|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
182-850 |
1.18e-127 |
|
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: 398.76 E-value: 1.18e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 182 RQPVSIGQHLKLFSQVPVPTLLDEPFVLQIRQQSDAFERLEWQSLLVVMLLLLGGMLMVAIGYLWLRRGLLKPFDRLMTE 261
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 262 LKEIDPSARRYTHISGCGGAEFKVLADRINNLLLRIFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQ 341
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 342 ALGRTLDSLLKSDDQLDEELLAFMSSGNRQPEYSKVTLQMQQPRIMERAVSNLCNHKG-------KVIGAVTVLRDITQE 414
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLlglllllLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 415 ETLKQQLRLKASVDGITGLYNRSAFEERLPGFAEGAD----TLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCL 490
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARrsgrRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 491 QGDEMLARLGGDEFGLAVRN-RSALEVAKLLKQLVKQVClQVLPCGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACL 569
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALA-EPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 570 AAKRKGSNQIHFFDDRNKELANERNApkWAVRIARAIEDKELLLYFQPIKGLngccRRQRL---EILLRIRDNSGRILPP 646
Cdd:COG5001 400 RAKAAGRNRYRFFDPEMDERARERLE--LEADLRRALERGELELHYQPQVDL----ATGRIvgaEALLRWQHPERGLVSP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 647 AQFIAAAERFKLMPEVDREVIRKAFLWLSE-HSQLWSELCVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITET 725
Cdd:COG5001 474 AEFIPLAEETGLIVPLGEWVLREACRQLAAwQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITES 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 726 SAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIET 805
Cdd:COG5001 554 ALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEV 633
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1100968759 806 VAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPLEQFYQWQKAHEQ 850
Cdd:COG5001 634 VAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
290-841 |
2.33e-112 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 369.39 E-value: 2.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 290 INNLLLRIFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLDEELLAFMSSG- 368
Cdd:PRK09776 524 VRQLNEALFQEKERLHITLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLHITFGDNGPLMENIYSCl 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 369 -NRQPEY--SKVTLQMqqpRIMER-----AVSNLCNHKGKVIGAVTVLRDITQEETLKQQLRLKASVDGITGLYNRSAFE 440
Cdd:PRK09776 604 tSRSAAYleQDVVLHC---RSGGSydvhySITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFE 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 441 ERLPGFAEGADTL----ALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLGGDEFGLAVRNRSaLEV 516
Cdd:PRK09776 681 KQLRRLLQTVNSThqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCN-VES 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 517 AKLLKQ-LVKQVCLQVLPCGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACLAAKRKGSNQIHFFDDRNKELANERNA 595
Cdd:PRK09776 760 ARFIATrIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRA 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 596 PKWAVRIARAIEDKELLLYFQPIKGLnGCCRRQRLEILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAFLwls 675
Cdd:PRK09776 840 LSLAEQWRMIKENQLMMLAHGVASPR-IPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFR--- 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 676 EHSQLWSE--LCVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDF 753
Cdd:PRK09776 916 QAAKAVASkgLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDF 995
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 754 GSGFASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIG 833
Cdd:PRK09776 996 GRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIA 1075
|
....*...
gi 1100968759 834 RPKPLEQF 841
Cdd:PRK09776 1076 RPQPLDLL 1083
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
293-844 |
1.42e-100 |
|
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: 324.43 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 293 LLLRIFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLDEELLAFMSSGNRQP 372
Cdd:COG2200 21 AEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 373 EYSKVTLQMQQPRIMERAVSNLCNHKGKVIGAVTVLRDITQEETLKQQLRLKASVDGITGLYNRSAFEERLPGF------ 446
Cdd:COG2200 101 LLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLllllll 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 447 AEGADTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLGGDEFGLAVRNRSALEVAKLLKQLVKQ 526
Cdd:COG2200 181 ALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 527 VCLQVLPCGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACLAAKRKGSNQIHFFDDRNKELANERnapKWAVRIARAI 606
Cdd:COG2200 261 LLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRL---ALESELREAL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 607 EDKELLLYFQPIKGLNGCcRRQRLEILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAFLWLSEHSQLWSELCV 686
Cdd:COG2200 338 EEGELRLYYQPIVDLRTG-RVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 687 SINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFASYGYLREL 766
Cdd:COG2200 417 SVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRL 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1100968759 767 PVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPLEQFYQW 844
Cdd:COG2200 497 PPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
601-840 |
1.00e-81 |
|
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: 262.48 E-value: 1.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 601 RIARAIEDKELLLYFQPIKGLNGccrrQRL---EILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAFLWLSEH 677
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDLRT----GRIvgyEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 678 SQLWSELCVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSGF 757
Cdd:cd01948 78 QAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 758 ASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPKP 837
Cdd:cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 1100968759 838 LEQ 840
Cdd:cd01948 238 AEE 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
599-835 |
1.41e-67 |
|
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: 224.50 E-value: 1.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 599 AVRIARAIEDKELLLYFQPIKGLNgCCRRQRLEILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAFLWLSEHS 678
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLR-TGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 679 QLwSELCVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFA 758
Cdd:pfam00563 80 LG-PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100968759 759 SYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRP 835
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
601-840 |
3.13e-65 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 218.24 E-value: 3.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 601 RIARAIEDKELLLYFQPIKGLNGccrrQRL---EILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAFLWLSE- 676
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRT----GRLvgvEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 677 HSQLWSELCVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSG 756
Cdd:smart00052 79 QAQGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 757 FASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPK 836
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
....
gi 1100968759 837 PLEQ 840
Cdd:smart00052 239 PLDD 242
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
410-848 |
2.31e-63 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 225.72 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 410 DITQEETLKQQLRLKASVDGITGLYNRSAFEERLPGFAEGAD--TLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIE 487
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADnnQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAIL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 488 SCLQGDEMLARLGGDEFGLAVRN--RSALE-VAKLLKQLVKQvclqvlPcggahYRVG---VSSGVAFhrGPCMAPAE-- 559
Cdd:PRK10060 302 SCLEEDQTLARLGGDEFLVLASHtsQAALEaMASRILTRLRL------P-----FRIGlieVYTGCSI--GIALAPEHgd 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 560 ----LLKDADIACLAAKRKGSNQIHFFD-DRNKELA-------NERnapkwavriaRAIEDKELLLYFQPIKGLNGCCRR 627
Cdd:PRK10060 369 dsesLIRSADTAMYTAKEGGRGQFCVFSpEMNQRVFeylwldtNLR----------KALENDQLVIHYQPKITWRGEVRS 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 628 qrLEILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAflwlSEHSQLWSE----LCVSINLSGNSLGSEGMLDY 703
Cdd:PRK10060 439 --LEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDV----VRQVAKWRDkginLRVAVNVSARQLADQTIFTA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 704 IAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFASYGYLRELPVDYVKIDGCFVRHLAS 783
Cdd:PRK10060 513 LKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHK 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100968759 784 NAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPLEQFYQWQKAH 848
Cdd:PRK10060 593 QPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRY 657
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
592-850 |
2.05e-54 |
|
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: 197.45 E-value: 2.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 592 ERNAPKWavRIARAIEDKELLLYFQPIKGLN-----GCcrrqrlEILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREV 666
Cdd:COG4943 268 RRLSPRR--RLRRAIKRREFYVHYQPIVDLKtgrcvGA------EALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 667 IRKAFL----WLSEHSQLWselcVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIqNRTRAMEMLNQLR 742
Cdd:COG4943 340 IEQVFRdlgdLLAADPDFH----ISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALR 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 743 RLGFAFALDDFGSGFASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEI 822
Cdd:COG4943 415 EAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRAR 494
|
250 260
....*....|....*....|....*...
gi 1100968759 823 GVDYAQGYAIGRPKPLEQFYQWQKAHEQ 850
Cdd:COG4943 495 GVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
430-841 |
6.03e-47 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 178.37 E-value: 6.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 430 ITGLYNRSAFEERLPGFAEGADTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLGGDEFGLAVR 509
Cdd:PRK13561 236 VSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIAN 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 510 NRSALEVAKLLKQLVKQVCLQVLPCGGAHYRVGVSSGVAFHRGPcMAPAELLKDADIACLAAKRKGSNQIHFFDDRNKEL 589
Cdd:PRK13561 316 GVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGD-LTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 590 ANERNAPKWAvrIARAIEDKELLLYFQP-IKGLNGccRRQRLEILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIR 668
Cdd:PRK13561 395 AQKRLTEESD--ILNALENHQFAIWLQPqVEMRSG--KLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 669 KAFLWLSEHSQLWSELCVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAF 748
Cdd:PRK13561 471 ESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRV 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 749 ALDDFGSGFASYGYL---RELPVDYVKIDGCFVRHLASnakDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVD 825
Cdd:PRK13561 551 ALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVG 627
|
410
....*....|....*.
gi 1100968759 826 YAQGYAIGRPKPLEQF 841
Cdd:PRK13561 628 IAQGFLFARALPIEIF 643
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
401-582 |
6.32e-46 |
|
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: 165.92 E-value: 6.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 401 VIGAVTVLRDITQEETLKQQLRLKASVDGITGLYNRSAFEERLPGFAEGAD----TLALCYLDLEQFKLINDNCGHDAGD 476
Cdd:COG2199 90 LLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARregrPLALLLIDLDHFKRINDTYGHAAGD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 477 QMLVMVARAIESCLQGDEMLARLGGDEFGLAVRNRSALEVAKLLKQLVKQVCLQVLPCGGAHYRVGVSSGVAFHRGPCMA 556
Cdd:COG2199 170 EVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDS 249
|
170 180
....*....|....*....|....*.
gi 1100968759 557 PAELLKDADIACLAAKRKGSNQIHFF 582
Cdd:COG2199 250 AEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
411-844 |
7.20e-46 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 176.88 E-value: 7.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 411 ITQEETlKQQLRLKASVDGITGLYNRSAFEERLPGFAEGADTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCL 490
Cdd:PRK11359 363 LEQEKS-RQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 491 QGDEMLARLGGDEFGLAVRNRSALEVAKLLKQLvKQVCLQVLPCGGAHYRVGVSSGVAFHRGPcmAPAELLKDADIACLA 570
Cdd:PRK11359 442 KPDQYLCRIEGTQFVLVSLENDVSNITQIADEL-RNVVSKPIMIDDKPFPLTLSIGISYDVGK--NRDYLLSTAHNAMDY 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 571 AKRKGSNQIHFFDDRNKELANERNAPKWAVRiaRAIEDKELLLYFQP-IKGLNGccRRQRLEILLRIRDNSGRILPPAQF 649
Cdd:PRK11359 519 IRKNGGNGWQFFSPAMNEMVKERLVLGAALK--EAISNNQLKLVYQPqIFAETG--ELYGIEALARWHDPLHGHVPPSRF 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 650 IAAAERFKLMPEVDREVIRKA----FLWLSEHSQLWSelcVSINLSGNSLGSEGMLDYIAEMQGRYGIPSSCVCFEITET 725
Cdd:PRK11359 595 IPLAEEIGEIENIGRWVIAEAcrqlAEWRSQNIHIPA---LSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITES 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 726 SAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIET 805
Cdd:PRK11359 672 MMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTV 751
|
410 420 430
....*....|....*....|....*....|....*....
gi 1100968759 806 VAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPLEQFYQW 844
Cdd:PRK11359 752 VAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGW 790
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
428-580 |
6.69e-41 |
|
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: 147.32 E-value: 6.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 428 DGITGLYNRSAFEERLPGFAEGAD----TLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLGGDE 503
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARrsgrPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100968759 504 FGLAVRNRSALEVAKLLKQLVKQVCLQVLPcGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACLAAKRKGSNQIH 580
Cdd:cd01949 83 FAILLPGTDLEEAEALAERLREAIEEPFFI-DGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
476-841 |
3.80e-40 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 158.18 E-value: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 476 DQMLVMVARAIESCLQGDEMLARLGGDEFGL----AVRNRSALEVA-KLLKQLVKQVCLQVLPcggahYRVGVSSGVAFH 550
Cdd:PRK11829 286 QQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVlargTRRSFPAMQLArRIMSQVTQPLFFDEIT-----LRPSASIGITRY 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 551 RGPCMAPAELLKDADIACLAAKRKGSNQIHFFD----DRNKELANERNapkwavRIARAIEDKELLLYFQPIKGLngccR 626
Cdd:PRK11829 361 QAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEphliEKTHKRLTQEN------DLLQAIENHDFTLFLQPQWDM----K 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 627 RQRL---EILLRIRDNSGRILPPAQFIAAAERFKLMPEVDREVIRKAFLWLSEHSQLWSELCVSINLSGNSLGSEGMLDY 703
Cdd:PRK11829 431 RQQVigaEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 704 IAEMQGRYGIPSSCVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFASYGYLR---ELPVDYVKIDGCFVRH 780
Cdd:PRK11829 511 LKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKN 590
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100968759 781 LasnAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPLEQF 841
Cdd:PRK11829 591 L---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEF 648
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
425-582 |
2.14e-37 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 137.76 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 425 ASVDGITGLYNRSAFEERLPGFAEGA----DTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLG 500
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRAqrqgSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 501 GDEFGLAVRNRSALEVAKLLKQLVKQVCLQVLPcGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACLAAKRKGSNQIH 580
Cdd:smart00267 83 GDEFALLLPETSLEEAIALAERILQQLREPIII-HGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 1100968759 581 FF 582
Cdd:smart00267 162 VY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
425-578 |
8.93e-34 |
|
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: 126.98 E-value: 8.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 425 ASVDGITGLYNRSAFEERL-----PGFAEGADtLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARL 499
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLeqelqRALREGSP-VAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 500 GGDEFGLAVRNRS---ALEVAKLLKQLVKQvcLQVLPCGGAHYR-VGVSSGVAFHRGPCMAPAELLKDADIACLAAKRKG 575
Cdd:pfam00990 80 GGDEFAILLPETSlegAQELAERIRRLLAK--LKIPHTVSGLPLyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
...
gi 1100968759 576 SNQ 578
Cdd:pfam00990 158 RNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
425-583 |
7.58e-28 |
|
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: 110.50 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 425 ASVDGITGLYNRSAFEERLPGFAEGADT----LALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLG 500
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRfqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 501 GDEFGLAVRNRS---ALEVAKLLKQLVKQVCLQVlpCGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACLAAKRKGSN 577
Cdd:TIGR00254 82 GEEFVVILPGTPledALSKAERLRDAINSKPIEV--AGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*.
gi 1100968759 578 QIHFFD 583
Cdd:TIGR00254 160 RVVVAD 165
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
422-838 |
2.57e-26 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 114.96 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 422 RLKASVDGITGLYNRSAFEERLPGFAEGADTLA----LCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQ--GDEM 495
Cdd:PRK11059 225 RSNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGahgvVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMryPGAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 496 LARLGGDEFGLAVRNRSALEVAKLLKQLVKQVCLQVLP----------CGGAHYRVGVSSGvafhrgpcmapaELLKDAD 565
Cdd:PRK11059 305 LARYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPPPkmldrddflhIGICAYRSGQSTE------------QVMEEAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 566 IACLAAKRKGSNQIHFFDDRNK-ELAneRNAPKWAVRIARAIEDKELLLYFQPIKGLNGccRRQRLEILLRIRDNSGRIL 644
Cdd:PRK11059 373 MALRSAQLQGGNGWFVYDKAQLpEKG--RGSVRWRTLLEQTLVRGGPRLYQQPAVTRDG--KVHHRELFCRIRDGQGELL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 645 PPAQFIAAAERFKLMPEVDREVIRKAFLWLSehsqLWSELCVSINLSGNSLGS--------EGMLDYIAEMQgrygipsS 716
Cdd:PRK11059 449 SAELFMPMVQQLGLSEQYDRQVIERVLPLLR----YWPEENLSINLSVDSLLSrafqrwlrDTLLQCPRSQR-------K 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 717 CVCFEITETSAIQNRTRAMEMLNQLRRLGFAFALDDFGSGFASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHD 796
Cdd:PRK11059 518 RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVG 597
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1100968759 797 VCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPL 838
Cdd:PRK11059 598 ACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
425-579 |
5.50e-23 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 103.06 E-value: 5.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 425 ASVDGITGLYNRSAFEERLPGFAEGA----DTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLG 500
Cdd:PRK09581 292 AVTDGLTGLHNRRYFDMHLKNLIERAnergKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 501 GDEF-------GLAVrnrsALEVAKLLKQLVKQVCLQVlPCGGAHYRVGVSSGVAFHRGPCMAPAELLKDADIACLAAKR 573
Cdd:PRK09581 372 GEEFvvvmpdtDIED----AIAVAERIRRKIAEEPFII-SDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKN 446
|
....*.
gi 1100968759 574 KGSNQI 579
Cdd:PRK09581 447 TGRNRV 452
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
602-846 |
9.86e-21 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 96.60 E-value: 9.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 602 IARAIEDKELLLYFQPIkgLNGCCRRQR-LEILLRIRDNS-GRIlPPAQFIAAAERFKLMPEVDREVIRkafLWLSEHSQ 679
Cdd:PRK10551 268 ILTGIKRGQFYVEYQPV--VDTQTLRVTgLEALLRWRHPTaGEI-PPDAFINYAEAQKLIVPLTQHLFE---LIARDAAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 680 LWSEL----CVSINLSGNSLGSEG----MLDYIAEMQGRYGIPsscvCFEITETSAIQNRtRAMEMLNQLRRLGFAFALD 751
Cdd:PRK10551 342 LQKVLpvgaKLGINISPAHLHSDSfkadVQRLLASLPADHFQI----VLEITERDMVQEE-EATKLFAWLHSQGIEIAID 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 752 DFGSGFASYGYLRELPVDYVKIDGCFVRHLASNAKDYAIVKSIHDVCRVMGIETVAEFVENQEIVDKLLEIGVDYAQGYA 831
Cdd:PRK10551 417 DFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYW 496
|
250
....*....|....*
gi 1100968759 832 IGRPKPLEQFYQWQK 846
Cdd:PRK10551 497 ISRPLPLEDFVRWLK 511
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
416-601 |
4.90e-18 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 88.53 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 416 TLKQQLRLKASVDGITGLYNRSAFEERLPGFAEGADT----LALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQ 491
Cdd:PRK15426 389 VLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRdqqpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLR 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 492 GDEMLARLGGDEFGLAVRNRS---ALEVAKLLKQLVKqvCLQVLPCGGAHYRVGVSSGVA-FHRGPCMAPAELLKDADIA 567
Cdd:PRK15426 469 AQDVAGRVGGEEFCVVLPGASlaeAAQVAERIRLRIN--EKEILVAKSTTIRISASLGVSsAEEDGDYDFEQLQSLADRR 546
|
170 180 190
....*....|....*....|....*....|....
gi 1100968759 568 CLAAKRKGSNQIhFFDDrnkelanerNAPKWAVR 601
Cdd:PRK15426 547 LYLAKQAGRNRV-CASD---------NAHEREVK 570
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
421-586 |
4.14e-17 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 82.81 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 421 LRLKASVDGITGLYNR----SAFEERLpgFAEGADTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEML 496
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRrvldESFDHQL--RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 497 ARLGGDEFGLAVRNRSALEVAKLLKQLVKQVCLQVLPCGGAHYRVGVSSGVAFHRgPCMAPAELLKDADIACLAAKRKGS 576
Cdd:PRK09894 203 YRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAF-PEETLDVVIGRADRAMYEGKQTGR 281
|
170
....*....|
gi 1100968759 577 NQIHFFDDRN 586
Cdd:PRK09894 282 NRVMFIDEQN 291
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
418-578 |
1.49e-15 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 79.10 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 418 KQQLRLKASVDGITGLYNRSAFEERLPGFAE----GADTLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGD 493
Cdd:PRK10245 198 KRRLQVMSTRDGMTGVYNRRHWETLLRNEFDncrrHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 494 EMLARLGGDEFGLAVRNRSALEVAKLLKQLVKQVCLQVLPCgGAHYRVGVSSGVAfHRGPCMAP-AELLKDADIACLAAK 572
Cdd:PRK10245 278 DVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPN-APQVTLRISVGVA-PLNPQMSHyREWLKSADLALYKAK 355
|
....*.
gi 1100968759 573 RKGSNQ 578
Cdd:PRK10245 356 NAGRNR 361
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
299-425 |
5.51e-15 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 77.58 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 299 QQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLDEELLAFMSSGNRQPEYsKVT 378
Cdd:COG3852 4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTER-EVT 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1100968759 379 LQM--QQPRIMERAVSNLCNHKGKvIGAVTVLRDITQEETLKQQLRLKA 425
Cdd:COG3852 83 LRRkdGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAE 130
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
282-425 |
1.83e-12 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 70.77 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 282 EFKVLADRINNLLLRIFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLDEEL 361
Cdd:PRK11360 242 ELGEISQAINNLAQALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100968759 362 LAFMSSGNrqpEYSKVTLQMQQPRIMER---AVSNLCNHKGKVIGAVTVLRDITQ----EETLKQQLRLKA 425
Cdd:PRK11360 322 LDTLEHGT---EHVDLEISFPGRDRTIElsvSTSLLHNTHGEMIGALVIFSDLTErkrlQRRVARQERLAA 389
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
295-435 |
3.60e-12 |
|
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: 69.41 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 295 LRIFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKsddqlDEELLAFMSSGNRqpey 374
Cdd:COG3829 4 LELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP-----NSPLLEVLKTGKP---- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1100968759 375 skVTLQMQQPRIMERAVsnLCN-----HKGKVIGAVTVLRDITQEETLKQQLRLKASVDGITGLYN 435
Cdd:COG3829 75 --VTGVIQKTGGKGKTV--IVTaipifEDGEVIGAVETFRDITELKRLERKLREEELERGLSAKYT 136
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
245-425 |
1.30e-11 |
|
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: 67.68 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 245 LWLRRGLLKPFDRL---MTELKEIDPSARrythISGCGGAEFKVLADRINNLLLRIFQQN---ERSRITLESIAE----A 314
Cdd:COG5000 27 LLLARRLTRPLRRLaeaTRAVAAGDLSVR----LPVTGDDEIGELARAFNRMTDQLKEQReelEERRRYLETILEnlpaG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 315 VILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLkSDDQLDEELLAFMSSGNRQpeysKVTLQMQQPRIMERAVSNL 394
Cdd:COG5000 103 VIVLDADGRITLANPAAERLLGIPLEELIGKPLEELL-PELDLAELLREALERGWQE----EIELTRDGRRTLLVRASPL 177
|
170 180 190
....*....|....*....|....*....|.
gi 1100968759 395 cnhkgKVIGAVTVLRDITQeetLKQQLRLKA 425
Cdd:COG5000 178 -----RDDGYVIVFDDITE---LLRAERLAA 200
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
414-523 |
2.83e-11 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 66.57 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 414 EETLKQQLRLKASV---------DGITGLYNRSAFEERLPGFAEGAD---TLALCYLDLEQFKLINDNCGHDAGDQMLVM 481
Cdd:PRK09966 228 DEMEEWQLRLQAKNaqllrtalhDPLTGLANRAAFRSGINTLMNNSDarkTSALLFLDGDNFKYINDTWGHATGDRVLIE 307
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1100968759 482 VARAIESCLQGDEMLARLGGDEFGLAVRN-RSALEVAKLLKQL 523
Cdd:PRK09966 308 IAKRLAEFGGLRHKAYRLGGDEFAMVLYDvQSESEVQQICSAL 350
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
299-504 |
5.33e-11 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 63.89 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 299 QQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLL--KSDDQLDEELLAFMSSGNRQPEYSK 376
Cdd:COG2202 8 ESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLppEDDDEFLELLRAALAGGGVWRGELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 377 VTLQMQQPRIMERAVSNLCNHKGKVIGAVTVLRDITQ----EETLKQQL-RLKASVDGITGLYNRSAFEERLPGFAEGAD 451
Cdd:COG2202 88 NRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITErkraEEALRESEeRLRLLVENAPDGIFVLDLDGRILYVNPAAE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1100968759 452 TLALCYLDLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEMLARLGGDEF 504
Cdd:COG2202 168 ELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDG 220
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
714-840 |
1.45e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 64.05 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 714 PSSCVcFEITETSAIqnRTRAMEMLNQLRRLGFAFALDDFGsgfASYGYLRELP-VDYVKIDgcfVRHLASNAKDyAIVK 792
Cdd:COG3434 83 PERVV-LEILEDVEP--DEELLEALKELKEKGYRIALDDFV---LDPEWDPLLPlADIIKID---VLALDLEELA-ELVA 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1100968759 793 SIHDvcrvMGIETVAEFVENQEIVDKLLEIGVDYAQGYAIGRPKPLEQ 840
Cdd:COG3434 153 RLKR----YGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
295-431 |
3.71e-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: 63.07 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 295 LRIFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLDE-ELLAFMSSGNRQPE 373
Cdd:COG5809 8 LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELrEILKLLKEGESRDE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1100968759 374 YSKvTLQMQQPRIME--RAVSNLCNHKGKVIGAVTVLRDITQEETLKQQLR---------LKASVDGIT 431
Cdd:COG5809 88 LEF-ELRHKNGKRLEfsSKLSPIFDQNGDIEGMLAISRDITERKRMEEALReseekfrliFNHSPDGII 155
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
297-422 |
5.63e-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: 62.68 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 297 IFQQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQldEELLAFMSSGNRQPEYSK 376
Cdd:COG5809 136 LRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQ--ENVAAFISQLLKDGGIAQ 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1100968759 377 --VTLQMQQPRIME-RAVSNLCNHKGKVIGAVTVLRDITQEETLKQQLR 422
Cdd:COG5809 214 geVRFWTKDGRWRLlEASGAPIKKNGEVDGIVIIFRDITERKKLEELLR 262
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
299-421 |
2.87e-08 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 55.80 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 299 QQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDD--QLDEELLAFMSSGNRQPEYSK 376
Cdd:COG2202 134 ESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDreRLLELLRRLLEGGRESYELEL 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1100968759 377 VTLQMQ-QPRIMERAVSNLCNhKGKVIGAVTVLRDITQEETLKQQL 421
Cdd:COG2202 214 RLKDGDgRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
308-415 |
3.69e-08 |
|
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: 52.03 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 308 LESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLD-EELLAFMSSGNRQPEYSKVTLQMQQPRI 386
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARlERALRRALEGEEPIDFLEELLLNGEERH 80
|
90 100
....*....|....*....|....*....
gi 1100968759 387 MERAVSNLCNHKGKVIGAVTVLRDITQEE 415
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDITERR 109
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
281-421 |
3.31e-07 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 53.31 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 281 AEFKVLADRINNLLLRIFQQNErsrITLESIAEAVILTNNKAKVIYLNPQAESLLGLrsqQALGRTLDSLLKS---DDQL 357
Cdd:COG3290 66 LLLAALLLKLLEEIARLVEERE---AVLESIREGVIAVDRDGRITLINDAARRLLGL---DAIGRPIDEVLAEvleTGER 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100968759 358 DEELLAfmssGNRQPEYSKVTLQmqqprimeravsnlcnHKGKVIGAVTVLRDITQEETLKQQL 421
Cdd:COG3290 140 DEEILL----NGRVLVVNRVPIR----------------DDGRVVGAVATFRDRTELERLEEEL 183
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
311-411 |
4.53e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 48.78 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 311 IAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDD--QLDEELLAFMSSGNRQPEYSKVTLQMQQPRIME 388
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDreELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1100968759 389 RAVSNLCNHKGKVIGAVTVLRDI 411
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
301-411 |
4.75e-07 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 48.95 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 301 NERSRItLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTL-DSLLKSDDQLDEELL--AFMSSGNRQPEYSKV 377
Cdd:pfam00989 1 EDLRAI-LESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLlDLIPEEDDAEVAELLrqALLQGEESRGFEVSF 79
|
90 100 110
....*....|....*....|....*....|....
gi 1100968759 378 TLQMQQPRIMERAVSNLCNHKGKVIGAVTVLRDI 411
Cdd:pfam00989 80 RVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
302-421 |
8.25e-07 |
|
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: 48.83 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 302 ERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDD-QLDEELLAFMSSGNRQPEYSKVTLQ 380
Cdd:TIGR00229 3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDrEEVRERIERRLEGEPEPVSEERRVR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1100968759 381 MQQPRI--MERAVSNLcNHKGKVIGAVTVLRDITQEETLKQQL 421
Cdd:TIGR00229 83 RKDGSEiwVEVSVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
299-423 |
9.78e-07 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 52.43 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 299 QQNERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQldEELLAFMSSGNRQPEYSKVT 378
Cdd:COG5805 154 EQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDK--EEFKERIESITEVWQEFIIE 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1100968759 379 LQM----QQPRIMERAVSNLCNHKGKVIGAVTVLRDITQ----EETLKQQLRL 423
Cdd:COG5805 232 REIitkdGRIRYFEAVIVPLIDTDGSVKGILVILRDITEkkeaEELMARSEKL 284
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
302-356 |
4.42e-06 |
|
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: 45.08 E-value: 4.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1100968759 302 ERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQ 356
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDR 55
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
323-413 |
3.12e-05 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 43.22 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 323 KVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQlDEELLAFMSSGNRQPEYSKVTLQMQQPRIMERAVSN-LCNHKGKV 401
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPED-SERLREALREGKAVREFEVVLYRKDGEPFPVLVSLApIRDDGGEL 81
|
90
....*....|..
gi 1100968759 402 IGAVTVLRDITQ 413
Cdd:pfam13426 82 VGIIAILRDITE 93
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
302-362 |
5.40e-04 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 39.07 E-value: 5.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100968759 302 ERSRITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQALGRTLDSLLKSDDQLDEELL 362
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELL 61
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
248-423 |
6.67e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 43.51 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 248 RRGLLKPFDRLMTELKEIDPSarryTHISGCGGAEFKVLADRINNLLLRifQQNERSRITLESIAEAVILTNNKAKVI-Y 326
Cdd:PRK13560 284 KDGRTRPVDVIFNHAEFDDKE----NHCAGLVGAITDISGRRAAERELL--EKEDMLRAIIEAAPIAAIGLDADGNICfV 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 327 LNPQAESLLGLRSQQALGRTLDSLlksDDQLDEEL---------------------LAFMSSGNRQPEYSKVTLQMQQPR 385
Cdd:PRK13560 358 NNNAAERMLGWSAAEVMGKPLPGM---DPELNEEFwcgdfqewypdgrpmafdacpMAKTIKGGKIFDGQEVLIEREDDG 434
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1100968759 386 IMERAV--SNLCNHKGKVIGAVTVLRDITQEETLKQQLRL 423
Cdd:PRK13560 435 PADCSAyaEPLHDADGNIIGAIALLVDITERKQVEEQLLL 474
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
459-548 |
3.32e-03 |
|
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: 38.49 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 459 DLEQFKLINDNCGHDAGDQMLVMVARAIESCLQGDEML-ARLGGDEFgLAVRN----RSALEVAKLLKQLVKQVCLQVLP 533
Cdd:cd07556 8 DIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkIKTIGDEF-MVVSGldhpAAAVAFAEDMREAVSALNQSEGN 86
|
90
....*....|....*
gi 1100968759 534 cgGAHYRVGVSSGVA 548
Cdd:cd07556 87 --PVRVRIGIHTGPV 99
|
|
| PRK11086 |
PRK11086 |
sensory histidine kinase DcuS; Provisional |
296-421 |
3.89e-03 |
|
sensory histidine kinase DcuS; Provisional
Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 40.67 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100968759 296 RIFQQneRSrITLESIAEAVILTNNKAKVIYLNPQAESLLGLRSQQAlgrtldsllksDDQLDEELLAFMSSGNrqpeYS 375
Cdd:PRK11086 218 TLFEQ--RQ-AMLQSIKEGVIAVDDRGEVTLINDEAKRLFNYKKGLE-----------DDPLGTDVESWMPVSR----LK 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1100968759 376 KVtLQMQQPRIMERAVSN----LCNH-----KGKVIGAVTVLRDITQEETLKQQL 421
Cdd:PRK11086 280 EV-LRTGTPRRDEEININgrllLTNTvpvrvNGEIIGAIATFRDKTEVRQLAQRL 333
|
|
| |
