|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
503-946 |
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: 647.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 503 VGIYGIGRDITEQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDE 582
Cdd:COG5001 228 VAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 583 ILKQVVQRILHVLPIEAHLGRFHGDKFCLLLTGQIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDA 662
Cdd:COG5001 308 LLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 663 HSLLKNADIAVSRAKRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPK 742
Cdd:COG5001 388 EELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 743 LGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQALGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLH 822
Cdd:COG5001 468 RGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 823 LELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGH 902
Cdd:COG5001 548 LEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAH 627
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1050292024 903 GLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEELSA 946
Cdd:COG5001 628 SLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
705-943 |
1.03e-119 |
|
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: 364.56 E-value: 1.03e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 705 LRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQAlGN 784
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA-GG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 785 QQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFS 864
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050292024 865 YLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEE 943
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
406-944 |
2.73e-116 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 370.94 E-value: 2.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYsTDLHGNLTNVNPAFEKVLGYKREEVLHTNALK-YIHPNDV---RRVSMHFYRalRGkiQYYNLE--I 479
Cdd:PRK10060 115 QVVSEANSVIVI-LDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKlFMSRREAaasRRNIRGFFR--SG--NAYEVErwI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 480 PTKSGkPLLFQIKNVPIVVDGKKVGIYGI--GRDITEQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKnrK 557
Cdd:PRK10060 190 KTRKG-QRLFLFRNKFVHSGSGKNEIFLIcsGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNN--Q 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 558 LAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFHGDKFCLLLTGQihSEKVFE-TATRIAKEMTKP 636
Cdd:PRK10060 267 VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHT--SQAALEaMASRILTRLRLP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 637 IVYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFL 716
Cdd:PRK10060 345 FRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVI 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 717 CYQPIVDITtGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQALGnQQLSIFVNVSAA 796
Cdd:PRK10060 425 HYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKG-INLRVAVNVSAR 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 797 QFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKI 876
Cdd:PRK10060 503 QLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKL 582
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1050292024 877 DRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEEL 944
Cdd:PRK10060 583 DQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
702-943 |
1.83e-108 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 335.34 E-value: 1.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 702 ERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQA 781
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 782 LGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYA 861
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 862 SFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATA 941
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 1050292024 942 EE 943
Cdd:smart00052 241 DD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
705-938 |
2.84e-92 |
|
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: 292.30 E-value: 2.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 705 LRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQalGN 784
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ--LG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 785 QQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFS 864
Cdd:pfam00563 82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050292024 865 YLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRP 938
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
525-684 |
3.20e-36 |
|
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: 134.39 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 525 LAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRF 604
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 605 HGDKFCLLLTGQIhSEKVFETATRIAKEM-TKPIVYDGKE-FFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGN 682
Cdd:TIGR00254 81 GGEEFVVILPGTP-LEDALSKAERLRDAInSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
..
gi 1050292024 683 RV 684
Cdd:TIGR00254 160 RV 161
|
|
| FIST |
COG3287 |
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms] ... |
42-358 |
4.66e-32 |
|
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms];
Pssm-ID: 442517 [Multi-domain] Cd Length: 382 Bit Score: 129.30 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 42 ELGKIIELLRRCLPQAQLLGMT-----CGDPFHPGGrfnICFTVF--EKVSVHSVLLPYKEfANELELAAYISDALI--- 111
Cdd:COG3287 46 DLEALLAALRAAFPGAPIIGCStageiSPGGVLEGS---VVLLAFsfDKFRVGVAVGDGLS-DDSREAGRELARRLLaal 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 112 --TEETNLLLLFTDQES-NFHSLIRHIPLVNDQTVIIAG-------RMKEGgRLFSHEGIVADGIVAISFnGSSLRVQLS 181
Cdd:COG3287 122 gpDPDLRFALLLSDGLSgNEEELLEGLYSALGPDVPIFGgsagddlRFEKT-YVFHNGEVLSDAAVVALL-GTSLPVGVG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 182 HPFLWEPVGATFRVTKCSGNKLYELDGKKAARLLEHYLGKEfIERLPFSGAEFPFVVEKNGHKQCL-SVAKANKDGSIEI 260
Cdd:COG3287 200 SSHGWKPTGPEMVVTKAEGRVVYEIDGEPAAEVYARYLGDD-AEELPASFLLFPLGVRIGGGEYLVrSPLAVEEDGSLTF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 261 NGRVDPGEMVKISFVPLPSLFWHMSDKLTKLAK----KPAEAIFFY---QSMAMEGYVSLALQQITATLEqiSPTFTPFS 333
Cdd:COG3287 279 AGDIPEGSVLRLMEGNPDDLIEAAERAAEAALArlggKPEAALLFDcvgRRLVLGQRVEEELEAVSELLG--APVAGFYT 356
|
330 340
....*....|....*....|....*.
gi 1050292024 334 FAELVTKDRYAPM-HPATFSMVALSE 358
Cdd:COG3287 357 YGEIGPFGGGGNQhHNQTLTGVAFGE 382
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
407-522 |
1.51e-21 |
|
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: 90.81 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 407 SLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRG--KIQYYNLEIPTKSG 484
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGepEPVSEERRVRRKDG 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1050292024 485 KPLLFQIKNVPIVVDGKKVGIYGIGRDITEQKKAEEKI 522
Cdd:TIGR00229 87 SEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
406-522 |
2.83e-21 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 94.32 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKIQYYNLEIPTKSGK 485
Cdd:COG2202 140 RLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGD 219
|
90 100 110
....*....|....*....|....*....|....*....
gi 1050292024 486 PLLFQIKN--VPIVVDGKKVGIYGIGRDITEQKKAEEKI 522
Cdd:COG2202 220 GRWVWVEAsaVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| FIST |
smart00897 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
41-209 |
2.73e-13 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 214894 Cd Length: 196 Bit Score: 69.65 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 41 SELGKIIELLRRCLPQA-QLLGMTCGDPFHPG------GRFNICFTVFEKVSVHSVLLPYKEFANEL---ELAAYISDAL 110
Cdd:smart00897 13 YDAEALLAALRERFPGAtPIVGCSTAGEITTGvvqefeDEPALSVMLFELPLVSFDVFSLVDPLPDLvagLLLAALLAAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 111 ITEETNLLLLFTDQ-ESNFHSLIRHIPLVNDQTVIIAG-----RMKEGGRLFSHEGIVADGIVAISFnGSSLRVQLSHPF 184
Cdd:smart00897 93 DPRNTFALLLLDDLsSSNEEELLEGLDEALPEGIPIGGgsagdNLRFQETYVFTNGRVHSGAVVVAF-GGGLRFGTGVTQ 171
|
170 180
....*....|....*....|....*
gi 1050292024 185 LWEPVGATFRVTKCSGNKLYELDGK 209
Cdd:smart00897 172 GWRPIGPPFVVTKAEGNVVYELDGE 196
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
414-512 |
1.50e-11 |
|
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: 61.88 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 414 DIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRV-SMHFYRALRGKIQYYNLEIPTKSGKPLLFQIK 492
Cdd:cd00130 3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELrERLENLLSGGEPVTLEVRLRRKDGSVIWVLVS 82
|
90 100
....*....|....*....|.
gi 1050292024 493 NVPIV-VDGKKVGIYGIGRDI 512
Cdd:cd00130 83 LTPIRdEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
406-512 |
1.73e-11 |
|
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: 62.05 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALR--GKIQYYNLEIPTKS 483
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLqgEESRGFEVSFRVPD 83
|
90 100 110
....*....|....*....|....*....|
gi 1050292024 484 GKPLLFQIKNVPIV-VDGKKVGIYGIGRDI 512
Cdd:pfam00989 84 GRPRHVEVRASPVRdAGGEILGFLGVLRDI 113
|
|
| FIST |
pfam08495 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
156-209 |
1.21e-09 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 462495 Cd Length: 126 Bit Score: 57.21 E-value: 1.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1050292024 156 FSHEGIVADGIVAISFNGSSLRVQ--LSHPflWEPVGATFRVTKCSGNKLYELDGK 209
Cdd:pfam08495 73 LFNGEVYSDGAVAVALYGDALKVGvgVSQG--WRPIGPPFVVTKADGNRVYELDGR 126
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
406-460 |
4.23e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 53.56 E-value: 4.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRV 460
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERV 58
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
379-522 |
7.17e-05 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 46.50 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 379 QGVMTLAHLLSATSREM--ErlhvCGQIS-------QSLFE---HNTDIVYST-------DLHGNLTNVNPAFEKVLGYK 439
Cdd:PRK11360 223 DGLSTLENDLSTRLPPLpgE----LGEISqainnlaQALREtrsLNELILESIadgviaiDRQGKITTMNPAAEVITGLQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 440 REEVLhtnalkYIHPNDVRRVSMHFY----RALRGKIQYYNLEI--PTKSGKPLLFQIKNVPIVVDGKKVGIYGIGRDIT 513
Cdd:PRK11360 299 RHELV------GKPYSELFPPNTPFAspllDTLEHGTEHVDLEIsfPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLT 372
|
....*....
gi 1050292024 514 EQKKAEEKI 522
Cdd:PRK11360 373 ERKRLQRRV 381
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
503-946 |
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: 647.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 503 VGIYGIGRDITEQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDE 582
Cdd:COG5001 228 VAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 583 ILKQVVQRILHVLPIEAHLGRFHGDKFCLLLTGQIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDA 662
Cdd:COG5001 308 LLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 663 HSLLKNADIAVSRAKRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPK 742
Cdd:COG5001 388 EELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 743 LGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQALGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLH 822
Cdd:COG5001 468 RGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 823 LELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGH 902
Cdd:COG5001 548 LEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAH 627
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1050292024 903 GLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEELSA 946
Cdd:COG5001 628 SLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
505-948 |
3.34e-130 |
|
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: 404.55 E-value: 3.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 505 IYGIGRDITEQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLE-KAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEI 583
Cdd:COG2200 133 VLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLlLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 584 LKQVVQRILHVLPIEAHLGRFHGDKFCLLLTGQIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDAH 663
Cdd:COG2200 213 LLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 664 SLLKNADIAVSRAKRSGGNRVQFYSAkMNDETLHRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKL 743
Cdd:COG2200 293 LLLAAAAAAAAAAAGGGRGRVVFFAA-AEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 744 GLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQALGnQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHL 823
Cdd:COG2200 372 GLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERG-LDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 824 ELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHG 903
Cdd:COG2200 451 EITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHR 530
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1050292024 904 LGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEELSAHI 948
Cdd:COG2200 531 LGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
705-943 |
1.03e-119 |
|
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: 364.56 E-value: 1.03e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 705 LRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQAlGN 784
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA-GG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 785 QQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFS 864
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050292024 865 YLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEE 943
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
406-944 |
2.73e-116 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 370.94 E-value: 2.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYsTDLHGNLTNVNPAFEKVLGYKREEVLHTNALK-YIHPNDV---RRVSMHFYRalRGkiQYYNLE--I 479
Cdd:PRK10060 115 QVVSEANSVIVI-LDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKlFMSRREAaasRRNIRGFFR--SG--NAYEVErwI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 480 PTKSGkPLLFQIKNVPIVVDGKKVGIYGI--GRDITEQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKnrK 557
Cdd:PRK10060 190 KTRKG-QRLFLFRNKFVHSGSGKNEIFLIcsGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNN--Q 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 558 LAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFHGDKFCLLLTGQihSEKVFE-TATRIAKEMTKP 636
Cdd:PRK10060 267 VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHT--SQAALEaMASRILTRLRLP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 637 IVYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFL 716
Cdd:PRK10060 345 FRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVI 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 717 CYQPIVDITtGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQALGnQQLSIFVNVSAA 796
Cdd:PRK10060 425 HYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKG-INLRVAVNVSAR 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 797 QFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKI 876
Cdd:PRK10060 503 QLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKL 582
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1050292024 877 DRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATAEEL 944
Cdd:PRK10060 583 DQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
702-943 |
1.83e-108 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 335.34 E-value: 1.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 702 ERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQA 781
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 782 LGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYA 861
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 862 SFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRPATA 941
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 1050292024 942 EE 943
Cdd:smart00052 241 DD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
514-953 |
1.55e-99 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 330.19 E-value: 1.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 514 EQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAkrknRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILH 593
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKA----VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 594 VLPIEAHLGRFHGDKFCLlltgqIHSEKVFETATRIAKEM----TKPIVYDGKEFFITASIGISFypSDGVDAHSLLKNA 669
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVL-----VSLENDVSNITQIADELrnvvSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 670 DIAVSRAKRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPD 749
Cdd:PRK11359 513 HNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPS 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 750 EFISLAEETGLIHEIGRWVLETACKQTKKWQALGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENS 829
Cdd:PRK11359 593 RFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESM 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 830 MLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIV 909
Cdd:PRK11359 673 MMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVV 752
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1050292024 910 AEGVETDEHLQLLKMLRCHYVQGYALYRPATAEELSAHITVGKP 953
Cdd:PRK11359 753 AEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLP 796
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
705-938 |
2.84e-92 |
|
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: 292.30 E-value: 2.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 705 LRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTKKWQalGN 784
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ--LG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 785 QQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFS 864
Cdd:pfam00563 82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050292024 865 YLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRP 938
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
697-946 |
2.24e-79 |
|
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: 267.94 E-value: 2.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 697 HRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQT 776
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 777 KKWQAlGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLrNLHHSIQVMKELQRIGVGIAIDDF 856
Cdd:COG4943 348 GDLLA-ADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDF 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 857 GSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALY 936
Cdd:COG4943 426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
|
250
....*....|
gi 1050292024 937 RPATAEELSA 946
Cdd:COG4943 506 KPLPAEEFIA 515
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
517-939 |
6.99e-74 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 256.41 E-value: 6.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 517 KAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKlAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLP 596
Cdd:PRK11829 223 DAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHF-HLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCID 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 597 IEAHLGRFHGDKFCLLLTGQIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRA 676
Cdd:PRK11829 302 DSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 677 KRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAE 756
Cdd:PRK11829 382 HHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 757 ETGLIHEIGRWVLETACKQTKKWQALGnQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHH 836
Cdd:PRK11829 462 EEGMMVPLGNWVLEEACRILADWKARG-VSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 837 SIQVMKELQRIGVGIAIDDFGSGYASFSYL---KNLPANILKIDRSFIKQIhtnSSDIAIVKAMITMGHGLGMKIVAEGV 913
Cdd:PRK11829 541 ALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGV 617
|
410 420
....*....|....*....|....*.
gi 1050292024 914 ETDEHLQLLKMLRCHYVQGYaLYRPA 939
Cdd:PRK11829 618 ETEEQRQWLLEHGIQCGQGF-LFSPP 642
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
516-946 |
9.45e-73 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 253.10 E-value: 9.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 516 KKAEEKISYLAYYDPDTHLPNRTKFMEIiteqLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVL 595
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMAL----LEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 596 PIEAHLGRFHGDKFCLLLTGQIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDgVDAHSLLKNADIAVSR 675
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGD-LTAEQLYSRAISAAFT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 676 AKRSGGNRVQFYSAKMNDETLHRLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLA 755
Cdd:PRK13561 376 ARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 756 EETGLIHEIGRWVLETACKQTKKWQALG-NQQLSifVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNL 834
Cdd:PRK13561 456 ESCGLMVTVGHWVLEESCRLLAAWQERGiMLPLS--VNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 835 HHSIQVMKELQRIGVGIAIDDFGSGYASFSYL---KNLPANILKIDRSFIKQIHTNSSdiaIVKAMITMGHGLGMKIVAE 911
Cdd:PRK13561 534 HAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAE 610
|
410 420 430
....*....|....*....|....*....|....*
gi 1050292024 912 GVETDEHLQLLKMLRCHYVQGYALYRPATAEELSA 946
Cdd:PRK13561 611 GVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
394-938 |
2.85e-72 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 259.60 E-value: 2.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 394 EMERLHVcgqISQSLfehnTDIVYSTDLHGNLTNVNPAFEKVLGYKREE--------VLH-TN-----ALKYIHPNDVRR 459
Cdd:PRK09776 534 EKERLHI---TLDSI----GEAVVCTDMAMKVTFMNPVAEKMTGWTQEEalgvplltVLHiTFgdngpLMENIYSCLTSR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 460 --------VSMHFYRALRGKIQYynleiptkSGKPLLfqiknvpiVVDGKKVGIYGIGRDITEQKKAEEKISYLAYYDPD 531
Cdd:PRK09776 607 saayleqdVVLHCRSGGSYDVHY--------SITPLS--------TLDGENIGSVLVIQDVTESRKMLRQLSYSASHDAL 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 532 THLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFHGDKFCL 611
Cdd:PRK09776 671 THLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 612 LLtgqihSEKVFETATRIAKEMTKPI-----VYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGNRVQF 686
Cdd:PRK09776 751 LL-----PDCNVESARFIATRIISAIndyhfPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTV 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 687 YSAKMNDETLHRLEMER--YLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEI 764
Cdd:PRK09776 826 YEPQQAAAHSEHRALSLaeQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHAL 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 765 GRWVLETACKQTKkwQALGNQQLSIFVNVSAAQFQHESFINDVKRALAQSQLSPDCLHLELTENSMLRNLHHSIQVMKEL 844
Cdd:PRK09776 906 DRRVIHEFFRQAA--KAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKL 983
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 845 QRIGVGIAIDDFGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKM 924
Cdd:PRK09776 984 RLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSG 1063
|
570
....*....|....
gi 1050292024 925 LRCHYVQGYALYRP 938
Cdd:PRK09776 1064 IGVDLAYGYAIARP 1077
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
510-687 |
8.62e-58 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 199.82 E-value: 8.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 510 RDITEQKKAEEKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQ 589
Cdd:COG2199 98 EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVAR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 590 RILHVLPIEAHLGRFHGDKFCLLLTGqIHSEKVFETATRIAKEMTK-PIVYDGKEFFITASIGISFYPSDGVDAHSLLKN 668
Cdd:COG2199 178 RLRASLRESDLVARLGGDEFAVLLPG-TDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRR 256
|
170
....*....|....*....
gi 1050292024 669 ADIAVSRAKRSGGNRVQFY 687
Cdd:COG2199 257 ADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
527-685 |
8.73e-56 |
|
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: 189.69 E-value: 8.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 527 YYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFHG 606
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050292024 607 DKFCLLLTGqIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGNRVQ 685
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
524-687 |
6.02e-48 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 167.81 E-value: 6.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 524 YLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGR 603
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 604 FHGDKFCLLLTGqIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGNR 683
Cdd:smart00267 81 LGGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1050292024 684 VQFY 687
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
526-683 |
1.81e-45 |
|
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: 160.88 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 526 AYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFH 605
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 606 GDKFCLLL--TGQIHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGNR 683
Cdd:pfam00990 81 GDEFAILLpeTSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
698-944 |
7.09e-45 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 170.17 E-value: 7.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 698 RLEMERYLRKALEKRELFLCYQPIVDITTGKIVGNEALIRWRHPKLGLVRPDEFISLAEETGLIHEIGRWVLETACKQTK 777
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 778 KWQALGNQQLSIFVNVSAAQFQHESFINDVKRALAQsqLSPDCLH--LELTENSMLRNlHHSIQVMKELQRIGVGIAIDD 855
Cdd:PRK10551 341 ELQKVLPVGAKLGINISPAHLHSDSFKADVQRLLAS--LPADHFQivLEITERDMVQE-EEATKLFAWLHSQGIEIAIDD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 856 FGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYAL 935
Cdd:PRK10551 418 FGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWI 497
|
....*....
gi 1050292024 936 YRPATAEEL 944
Cdd:PRK10551 498 SRPLPLEDF 506
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
525-684 |
3.20e-36 |
|
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: 134.39 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 525 LAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRF 604
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 605 HGDKFCLLLTGQIhSEKVFETATRIAKEM-TKPIVYDGKE-FFITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSGGN 682
Cdd:TIGR00254 81 GGEEFVVILPGTP-LEDALSKAERLRDAInSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
..
gi 1050292024 683 RV 684
Cdd:TIGR00254 160 RV 161
|
|
| FIST |
COG3287 |
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms] ... |
42-358 |
4.66e-32 |
|
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms];
Pssm-ID: 442517 [Multi-domain] Cd Length: 382 Bit Score: 129.30 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 42 ELGKIIELLRRCLPQAQLLGMT-----CGDPFHPGGrfnICFTVF--EKVSVHSVLLPYKEfANELELAAYISDALI--- 111
Cdd:COG3287 46 DLEALLAALRAAFPGAPIIGCStageiSPGGVLEGS---VVLLAFsfDKFRVGVAVGDGLS-DDSREAGRELARRLLaal 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 112 --TEETNLLLLFTDQES-NFHSLIRHIPLVNDQTVIIAG-------RMKEGgRLFSHEGIVADGIVAISFnGSSLRVQLS 181
Cdd:COG3287 122 gpDPDLRFALLLSDGLSgNEEELLEGLYSALGPDVPIFGgsagddlRFEKT-YVFHNGEVLSDAAVVALL-GTSLPVGVG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 182 HPFLWEPVGATFRVTKCSGNKLYELDGKKAARLLEHYLGKEfIERLPFSGAEFPFVVEKNGHKQCL-SVAKANKDGSIEI 260
Cdd:COG3287 200 SSHGWKPTGPEMVVTKAEGRVVYEIDGEPAAEVYARYLGDD-AEELPASFLLFPLGVRIGGGEYLVrSPLAVEEDGSLTF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 261 NGRVDPGEMVKISFVPLPSLFWHMSDKLTKLAK----KPAEAIFFY---QSMAMEGYVSLALQQITATLEqiSPTFTPFS 333
Cdd:COG3287 279 AGDIPEGSVLRLMEGNPDDLIEAAERAAEAALArlggKPEAALLFDcvgRRLVLGQRVEEELEAVSELLG--APVAGFYT 356
|
330 340
....*....|....*....|....*.
gi 1050292024 334 FAELVTKDRYAPM-HPATFSMVALSE 358
Cdd:COG3287 357 YGEIGPFGGGGNQhHNQTLTGVAFGE 382
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
525-684 |
1.29e-24 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 108.45 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 525 LAYYDPDTHLPNRtKFMEIITEQL-EKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGR 603
Cdd:PRK09581 291 MAVTDGLTGLHNR-RYFDMHLKNLiERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 604 FHGDKFCLLLTGqIHSEKVFETATRIAKEM-TKP-IVYDGKEFF-ITASIGISFYPSDGVDAHSLLKNADIAVSRAKRSG 680
Cdd:PRK09581 370 YGGEEFVVVMPD-TDIEDAIAVAERIRRKIaEEPfIISDGKERLnVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTG 448
|
....
gi 1050292024 681 GNRV 684
Cdd:PRK09581 449 RNRV 452
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
406-643 |
4.67e-22 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 100.82 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKI-QYYNLEIPTKSG 484
Cdd:COG5809 18 RSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESrDELEFELRHKNG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 485 KPLLFQIKNVPIVVD-GKKVGIYGIGRDITEQKKAEekisylayydpdthlpnrtkfmeiitEQLEKAKRKNRKLA---- 559
Cdd:COG5809 98 KRLEFSSKLSPIFDQnGDIEGMLAISRDITERKRME--------------------------EALRESEEKFRLIFnhsp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 560 --VVFIDLD-RFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFHGDKFCLLLTGQIHSEKVFETA---TRIAKEM 633
Cdd:COG5809 152 dgIIVTDLDgRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKdgrWRLLEAS 231
|
250
....*....|
gi 1050292024 634 TKPIVYDGKE 643
Cdd:COG5809 232 GAPIKKNGEV 241
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
526-932 |
6.42e-22 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 101.48 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 526 AYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVL---PiEAHLG 602
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmryP-GALLA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 603 RFHGDKFCLLLTGQihSEKvfeTATRIAKEMTK-------PIVYDGKEFFitaSIGISFYPSdGVDAHSLLKNADIAVSR 675
Cdd:PRK11059 307 RYSRSDFAVLLPHR--SLK---EADSLASQLLKavdalppPKMLDRDDFL---HIGICAYRS-GQSTEQVMEEAEMALRS 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 676 AKRSGGNRVQFYsAKMNDEtlhrlEMER-------YLRKALEKRELFLCYQPIVDiTTGKIVGNEALIRWRHPKLGLVRP 748
Cdd:PRK11059 378 AQLQGGNGWFVY-DKAQLP-----EKGRgsvrwrtLLEQTLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRDGQGELLSA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 749 DEFISLAEETGLIHEIGRWVLETACKQTKKWQalgNQQLSIfvNVSAAQFQHESFINDVKRALAQ---SQLSpdCLHLEL 825
Cdd:PRK11059 451 ELFMPMVQQLGLSEQYDRQVIERVLPLLRYWP---EENLSI--NLSVDSLLSRAFQRWLRDTLLQcprSQRK--RLIFEL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 826 TENSMLRNLHHSIQVMKELQRIGVGIAIDDFGSGYASFSYLKNLPANILKIDRSFIKQIHTNSSDIAIVKAMITMGHGLG 905
Cdd:PRK11059 524 AEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTE 603
|
410 420
....*....|....*....|....*..
gi 1050292024 906 MKIVAEGVETDEHLQLLKMLRCHYVQG 932
Cdd:PRK11059 604 TQVFATGVESREEWQTLQELGVSGGQG 630
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
407-522 |
1.51e-21 |
|
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: 90.81 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 407 SLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRG--KIQYYNLEIPTKSG 484
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGepEPVSEERRVRRKDG 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1050292024 485 KPLLFQIKNVPIVVDGKKVGIYGIGRDITEQKKAEEKI 522
Cdd:TIGR00229 87 SEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
406-605 |
1.86e-21 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 95.09 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALR-GKIQYYNLEIPTKSG 484
Cdd:COG2202 14 RALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAgGGVWRGELRNRRKDG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 485 KPLLFQIKNVPIV-VDGKKVGIYGIGRDITEQKKAEekisylayydpdthlpnrtkfmeiitEQLEKAKRKNRKL----- 558
Cdd:COG2202 94 SLFWVELSISPVRdEDGEITGFVGIARDITERKRAE--------------------------EALRESEERLRLLvenap 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1050292024 559 -AVVFIDLD-RFKRINDS---IGHYAGDEILKQVVQRILHVLPIEAHLGRFH 605
Cdd:COG2202 148 dGIFVLDLDgRILYVNPAaeeLLGYSPEELLGKSLLDLLHPEDRERLLELLR 199
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
406-522 |
2.83e-21 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 94.32 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKIQYYNLEIPTKSGK 485
Cdd:COG2202 140 RLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGD 219
|
90 100 110
....*....|....*....|....*....|....*....
gi 1050292024 486 PLLFQIKN--VPIVVDGKKVGIYGIGRDITEQKKAEEKI 522
Cdd:COG2202 220 GRWVWVEAsaVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
528-688 |
2.99e-19 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 89.36 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 528 YDPDTHLPNRTKFMEIITEQLekAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRI-LHVLPIEAhLGRFHG 606
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQL--RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLaSWTRDYET-VYRYGG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 607 DKFCLLLtgqihSEKVFETATRIAKEM-----TKPIVYDGKEFFITASIGIS-FYPSDGVDahSLLKNADIAVSRAKRSG 680
Cdd:PRK09894 208 EEFIICL-----KAATDEEACRAGERIrqliaNHAITHSDGRINITATFGVSrAFPEETLD--VVIGRADRAMYEGKQTG 280
|
....*...
gi 1050292024 681 GNRVQFYS 688
Cdd:PRK09894 281 RNRVMFID 288
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
390-522 |
3.74e-19 |
|
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: 91.96 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 390 ATSREM-ERLHVCGQISQS------LFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSM 462
Cdd:COG5809 121 AISRDItERKRMEEALRESeekfrlIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAA 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1050292024 463 HFYRALRGKiQYYNLEIP--TKSGKPLLFQIKNVPIVVDGKKVGIYGIGRDITEQKKAEEKI 522
Cdd:COG5809 201 FISQLLKDG-GIAQGEVRfwTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELL 261
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
520-684 |
3.51e-17 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 86.22 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 520 EKISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEA 599
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 600 HLGRFHGDKFCLLLTGqIHSEKVFETATRI-----AKEMtkpIVYDGKEFFITASIGISFYPSDG-VDAHSLLKNADIAV 673
Cdd:PRK15426 472 VAGRVGGEEFCVVLPG-ASLAEAAQVAERIrlrinEKEI---LVAKSTTIRISASLGVSSAEEDGdYDFEQLQSLADRRL 547
|
170
....*....|.
gi 1050292024 674 SRAKRSGGNRV 684
Cdd:PRK15426 548 YLAKQAGRNRV 558
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
406-520 |
1.27e-15 |
|
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: 80.93 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHF-YRALRGKIQYYNLEIPTKSG 484
Cdd:COG5805 160 QTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIeSITEVWQEFIIEREIITKDG 239
|
90 100 110
....*....|....*....|....*....|....*..
gi 1050292024 485 KPLLFQIKNVPIV-VDGKKVGIYGIGRDITEQKKAEE 520
Cdd:COG5805 240 RIRYFEAVIVPLIdTDGSVKGILVILRDITEKKEAEE 276
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
390-559 |
7.53e-14 |
|
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: 74.81 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 390 ATSREMERLHvcgQISQSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVsmhfyraLR 469
Cdd:COG3829 1 AEELELKELE---EELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEV-------LK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 470 GKIQYYNlEIPTKSGKPLLFQIKNVPIVVDGKKVGIYGIGRDITEQKKAEEKISYLAYydpDTHLPNRTKFMEIITE--Q 547
Cdd:COG3829 71 TGKPVTG-VIQKTGGKGKTVIVTAIPIFEDGEVIGAVETFRDITELKRLERKLREEEL---ERGLSAKYTFDDIIGKspA 146
|
170
....*....|..
gi 1050292024 548 LEKAKRKNRKLA 559
Cdd:COG3829 147 MKELLELAKRVA 158
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
406-522 |
2.66e-13 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 72.57 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKIQYYNLEIPTKSGK 485
Cdd:COG3852 10 RAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRRKDGE 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 1050292024 486 PLLFQIKNVPIVVDGKKVGIYGIGRDITEQKKAEEKI 522
Cdd:COG3852 90 ERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLEREL 126
|
|
| FIST |
smart00897 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
41-209 |
2.73e-13 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 214894 Cd Length: 196 Bit Score: 69.65 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 41 SELGKIIELLRRCLPQA-QLLGMTCGDPFHPG------GRFNICFTVFEKVSVHSVLLPYKEFANEL---ELAAYISDAL 110
Cdd:smart00897 13 YDAEALLAALRERFPGAtPIVGCSTAGEITTGvvqefeDEPALSVMLFELPLVSFDVFSLVDPLPDLvagLLLAALLAAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 111 ITEETNLLLLFTDQ-ESNFHSLIRHIPLVNDQTVIIAG-----RMKEGGRLFSHEGIVADGIVAISFnGSSLRVQLSHPF 184
Cdd:smart00897 93 DPRNTFALLLLDDLsSSNEEELLEGLDEALPEGIPIGGgsagdNLRFQETYVFTNGRVHSGAVVVAF-GGGLRFGTGVTQ 171
|
170 180
....*....|....*....|....*
gi 1050292024 185 LWEPVGATFRVTKCSGNKLYELDGK 209
Cdd:smart00897 172 GWRPIGPPFVVTKAEGNVVYELDGE 196
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
513-685 |
1.25e-12 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 70.63 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 513 TEQKKAEEK--ISYLAYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKLAVVFIDLDRFKRINDSIGHYAGDEILKQVVQR 590
Cdd:PRK10245 190 TATKLAEHKrrLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 591 ILHVLPIEAHLGRFHGDKFCLLLTGQiHSEKVFETATRIAKEMTKPIVYDGKEFFITASIGISFYPSDGVDAHSLLKNAD 670
Cdd:PRK10245 270 LQITLRGSDVIGRFGGDEFAVIMSGT-PAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSAD 348
|
170
....*....|....*
gi 1050292024 671 IAVSRAKRSGGNRVQ 685
Cdd:PRK10245 349 LALYKAKNAGRNRTE 363
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
526-683 |
1.65e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 70.42 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 526 AYYDPDTHLPNRTKFMEIITEQLEKAKRKNRKlAVVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVLPIEAHLGRFH 605
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 606 GDKFCLLLTGqIHSE-KVFETATRIAKEMTKPI-VYDGKEFFITASIGISFyPSDGVDAHSLLKNADIAVSRAKRSGGNR 683
Cdd:PRK09966 327 GDEFAMVLYD-VQSEsEVQQICSALTQIFNLPFdLHNGHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAKHQRAEK 404
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
407-523 |
1.18e-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: 68.22 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 407 SLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKIQYYNLEIPTKSGKP 486
Cdd:COG5805 38 TILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDGEL 117
|
90 100 110
....*....|....*....|....*....|....*..
gi 1050292024 487 LLFQIKNVPIVVDGKKVGIYGIgRDITEQKKAEEKIS 523
Cdd:COG5805 118 IYVEVKLFPIYNQNGQAAILAL-RDITKKKKIEEILQ 153
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
414-512 |
1.50e-11 |
|
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: 61.88 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 414 DIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRV-SMHFYRALRGKIQYYNLEIPTKSGKPLLFQIK 492
Cdd:cd00130 3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELrERLENLLSGGEPVTLEVRLRRKDGSVIWVLVS 82
|
90 100
....*....|....*....|.
gi 1050292024 493 NVPIV-VDGKKVGIYGIGRDI 512
Cdd:cd00130 83 LTPIRdEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
406-512 |
1.73e-11 |
|
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: 62.05 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALR--GKIQYYNLEIPTKS 483
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLqgEESRGFEVSFRVPD 83
|
90 100 110
....*....|....*....|....*....|
gi 1050292024 484 GKPLLFQIKNVPIV-VDGKKVGIYGIGRDI 512
Cdd:pfam00989 84 GRPRHVEVRASPVRdAGGEILGFLGVLRDI 113
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
422-514 |
4.77e-10 |
|
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: 57.09 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 422 HGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKIQyYNLEIPTKSGKPLLFQIKNVPIVVDGK 501
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVRE-FEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 1050292024 502 KV-GIYGIGRDITE 514
Cdd:pfam13426 80 ELvGIIAILRDITE 93
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
712-938 |
8.93e-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: 61.74 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 712 RELFLCYQPIVDiTTGKIVGNEalIRWRHpklGLVRPDEFISLAEET-----GLIHEIGrwvLETAckqtkkwqaLGNQQ 786
Cdd:COG3434 2 MDVFVARQPILD-RDQRVVGYE--LLFRS---GLENSAPDVDGDQATarvllNAFLEIG---LDRL---------LGGKL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 787 LsiFVNVSaaqfqHESFINDVKRALAQSQLSpdclhLELTENSMLRNLHhsIQVMKELQRIGVGIAIDDF--GSGYASFs 864
Cdd:COG3434 64 A--FINFT-----EELLLSDLPELLPPERVV-----LEILEDVEPDEEL--LEALKELKEKGYRIALDDFvlDPEWDPL- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1050292024 865 ylknLP-ANILKIDrsfikqihTNSSDIAIVKAMITMGHGLGMKIVAEGVETDEHLQLLKMLRCHYVQGYALYRP 938
Cdd:COG3434 129 ----LPlADIIKID--------VLALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| FIST |
pfam08495 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
156-209 |
1.21e-09 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 462495 Cd Length: 126 Bit Score: 57.21 E-value: 1.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1050292024 156 FSHEGIVADGIVAISFNGSSLRVQ--LSHPflWEPVGATFRVTKCSGNKLYELDGK 209
Cdd:pfam08495 73 LFNGEVYSDGAVAVALYGDALKVGvgVSQG--WRPIGPPFVVTKADGNRVYELDGR 126
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
406-460 |
4.23e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 53.56 E-value: 4.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRV 460
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERV 58
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
428-508 |
8.02e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 47.72 E-value: 8.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 428 VNPAFEKVLGYKREEVLHTNA--LKYIHPNDVRRVSMHFYRALRGKiQYYNLE--IPTKSGKPLLFQIKNVPI-VVDGKK 502
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKGEswLDLVHPDDRERVREALWEALKGG-EPYSGEyrIRRKDGEYRWVEARARPIrDENGKP 82
|
....*.
gi 1050292024 503 VGIYGI 508
Cdd:pfam08447 83 VRVIGV 88
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
409-516 |
1.05e-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. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 48.18 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 409 FEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVSMHFYRALRGKIQYYNLEIPTKSGKPLL 488
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERH 80
|
90 100
....*....|....*....|....*....
gi 1050292024 489 FQIKNVPIV-VDGKKVGIYGIGRDITEQK 516
Cdd:pfam08448 81 YELRLTPLRdPDGEVIGVLVISRDITERR 109
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
379-522 |
7.17e-05 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 46.50 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 379 QGVMTLAHLLSATSREM--ErlhvCGQIS-------QSLFE---HNTDIVYST-------DLHGNLTNVNPAFEKVLGYK 439
Cdd:PRK11360 223 DGLSTLENDLSTRLPPLpgE----LGEISqainnlaQALREtrsLNELILESIadgviaiDRQGKITTMNPAAEVITGLQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 440 REEVLhtnalkYIHPNDVRRVSMHFY----RALRGKIQYYNLEI--PTKSGKPLLFQIKNVPIVVDGKKVGIYGIGRDIT 513
Cdd:PRK11360 299 RHELV------GKPYSELFPPNTPFAspllDTLEHGTEHVDLEIsfPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLT 372
|
....*....
gi 1050292024 514 EQKKAEEKI 522
Cdd:PRK11360 373 ERKRLQRRV 381
|
|
| FIST_C |
pfam10442 |
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal ... |
211-336 |
1.67e-04 |
|
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 463094 Cd Length: 135 Bit Score: 42.68 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 211 AARLLEHYLGKEFIERLPFSGAEFPF-VVEKNGHKQCLSVAKAN-KDGSIEINGRVDPGEMVKISFVPLPSLFWHMSDKL 288
Cdd:pfam10442 1 ALEVYKEYLGGEEDEELPASALEFPLgVVVGGGDYLVRSPLGVDpEDGSLAFAGDVPEGSVVQLMLRDADDLIEAAERAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1050292024 289 TKLAKKPAEAIFFY----QSMAMEGYVSLALQQITATLEQISPTFTPFSFAE 336
Cdd:pfam10442 81 EAALANPPEGALLFscagRGLGLGERFDEELEAIREALGDGVPLAGFYTYGE 132
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
388-521 |
1.82e-04 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 44.95 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 388 LSATSREMERLHvcgQISQSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRRVsmhFYRA 467
Cdd:COG5000 78 LKEQREELEERR---RYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAEL---LREA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1050292024 468 LRGKIQyynLEIPTKSGKPLLFQIKNVPIVVDGKKVGIygigRDITEQKKAEEK 521
Cdd:COG5000 152 LERGWQ---EEIELTRDGRRTLLVRASPLRDDGYVIVF----DDITELLRAERL 198
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
560-653 |
4.47e-04 |
|
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: 41.19 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 560 VVFIDLDRFKRINDSIGHYAGDEILKQVVQRILHVlpIEAHLG---RFHGDKFcLLLTGQIHSekvfETATRIAKEMTKP 636
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSL--IRRSGDlkiKTIGDEF-MVVSGLDHP----AAAVAFAEDMREA 76
|
90
....*....|....*....
gi 1050292024 637 I--VYDGKEFFITASIGIS 653
Cdd:cd07556 77 VsaLNQSEGNPVRVRIGIH 95
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
406-459 |
1.06e-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: 38.30 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1050292024 406 QSLFEHNTDIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNALKYIHPNDVRR 459
Cdd:pfam13188 4 RALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDA 57
|
|
| FIST |
COG4398 |
Small ligand-binding sensory domain FIST [Signal transduction mechanisms]; |
146-216 |
1.64e-03 |
|
Small ligand-binding sensory domain FIST [Signal transduction mechanisms];
Pssm-ID: 443524 [Multi-domain] Cd Length: 386 Bit Score: 41.74 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1050292024 146 AGRMKEGGRLFSHEGIVADGIVAISFNGS-SLRVQLSHPFlwEPVGATFRVTKCSGNKLYELDGKKA-ARLLE 216
Cdd:COG4398 156 SGRGAPGQNLFAAGEVYEGGLVGVAFSGNvTLETRVSQGC--RPIGPPHQVTEAERNVILELDGRPAlDVLLE 226
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
601-677 |
2.33e-03 |
|
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: 39.89 E-value: 2.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050292024 601 LGRFHGDKFCLLLTGqIHSEKVFETATRIAKEMTKPivydgKEFFITASIGISfypsdgvdAHSLLKNADiAVSRAK 677
Cdd:COG3706 118 VARYGGEEFAILLPG-TDLEGALAVAERIREAVAEL-----PSLRVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
414-548 |
3.62e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 41.08 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 414 DIVYSTDLHGNLTNVNPAFEKVLGYKREEVLHTNAlKYIHPNDV--------RRVSMHfYRALRGKIQyynLEIPtkSGK 485
Cdd:PRK11091 166 DLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTP-KDVYSPEAaekvietdEKVFRH-NVSLTYEQW---LDYP--DGR 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050292024 486 PLLFQIKNVP-IVVDGKKVGIYGIGRDITEQKKAEEKISYlAYYDpdthlpnRTKFMEIITEQL 548
Cdd:PRK11091 239 KACFELRKVPfYDRVGKRHGLMGFGRDITERKRYQDALEK-ASRD-------KTTFISTISHEL 294
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
548-654 |
9.39e-03 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 37.55 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050292024 548 LEKAKRKNRKLAVVFIDLDRFKRINDSIGhyagdEILKQVVQRILHVLPIeahlgrfhgDKFCLLLTGqihSEKVFETAT 627
Cdd:pfam00817 52 VFEAKKLCPNLIVVPPDLELYRRASRKIF-----EILRRFSTPKVEQASI---------DEAFLDLTG---LEKLFGAEE 114
|
90 100
....*....|....*....|....*..
gi 1050292024 628 RIAKEMTKPIVydgKEFFITASIGISF 654
Cdd:pfam00817 115 ALAKRLRREIA---EETGLTCSIGIAP 138
|
|
| |
