
976-1143 |
3.51e-59 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 200.55 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 976 RLAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVAR 1055
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1056 MGGDEFTLLLPsqgdrEIALKRAIQVAELILGRLARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEM 1135
Cdd:smart00267 81 LGGDEFALLLP-----ETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
|
....*...
gi 15599797 1136 GKNNFQFY 1143
Cdd:smart00267 156 GRNQVAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
978-1139 |
2.52e-58 |
|
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: 198.25 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 978 AYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMG 1057
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1058 GDEFTLLLPsqgdrEIALKRAIQVAELI---LGRLARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKE 1134
Cdd:pfam00990 81 GDEFAILLP-----ETSLEGAQELAERIrrlLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155
|
....*
gi 15599797 1135 MGKNN 1139
Cdd:pfam00990 156 AGRNR 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
1154-1400 |
2.45e-40 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 157.46 E-value: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1154 RLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLL---AEACK 1230
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFeliARDAA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1231 QLRswhkaKVrVP---KVSVNLSARQFADGQLGERIAAILyeTGIPPACLE--LELTESILMSDvAEAMQILSGLKRLGL 1305
Cdd:PRK10551 341 ELQ-----KV-LPvgaKLGINISPAHLHSDSFKADVQRLL--ASLPADHFQivLEITERDMVQE-EEATKLFAWLHSQGI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1306 AIAVDDFGTGYSSLNYLKQFPIDVLKIDRSFVDGLphGEQD--AQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGC 1383
Cdd:PRK10551 412 EIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAI--GTETvtSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGV 489
|
250
....*....|....*..
gi 15599797 1384 DEVQGYLFGRPMPAEQF 1400
Cdd:PRK10551 490 NFLQGYWISRPLPLEDF 506
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
977-1138 |
3.45e-39 |
|
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: 143.63 E-value: 3.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 977 LAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARM 1056
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1057 GGDEFTLLLPsQGDREIALKRAIQVAELIlgrLARPFTLEGRE-FFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEM 1135
Cdd:TIGR00254 81 GGEEFVVILP-GTPLEDALSKAERLRDAI---NSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
...
gi 15599797 1136 GKN 1138
Cdd:TIGR00254 157 GRN 159
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
707-974 |
6.75e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 134.77 E-value: 6.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 707 EANNALRENGRRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEWALlnglhqtatnprqlGRLNGLLRRVRHAI 786
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELL--------------GKTLRDLLPPEDDD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 787 GDRQKLAELRENPGQHLFALDCLRADGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQRRAERELR----MAATVFEHS 862
Cdd:COG2202 67 EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALReseeRLRLLVENA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 863 TAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADrQEANQLKHVLASLQHSGSWEGEILQKRKTGELYPSWV 942
Cdd:COG2202 147 PDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHP-EDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWV 225
|
250 260 270
....*....|....*....|....*....|...
gi 15599797 943 GITAVRDEEGDLV-SFVCFFSDISERKASERRI 974
Cdd:COG2202 226 EASAVPLRDGGEViGVLGIVRDITERKRAEEAL 258
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
977-1138 |
3.53e-32 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 131.95 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 977 LAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARM 1056
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1057 GGDEFTLLLPsqgdrEIALKRAIQVAELILGRLA-RPFTLEG--REFFVTASIGVALSPQDGAELSLLMKNADTAMYHAK 1133
Cdd:PRK09581 371 GGEEFVVVMP-----DTDIEDAIAVAERIRRKIAeEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAK 445
|
....*
gi 15599797 1134 EMGKN 1138
Cdd:PRK09581 446 NTGRN 450
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
574-852 |
3.80e-30 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 120.90 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 574 EVELSLIEREKFWSDAVQAVPDTLYIHDLHaRRVIFSNHHLGQQLGYNQEELarMGENFWETLLHPDDQEYYwriRNLQH 653
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLD-GRILYVNPAFERLTGYSAEEL--LGKTLRDLLPPEDDDEFL---ELLRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 654 VVGDGLLLDSQLRWRHRDGRWHWFDIREQAFsRDRSGRVARLIGVAKDITFTVEANNALRENGRRYRMLAENISDVIFST 733
Cdd:COG2202 75 ALAGGGVWRGELRNRRKDGSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 734 DAELNASYVSPSVQHVFGYSPEwALLNGLHQTATNPRQLGRLNGLLRRVrhaigdrqklaeLRENPGQHLFALDCLRADG 813
Cdd:COG2202 154 DLDGRILYVNPAAEELLGYSPE-ELLGKSLLDLLHPEDRERLLELLRRL------------LEGGRESYELELRLKDGDG 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 15599797 814 RKIPIELRIVLMWDEhDRFEGLLGIARDISQQRRAEREL 852
Cdd:COG2202 221 RWVWVEASAVPLRDG-GEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
956-1138 |
5.28e-26 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 109.77 E-value: 5.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 956 SFVCFFSDISERKASERRIHR-----LAYYDALTHLPNRTLFQDRLHTALQQaeRNGQWVVLMFLDLDRFKPINDSLGHA 1030
Cdd:PRK09894 102 HFDAFQEGLLSFTAALTDYKIylltiRSNMDVLTGLPGRRVLDESFDHQLRN--REPQNLYLALLDIDRFKLVNDTYGHL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1031 AGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLLPSQGDREialkrAIQVAELILGRLAR-PFTLEGREFFVTASIGVA 1109
Cdd:PRK09894 180 IGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEE-----ACRAGERIRQLIANhAITHSDGRINITATFGVS 254
|
170 180
....*....|....*....|....*....
gi 15599797 1110 LSPQdGAELSLLMKNADTAMYHAKEMGKN 1138
Cdd:PRK09894 255 RAFP-EETLDVVIGRADRAMYEGKQTGRN 282
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
844-1062 |
5.49e-26 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 108.96 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 844 QQRRAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLASLQHSGS 923
Cdd:COG2202 2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 924 WEGEILQKRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHRL-AYYDALTHLPNRTLFQDRLHTALQQ 1002
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESeERLRLLVENAPDGIFVLDLDGRILY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599797 1003 AerNGQWVVLMFLDLDRF--KPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFT 1062
Cdd:COG2202 162 V--NPAAEELLGYSPEELlgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGR 221
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
977-1138 |
1.37e-25 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 113.57 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 977 LAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARM 1056
Cdd:PRK15426 397 QAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1057 GGDEFTLLLPSQGdreiaLKRAIQVAELILGRLARPFTLE--GREFFVTASIGVALSPQDGA-ELSLLMKNADTAMYHAK 1133
Cdd:PRK15426 477 GGEEFCVVLPGAS-----LAEAAQVAERIRLRINEKEILVakSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLAK 551
|
....*
gi 15599797 1134 EMGKN 1138
Cdd:PRK15426 552 QAGRN 556
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
571-858 |
5.30e-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: 101.59 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 571 SRKEVELSLIEREKFWSDAVQAVPDTLYIHDLHARrVIFSNHHLGQQLGYNQEELarMGENFWEtLLHPDDQEYYWRIRN 650
Cdd:COG5809 2 KSSKMELQLRKSEQRFRSLFENAPDAILILDLEGK-ILKVNPAAERIFGYTEDEL--LGTNILD-FLHPDDEKELREILK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 651 LQHvvGDGLLLDSQLRWRHRDGRWHWFDIREQAFsRDRSGRVARLIGVAKDITFTVEANNALRENGRRYRMLAENISDVI 730
Cdd:COG5809 78 LLK--EGESRDELEFELRHKNGKRLEFSSKLSPI-FDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 731 FSTDAELNASYVSPSVQHVFGYSPEwALLNGLHQTATNPRQLGRLNGLLRRVRHAIGDRQklAELRenpgqhlfaldCLR 810
Cdd:COG5809 155 IVTDLDGRIIYANPAACKLLGISIE-ELIGKSILELIHSDDQENVAAFISQLLKDGGIAQ--GEVR-----------FWT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599797 811 ADGRKIPIELRIVLMwDEHDRFEGLLGIARDISQQRRAERELR----------MAATV 858
Cdd:COG5809 221 KDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELLRkseklsvvgeLAAGI 277
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
711-974 |
1.03e-20 |
|
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: 97.35 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 711 ALRENGRRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEwALLNglhqtaTNPRQLgrlngLLRRVRHAIGDRQ 790
Cdd:COG5809 9 QLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTED-ELLG------TNILDF-----LHPDDEKELREIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 791 KLAELRENPGQHLFALDCLraDGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQRRAERELRMAA----TVFEHSTAAI 866
Cdd:COG5809 77 KLLKEGESRDELEFELRHK--NGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEekfrLIFNHSPDGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 867 MVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLASLQHSGSWEGEILQKRKTGELYpsWVGITA 946
Cdd:COG5809 155 IVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWR--LLEASG 232
|
250 260
....*....|....*....|....*....
gi 15599797 947 VR-DEEGDLVSFVCFFSDISERKASERRI 974
Cdd:COG5809 233 APiKKNGEVDGIVIIFRDITERKKLEELL 261
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
978-1397 |
1.03e-20 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 98.40 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 978 AYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACV-SQDDTV-AR 1055
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPGALlAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1056 MGGDEFTLLLPSQGdreiaLKRAIQVA-ELILGRLARPFT-LEGREFFVtaSIGVALSpQDGAELSLLMKNADTAMYHAK 1133
Cdd:PRK11059 308 YSRSDFAVLLPHRS-----LKEADSLAsQLLKAVDALPPPkMLDRDDFL--HIGICAY-RSGQSTEQVMEEAEMALRSAQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1134 EMGKNNFQFY---QAEMNARALERleLESDLRRALELGEFVLHYQPQFTGDGRRLTgAEALLRWQHPRRGLVPPSEFIPV 1210
Cdd:PRK11059 380 LQGGNGWFVYdkaQLPEKGRGSVR--WRTLLEQTLVRGGPRLYQQPAVTRDGKVHH-RELFCRIRDGQGELLSAELFMPM 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1211 LEEIGLVAQVGDWLLAEACKQLRSWHKAkvrvpKVSVNLSA---------RQFADgqlgeriaaILYETGIPPA-CLELE 1280
Cdd:PRK11059 457 VQQLGLSEQYDRQVIERVLPLLRYWPEE-----NLSINLSVdsllsrafqRWLRD---------TLLQCPRSQRkRLIFE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1281 LTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYSSLNYLKQFPIDVLKIDRSFVDGLpHGEQDAQIA-RAIIAMAHS 1359
Cdd:PRK11059 523 LAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNI-HKRTENQLFvRSLVGACAG 601
|
410 420 430
....*....|....*....|....*....|....*...
gi 15599797 1360 LNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPA 1397
Cdd:PRK11059 602 TETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
816-1133 |
2.75e-18 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 88.91 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 816 IPIELRIVLMWDehdrfegLLGIARDISQQRRAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLD 895
Cdd:PRK09966 23 TSIFITMMLIWL-------LLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQFSTAEVRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 896 QQPRLLTADRQEANQ--------LKH------VLASLQHSGSWEGEI-LQKRK--------------TGE-LYPSWVGIT 945
Cdd:PRK09966 96 KQQNILASWHYTRKDpgdtfsnfISHwlfpapIIQPIRHNGETIGEVrLTARDssishfiwfslavlTGCiLLASGIAIT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 946 AVRDEEGDLVSFVCFFSDISE---------RKASERRIH-------------------------------RLAYYDALTH 985
Cdd:PRK09966 176 LTRHLHNGLVEALKNITDVVHdvrsnrnfsRRVSEERIAefhrfaldfnslldemeewqlrlqaknaqllRTALHDPLTG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 986 LPNRTLFQDRLhTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLL 1065
Cdd:PRK09966 256 LANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1066 PS-QGDREIAlkraiQVAELILGRLARPFTLE-GREFFVTASIGVALSpQDGAELSLLMKNADTAMYHAK 1133
Cdd:PRK09966 335 YDvQSESEVQ-----QICSALTQIFNLPFDLHnGHQTTMTLSIGYAMT-IEHASAEKLQELADHNMYQAK 398
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
873-966 |
4.11e-17 |
|
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: 77.89 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 873 GYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLASLQHsgSWEGEILQKRKTGELYPSWVGITAVRDEEG 952
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKA--VREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 15599797 953 DLVSFVCFFSDISE 966
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
480-712 |
1.37e-16 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 81.22 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 480 RITEINDVSRRLLQIDSTEQAWQRLLDHGPLQPDSLRLQVIEALIERRPVLELEATLRCGKSTPRHLWLQLRLPENP-GE 558
Cdd:COG2202 32 RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEdGE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 559 WHAVTLSLSDVTSRKEVELSLIEREKFWSDAVQAVPDTLYIHDLHArRVIFSNHHLGQQLGYNQEELarMGENFWETLLH 638
Cdd:COG2202 112 ITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDG-RILYVNPAAEELLGYSPEEL--LGKSLLDLLHP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599797 639 PDDQEYYWRIRNLQhvvgDGLLLDSQLRWRHRDGRWHWFDIREQAFSRDRSGRVARLIGVAKDITFTVEANNAL 712
Cdd:COG2202 189 EDRERLLELLRRLL----EGGRESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
847-986 |
5.45e-15 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 78.35 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 847 RAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPR-LLTADRQEANQLKHVLASlqHSGSWE 925
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAeLFPEDSPLRELLERALAE--GQPVTE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599797 926 GEILQKRKTGELYPSWVGITAVRDEEGDlVSFVCFFSDISERKASERRIHRLAYYDALTHL 986
Cdd:COG3852 79 REVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
607-699 |
3.00e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 69.29 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 607 VIFSNHHLGQQLGYNQEELARMGEnFWETLLHPDDQEYYWRirNLQHVVGDGLLLDSQLRWRHRDGRWHWFDIREQAFsR 686
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGE-SWLDLVHPDDRERVRE--ALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPI-R 76
|
90
....*....|...
gi 15599797 687 DRSGRVARLIGVA 699
Cdd:pfam08447 77 DENGKPVRVIGVA 89
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
581-974 |
1.47e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 75.86 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 581 EREKFWSDAVQAVPDTLYIHDLHARRViFSNHHLGQQLGynqeELARMGE-------NFWETLLHPDDQEYYW-RIRNLQ 652
Cdd:PRK13560 65 CREQCERNLKANIPGGMFLFALDGDGT-FSFPSLLDANG----ELAAIAKhdlmadkGLLAMLIGGDDGDFFFaNPFRSA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 653 HVVGDGLLLDS----QLRWRHRDGRWHWFDIReqaFSRDRSGRVaRLIGVAKDITFTVEANNALRENGRRYRMLAENISD 728
Cdd:PRK13560 140 ETIAMALQSDDwqeeEGHFRCGDGRFIDCCLR---FERHAHADD-QVDGFAEDITERKRAEERIDEALHFLQQLLDNIAD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 729 VIFSTDAELNASYVSPSVQHVFGYSPEWALLNGLHQTATNPRqlgrlngllrrvrhaIGDRQKL-AELRENPGQHLFALD 807
Cdd:PRK13560 216 PAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQP---------------ADDYQEAdAAKFDADGSQIIEAE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 808 CLRADGRKIPIELRI--VLMWDEHDRFEGLLGIARDISQQRRAERELR----MAATVFEHSTAAIMVTDPAGYIVQV-ND 880
Cdd:PRK13560 281 FQNKDGRTRPVDVIFnhAEFDDKENHCAGLVGAITDISGRRAAERELLekedMLRAIIEAAPIAAIGLDADGNICFVnNN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 881 SFSRLTGYSPADVL---------DQQPRLLTADRQE--------ANQLKHVLASLQHSGSWEG-EILQKRKTGE-----L 937
Cdd:PRK13560 361 AAERMLGWSAAEVMgkplpgmdpELNEEFWCGDFQEwypdgrpmAFDACPMAKTIKGGKIFDGqEVLIEREDDGpadcsA 440
|
410 420 430
....*....|....*....|....*....|....*..
gi 15599797 938 YPSwvgitAVRDEEGDLVSFVCFFSDISERKASERRI 974
Cdd:PRK13560 441 YAE-----PLHDADGNIIGAIALLVDITERKQVEEQL 472
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
695-978 |
2.85e-13 |
|
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: 74.00 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 695 LIGVAKDITFTVEANNALR---ENGRRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEWALLNglhqtatnprq 771
Cdd:COG5805 9 IHEVKKDGTPIWINNEVLRmaiEITEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGK----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 772 lgRLNGLLRRVRHAIGDRQKlaELRENPGQHLFALDCLRADGRKIPIELRIVLMWDEHDRFEglLGIARDISQQRRAERE 851
Cdd:COG5805 78 --TIFDFLEKEYHYRVKTRI--ERLQKGYDVVMIEQIYCKDGELIYVEVKLFPIYNQNGQAA--ILALRDITKKKKIEEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 852 LR----MAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQ-PRLLTADrqEANQLKHVLASLQHSGSwEG 926
Cdd:COG5805 152 LQeqeeRLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNlLELLHPC--DKEEFKERIESITEVWQ-EF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599797 927 EILQKRKTGELYPSW--VGITAVRDEEGDLVSFVCFFSDISERKASE---RRIHRLA 978
Cdd:COG5805 229 IIEREIITKDGRIRYfeAVIVPLIDTDGSVKGILVILRDITEKKEAEelmARSEKLS 285
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
857-974 |
3.81e-13 |
|
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: 67.70 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 857 TVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTA--DRQEANQLKHVLASLQHSGSWEGEILQkRKT 934
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPeeDREEVRERIERRLEGEPEPVSEERRVR-RKD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15599797 935 GELYPSWVGITAVRdEEGDLVSFVCFFSDISERKASERRI 974
Cdd:TIGR00229 86 GSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
285-579 |
4.71e-13 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 70.82 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 285 LASQRSLRQAATALAAIDERVLVTRADGRLSYLNPQAERLFGISSAQARQHHLLGLLPDLEPG-----WLTDAGGDGETR 359
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDeflelLRAALAGGGVWR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 360 SELLPLRVRGEPRTFTLSRHPLasypaladqawtLREQILQGGQVWVLRDVTEEQHALGVLEETRRRYQDIFEGVGVALC 439
Cdd:COG2202 84 GELRNRRKDGSLFWVELSISPV------------RDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 440 VLDLSAlrqalveqgldscaalrawlagepgrqqalleriRITEINDVSRRLLQIDSTEQAWQRLLDHGPLQPDSLRLQV 519
Cdd:COG2202 152 VLDLDG----------------------------------RILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599797 520 IEALIER-RPVLELEATLRCGKSTPRHLWLQLRLPENPGEWHAVTLSLSDVTSRKEVELSL 579
Cdd:COG2202 198 LRRLLEGgRESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
518-974 |
5.92e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 73.94 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 518 QVIEALIERRPVLELEATLRCGK-------STPRhlwlqlRLPENPGEWHAVTLslsDVTSRKEVELSLIEREKFWSDAV 590
Cdd:PRK13560 140 ETIAMALQSDDWQEEEGHFRCGDgrfidccLRFE------RHAHADDQVDGFAE---DITERKRAEERIDEALHFLQQLL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 591 QAVPDTLYIHDLHARrVIFSNHHLGQQLGYNQEELARMGenfwetlLHPDDQEYywRIRNLQHVvgDGLLLDS------Q 664
Cdd:PRK13560 211 DNIADPAFWKDEDAK-VFGCNDAACLACGFRREEIIGMS-------IHDFAPAQ--PADDYQEA--DAAKFDAdgsqiiE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 665 LRWRHRDGRWHWFDIR-EQAFSRDRSGRVARLIGVAKDITFTVEANNALRENGRRYRMLAENISDVIFSTDAELNASYV- 742
Cdd:PRK13560 279 AEFQNKDGRTRPVDVIfNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIAAIGLDADGNICFVn 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 743 SPSVQHVFGYSPEWAL---LNGLHQTATNPRQLGRLNGLLRRVRHAIGDRQKLAELRENpGQHLFALDCL--RADGRKIP 817
Cdd:PRK13560 359 NNAAERMLGWSAAEVMgkpLPGMDPELNEEFWCGDFQEWYPDGRPMAFDACPMAKTIKG-GKIFDGQEVLieREDDGPAD 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 818 IELRIVLMWDEHDRFEGLLGIARDISQQRRAERELRMAATVFEHSTAAIM--VTDPAGYIVQVNDSFSRLtGYSPADVLD 895
Cdd:PRK13560 438 CSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLANLIVENSPLVLFrwKAEEGWPVELVSKNITQF-GYEPDEFIS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 896 QQPRLLT----ADRQEANQLKHVLASlQHSGSWEGEILQKRKTGELypSWVG--ITAVRDEEGDLVSFVCFFSDISERKA 969
Cdd:PRK13560 517 GKRMFAAiihpADLEQVAAEVAEFAA-QGVDRFEQEYRILGKGGAV--CWIDdqSAAERDEEGQISHFEGIVIDISERKH 593
|
....*
gi 15599797 970 SERRI 974
Cdd:PRK13560 594 AEEKI 598
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
839-976 |
7.34e-13 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 73.33 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 839 ARDISQQRRAERELRMAATVFEHSTAAIMVTDPAGY---IVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVL 915
Cdd:PRK13558 134 ARMPISDLTVESDRRLKERALDEAPVGITIADATLPdepLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELR 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599797 916 ASLQHSGSWEGEILQKRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHR 976
Cdd:PRK13558 214 EAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQR 274
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
971-1138 |
4.55e-12 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 69.47 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 971 ERRIHRLAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQD 1050
Cdd:PRK10245 198 KRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1051 DTVARMGGDEFTLLLpSQGDREIALKRAIQVAELiLGRLARPFTLEGReffVTASIGVA-LSPQDGAELSLLmKNADTAM 1129
Cdd:PRK10245 278 DVIGRFGGDEFAVIM-SGTPAESAITAMSRVHEG-LNTLRLPNAPQVT---LRISVGVApLNPQMSHYREWL-KSADLAL 351
|
....*....
gi 15599797 1130 YHAKEMGKN 1138
Cdd:PRK10245 352 YKAKNAGRN 360
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
560-858 |
1.39e-11 |
|
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: 68.60 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 560 HAVTLSLSDVTSRKEVELSLIEREKFWSDAVQAVPDTLYIHDLHARrVIFSNHHLGQQLGYNQEEL-ARMGENFWETLLH 638
Cdd:COG5805 10 HEVKKDGTPIWINNEVLRMAIEITEELETILENLPDAIIAVNREGK-VIYINPAMEKLLGYTSEEIiGKTIFDFLEKEYH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 639 PDDQEYYWRIRNLQHVVGdgllldsQLRWRHRDGRWHWFDIReQAFSRDRSGRVArlIGVAKDITFTVEANNALRENGRR 718
Cdd:COG5805 89 YRVKTRIERLQKGYDVVM-------IEQIYCKDGELIYVEVK-LFPIYNQNGQAA--ILALRDITKKKKIEEILQEQEER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 719 YRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEWALLNGLHQTATNPRQLgrlngllrRVRHAIgdrQKLAELREN 798
Cdd:COG5805 159 LQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKE--------EFKERI---ESITEVWQE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 799 PGQHLFALDclrADGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQRRAERELR----------MAATV 858
Cdd:COG5805 228 FIIEREIIT---KDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMArseklsiagqLAAGI 294
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
1279-1399 |
8.18e-11 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 65.98 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1279 LELTESILMSDvaEAMQILSGLKRLGLAIAVDDFGTGYSSLNYLKQfpIDVLKIDrsfVDGLPHGEqdaqiARAIIAMAH 1358
Cdd:COG3434 88 LEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID---VLALDLEE-----LAELVARLK 155
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15599797 1359 SLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPAEQ 1399
Cdd:COG3434 156 RYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
711-856 |
1.17e-10 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 64.87 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 711 ALRENGRRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEWALLNGLHQTatnPRQLGRLNGLLRRVrhaigdrq 790
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAEL---FPEDSPLRELLERA-------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599797 791 klaeLRENPGQHLFALDCLRADGRKIPIELRIVLMwDEHDRFEGLLGIARDISQQRRAERELRMAA 856
Cdd:COG3852 70 ----LAEGQPVTEREVTLRRKDGEERPVDVSVSPL-RDAEGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
844-975 |
1.21e-10 |
|
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: 65.77 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 844 QQRRAERELRmaaTVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEAnQLKHVLASLQHSGS 923
Cdd:COG5809 9 QLRKSEQRFR---SLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK-ELREILKLLKEGES 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15599797 924 WEGEILQKR-KTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIH 975
Cdd:COG5809 85 RDELEFELRhKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALR 137
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
288-428 |
9.40e-10 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 62.17 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 288 QRSLRQAATALAAIDERVLVTRADGRLSYLNPQAERLFGISSAQARQHHLLGLLPDLEP--GWLTDA--GGDGETRSELL 363
Cdd:COG3852 3 RESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPlrELLERAlaEGQPVTEREVT 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599797 364 PLRVRGEPRTFTLSRHPlasypaladqawtLREQILQGGQVWVLRDVTEEQHalgvLEETRRRYQ 428
Cdd:COG3852 83 LRRKDGEERPVDVSVSP-------------LRDAEGEGGVLLVLRDITERKR----LERELRRAE 130
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
1021-1133 |
2.01e-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: 58.38 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1021 KPINDslghaagdrmlQEVATRLsacvsqdDTVARMGGDEFTLLLPsqgdrEIALKRAIQVAELILGRLARPftlegREF 1100
Cdd:COG3706 104 KPFDP-----------EELLARV-------DLVARYGGEEFAILLP-----GTDLEGALAVAERIREAVAEL-----PSL 155
|
90 100 110
....*....|....*....|....*....|...
gi 15599797 1101 FVTASIGVALSPqdgaelslLMKNADtAMYHAK 1133
Cdd:COG3706 156 RVTVSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
1010-1109 |
3.15e-09 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 56.60 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1010 VVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQD-DTVARMGGDEFTLLLPSQgdreiALKRAIQVAELILGR 1088
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLD-----HPAAAVAFAEDMREA 76
|
90 100
....*....|....*....|.
gi 15599797 1089 LARpfTLEGREFFVTASIGVA 1109
Cdd:cd07556 77 VSA--LNQSEGNPVRVRIGIH 95
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
857-964 |
3.48e-09 |
|
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: 55.89 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 857 TVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLL---TADRQEANQLKHVLASLQHSGSweGEILQKRK 933
Cdd:pfam00989 5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLipeEDDAEVAELLRQALLQGEESRG--FEVSFRVP 82
|
90 100 110
....*....|....*....|....*....|.
gi 15599797 934 TGELYPSWVGITAVRDEEGDLVSFVCFFSDI 964
Cdd:pfam00989 83 DGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
862-964 |
9.68e-09 |
|
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: 54.18 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 862 STAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLT--ADRQEANQLkhVLASLQHSGSWEGEILQKRKTGELYP 939
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIhpEDREELRER--LENLLSGGEPVTLEVRLRRKDGSVIW 78
|
90 100
....*....|....*....|....*
gi 15599797 940 SWVGITAVRDEEGDLVSFVCFFSDI 964
Cdd:cd00130 79 VLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
582-712 |
1.28e-08 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 54.60 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 582 REKFWSDAVQAVPDTLYIHDLHArRVIFSNHHLGQQLGYNQEELarMGENFWEtLLHPDD----QEYYWRIRNLQHVVgd 657
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEG-NILYVNPAFEEIFGYSAEEL--IGRNVLE-LIPEEDreevRERIERRLEGEPEP-- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599797 658 glllDSQLRW-RHRDGRWHWFDIREQafSRDRSGRVARLIGVAKDITFTVEANNAL 712
Cdd:TIGR00229 75 ----VSEERRvRRKDGSEIWVEVSVS--PIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
717-852 |
2.44e-08 |
|
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: 53.83 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 717 RRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEwallnglhqtatnprqlgRLNGLLRRVRHAIGDRQKLAEL- 795
Cdd:TIGR00229 3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAE------------------ELIGRNVLELIPEEDREEVRERi 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599797 796 ------RENPGQHLFALdcLRADGRKIPIELRIVLMwDEHDRFEGLLGIARDISQQRRAEREL 852
Cdd:TIGR00229 65 errlegEPEPVSEERRV--RRKDGSEIWVEVSVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
594-702 |
9.82e-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: 51.48 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 594 PDTLYIHDLHaRRVIFSNHHLGQQLGYNQEELarMGENFWEtLLHPDDQEYYwrIRNLQHVVGDGLLLDSQLRWRHRDGR 673
Cdd:cd00130 2 PDGVIVLDLD-GRILYANPAAEQLLGYSPEEL--IGKSLLD-LIHPEDREEL--RERLENLLSGGEPVTLEVRLRRKDGS 75
|
90 100
....*....|....*....|....*....
gi 15599797 674 WHWFDIREQAFsRDRSGRVARLIGVAKDI 702
Cdd:cd00130 76 VIWVLVSLTPI-RDEGGEVIGLLGVVRDI 103
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
606-703 |
2.60e-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: 49.77 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 606 RVIFSNHHLGQQLGYNQEELarMGENFWETLLHPDDQEYYWRIRNLQHVVGDGllldsQLRWRHRDGRWHWFDIREQAFs 685
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREEL--LGKSITDLFAEPEDSERLREALREGKAVREF-----EVVLYRKDGEPFPVLVSLAPI- 74
|
90
....*....|....*...
gi 15599797 686 RDRSGRVARLIGVAKDIT 703
Cdd:pfam13426 75 RDDGGELVGIIAILRDIT 92
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
875-960 |
2.32e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 46.95 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 875 IVQVNDSFSRLTGYSPADVLDQQPRLLTA----DRQEAnqLKHVLASLQHSGSWEGEILQKRKTGELYPSWVGITAVRDE 950
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhpdDRERV--REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|
gi 15599797 951 EGDLVSFVCF 960
Cdd:pfam08447 79 NGKPVRVIGV 88
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
280-416 |
8.02e-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: 49.96 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 280 LRAMTLASQRSLRQAATALAAIDERVLVTRADGRLSYLNPQAERLFGISSAQARQHHLLGLLPDLEPGWLTDAGGDGETR 359
Cdd:COG5000 78 LKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQ 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599797 360 SELlpLRVRGEPRTFTLSRHPLasypaladqawtlreqiLQGGQVWVLRDVTEEQHA 416
Cdd:COG5000 158 EEI--ELTRDGRRTLLVRASPL-----------------RDDGYVIVFDDITELLRA 195
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
868-986 |
1.17e-05 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 49.67 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 868 VTDPA---GYIVQVNDSFSRLTGYSPADVLDQQPRLLTA---DRQEANQLKHVLASLQHSGSwegEILQKRKTGELYPSW 941
Cdd:PRK13557 45 VTDPNqpdNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGpetDRATVAEVRDAIAERREIAT---EILNYRKDGSSFWNA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15599797 942 VGITAVRDEEGDLVSFvcFFS--DISERKASERRIHRLAYYDALTHL 986
Cdd:PRK13557 122 LFVSPVYNDAGDLVYF--FGSqlDVSRRRDAEDALRQAQKMEALGQL 166
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
859-978 |
1.41e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 49.05 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 859 FEHSTAAIMVTDPAGY---IVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLASLQHSGSWEGEILQKRKTG 935
Cdd:PRK13559 49 MEQTRMAMCITDPHQPdlpIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDG 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15599797 936 ELYPSWVGITAVRDEEGDLVSFvcF-----FSDISERKASERRIHRLA 978
Cdd:PRK13559 129 EPFWNALHLGPVYGEDGRLLYF--FgsqwdVTDIRAVRALEAHERRLA 174
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
853-896 |
1.95e-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: 43.93 E-value: 1.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15599797 853 RMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQ 896
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGK 44
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
741-844 |
3.20e-05 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 43.99 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 741 YVSPSVQHVFGYSPEwALLNglhqtaTNPRQLgrlngllrrVRHAIGDRQKLAELRENPGQHLFALDCLRADGRKIPIEL 820
Cdd:pfam13426 6 YVNDAALRLLGYTRE-ELLG------KSITDL---------FAEPEDSERLREALREGKAVREFEVVLYRKDGEPFPVLV 69
|
90 100
....*....|....*....|....
gi 15599797 821 RIVLMWDEHDRFEGLLGIARDISQ 844
Cdd:pfam13426 70 SLAPIRDDGGELVGIIAILRDITE 93
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
843-974 |
3.24e-05 |
|
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: 48.23 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 843 SQQRRAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRqeanQLKHVLASLQhsg 922
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS----PLLEVLKTGK--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15599797 923 SWEGEILQKRKTGELYpswVGITAVRDEEGDLVSFVCFFSDISERKASERRI 974
Cdd:COG3829 74 PVTGVIQKTGGKGKTV---IVTAIPIFEDGEVIGAVETFRDITELKRLERKL 122
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
1277-1403 |
3.51e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 46.92 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 1277 LELELTESILMSDVAEAMQiLSGLKRLGLaiavDDFGTG---YSSLNYLKqfpIDVLKIDRSFVDGLPHGEQDAQIARAI 1353
Cdd:PRK11596 130 LRFELVEHIRLPKDSPFAS-MCEFGPLWL----DDFGTGmanFSALSEVR---YDYIKVARELFIMLRQSEEGRNLFSQL 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15599797 1354 IAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPAEQFGML 1403
Cdd:PRK11596 202 LHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLETL 251
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
717-842 |
3.72e-05 |
|
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: 44.33 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 717 RRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEwallNGLHQTatnprqlgrLNGLLRRVRHAIGDRQKLAELR 796
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSRE----EVIGKS---------LLDLIPEEDDAEVAELLRQALL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15599797 797 ENPGQHLFALDCLRADGRKIPIELRIVLMWDEHDRFEGLLGIARDI 842
Cdd:pfam00989 68 QGEESRGFEVSFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
726-842 |
5.18e-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. 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: 43.78 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 726 ISDVIFSTDAELNASYVSPSVQHVFGYSPEwALLNGLHQTATNPRQLGRLNGLLRRVRHAIGDRQKLAELRenpgqhlfa 805
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPE-ELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLR--------- 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 15599797 806 ldclRADGRKIPIELRIVLMWDEHDRFEGLLGIARDI 842
Cdd:cd00130 71 ----RKDGSVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
420-584 |
6.33e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 46.76 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 420 LEETRRRYQDIFEGVGVALCVLDlsalrqalvEQGldscaalrawlagepgrqqalleriRITEINDVSRRLLQIdSTEQ 499
Cdd:COG3852 2 LRESEELLRAILDSLPDAVIVLD---------ADG-------------------------RITYVNPAAERLLGL-SAEE 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 500 AWQRLLDHGPLQPDSLRLQVIEALIERRPVLELEATLRCGKSTPRHLWLQL-RLPENPGEWHAVtLSLSDVTSRKEVELS 578
Cdd:COG3852 47 LLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRRKDGEERPVDVSVsPLRDAEGEGGVL-LVLRDITERKRLERE 125
|
....*.
gi 15599797 579 LIEREK 584
Cdd:COG3852 126 LRRAEK 131
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
590-702 |
1.05e-04 |
|
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: 43.17 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 590 VQAVPDTLYIHDlHARRVIFSNHHLGQQLGYNQEELarMGENFWETLLHPDDQEYYWRIRNLQHVVGDGllLDSQLRWRH 669
Cdd:pfam00989 7 LESLPDGIFVVD-EDGRILYVNAAAEELLGLSREEV--IGKSLLDLIPEEDDAEVAELLRQALLQGEES--RGFEVSFRV 81
|
90 100 110
....*....|....*....|....*....|...
gi 15599797 670 RDGRWHWFDIREQAFsRDRSGRVARLIGVAKDI 702
Cdd:pfam00989 82 PDGRPRHVEVRASPV-RDAGGEILGFLGVLRDI 113
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
585-653 |
1.13e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 41.62 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 585 FWSDAVQAVPDTLYIHDLHaRRVIFSNHHLGQQLGYNQEELarMGENFWEtLLHPDD-QEYYWRIRNLQH 653
Cdd:smart00091 2 RLRAILESLPDGIFVLDLD-GRILYANPAAEELLGYSPEEL--IGKSLLE-LIHPEDrERVQEALQRLLS 67
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
282-426 |
2.08e-04 |
|
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: 45.53 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 282 AMTLASQRSLRQAATALAAIDERVLVTRADGRLSYLNPQAERLFGISSAQARQHHLLGLLPDLEpgwLTDAGGDGETRSE 361
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSP---LLEVLKTGKPVTG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599797 362 LLpLRVRGEPRTFTLSRHPlasypaladqawtlreqILQGGQVW----VLRDVTEEQHALGVLEETRRR 426
Cdd:COG3829 78 VI-QKTGGKGKTVIVTAIP-----------------IFEDGEVIgaveTFRDITELKRLERKLREEELE 128
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
664-703 |
4.67e-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: 39.09 E-value: 4.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15599797 664 QLRWRHRDGRWHWFDIREQAFsRDRSGRVARLIGVAKDIT 703
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPI-RDEDGEVEGILGVVRDIT 41
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
925-967 |
4.95e-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: 39.09 E-value: 4.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15599797 925 EGEILQKRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISER 967
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
809-845 |
5.15e-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: 39.09 E-value: 5.15e-04
10 20 30
....*....|....*....|....*....|....*..
gi 15599797 809 LRADGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQ 845
Cdd:smart00086 7 RRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
864-976 |
5.78e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 44.19 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 864 AAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPR-LLTADRQEANqlkHVLASLQHSGSWEG-EILQKRKTGELYPSw 941
Cdd:PRK11360 273 DGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSeLFPPNTPFAS---PLLDTLEHGTEHVDlEISFPGRDRTIELS- 348
|
90 100 110
....*....|....*....|....*....|....*
gi 15599797 942 VGITAVRDEEGDLVSFVCFFSDISERKASERRIHR 976
Cdd:PRK11360 349 VSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVAR 383
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
724-847 |
1.28e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 39.70 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 724 ENISDVIFSTDAELNASYVSPSVQHVFGYSPEwALLNGLHQTATNPRQLGRLNGLLRRVrhaigdrqkLAElrenpGQHL 803
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPE-ELLGKTLAELLPPEDAARLERALRRA---------LEG-----EEPI 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15599797 804 FALDCLRADGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQRR 847
Cdd:pfam08448 67 DFLEELLLNGEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
859-969 |
1.31e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 39.70 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599797 859 FEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVL----------DQQPRLLTADRQEANQLKHVLASLQHSGSWEGEI 928
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLgktlaellppEDAARLERALRRALEGEEPIDFLEELLLNGEERH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15599797 929 LQKRKtgelypswvgiTAVRDEEGDLVSFVCFFSDISERKA 969
Cdd:pfam08448 81 YELRL-----------TPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
857-889 |
2.41e-03 |
|
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: 37.91 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|...
gi 15599797 857 TVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYS 889
Cdd:pfam13188 5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYE 37
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
717-755 |
4.73e-03 |
|
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: 36.99 E-value: 4.73e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15599797 717 RRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPE 755
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPE 39
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
272-345 |
7.42e-03 |
|
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: 40.73 E-value: 7.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599797 272 RLHREQQgLRAmtlaSQRSLRQAATALAAIderVLVTRADGRLSYLNPQAERLFGISSAQARQHHLLGLLPDLE 345
Cdd:COG5809 129 RKRMEEA-LRE----SEEKFRLIFNHSPDG---IIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDD 194
|
|
| |
