|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
286-956 |
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: 663.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 286 ADINMEVYEDSQYSAENLLYDDNGIPDMRNAPRSDSLALTQSITVFGHTWSLYFTTRPAFHAAFDQNKPLRFLGFGTIFS 365
Cdd:COG5001 3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 366 VLLSALMWLFTKQRRRALVQASYMQEEIVERKKAEEELRLAALMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAV 445
Cdd:COG5001 83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 446 GRNCSLHKANNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVHRYVAQTSD-----ITQKKA 520
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLaiarlITERKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 521 SEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRE 600
Cdd:COG5001 243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 601 SDTVARLGGDEFTVILSELVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAK 680
Cdd:COG5001 323 GDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 681 NLGGNRFSRFTQDLQEAAETRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEE 760
Cdd:COG5001 403 AAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 761 SRLIHDINDWVFHEATRELASWRKQLVPEFQISVNVSPVELRQNRekVGAHWIRHLQALGLPGKSLAIEITESILLNAES 840
Cdd:COG5001 483 TGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPD--LVDRVRRALAETGLPPSRLELEITESALLEDPE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 841 NVTDKLHLFRDAGIEVSIDDFGTGYSSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVET 920
Cdd:COG5001 561 EALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVET 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1833325744 921 QAQLDLLTAYGCDYAQGWLYSKAVTAPDFFALLLKN 956
Cdd:COG5001 641 EEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| CHASE1 |
COG3614 |
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms]; |
29-633 |
4.94e-122 |
|
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442832 [Multi-domain] Cd Length: 588 Bit Score: 383.66 E-value: 4.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 29 MRSAIKSISRqisavilnWPVAWIILFISLLLTFLVWRSAQEDLARLQQVQLESRVSKVSDAVLRRVQAYEQVLRGGVGL 108
Cdd:COG3614 1 MSRSRSLLRR--------RLLPLLVLLLGLLLTALAWWAVRRAEEQRARARFERLADELASALEERLDAYEQVLRGLAGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 109 LAASDVVTRSEFQDYIASLNVKEHYPAIQGIGYAVHIPAADLELHKRKMRAEGFPDYDIYPTGERDQYTSIIYLEPFNLR 188
Cdd:COG3614 73 FAASDDVTRAEFRRYVASLDLLRRYPGIQGLGWAPRVPAAERAAFEAAARAEGFPDFRIRPAGERDEYFPITYIEPLDAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 189 NQRAFGFDMFSEPKRRAAMEVARDTGNTAVSTKVTLVQESGEkmQASILMYLPFYKNGKPRATLEERRSNLQGYVYSPFR 268
Cdd:COG3614 153 NRRALGFDMASEPVRRAAMERARDTGRPAASGPVTLVQETDG--QPGFLLYLPVYRGGAPPDTVAERRAALRGFVYAPFR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 269 LDKLMGGILNEAQTGvkaDINMEVYEDSQYSAENLLYDDNGIPDMRNAPRsdsLALTQSITVFGHTWSLYFTTRPAFHAA 348
Cdd:COG3614 231 MDDLLAGVLGRLADR---DLDLRLYDGTDPGPPQLLYDSSPAAPAAAAPA---LSATRTLEVAGRTWTLEFRPTPAFEAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 349 FDQNKPLRFLGFGTIFSVLLSALMWLFTKQRRRA--LVQASYMQEEIVERKKAEEELRLAALMYQHSSEAMSVADSTGAI 426
Cdd:COG3614 305 LRSWLPWLVLLGGLLLSLLLALLLLSLARRRRRAeaLAAARAALRALRAAELRLRALLRRALLALLRNALALALLLAALL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 427 VSINPAYtkvtgytLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVH 506
Cdd:COG3614 385 LLLARLL-------LLLAALLLLLARALSAADLLLLQADLLLLRLLLLLRRRLLLVRDLRLGRGLGLGVVLLLDAILLDL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 507 RYVAQTSDITQKKASEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVL 586
Cdd:COG3614 458 LALAELELAAARAEVALAEALLALLVVLLLALLLALLRLLLALAELAATAAREAAGAALLLDREAALLDAALEALLDLLG 537
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1833325744 587 LVEAARRIATCVRESDTVARLGGDEFTVILSELVDINSAEHIAQNII 633
Cdd:COG3614 538 LLVLLLLAELLLRLGALLLGRALLGGVGAGEGLVIIAELAALELELL 584
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
378-953 |
1.44e-120 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 379.51 E-value: 1.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 378 QRRRALVQASYMQEEIVERKKAEEELRLAALMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNH 457
Cdd:COG2200 4 LLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 458 DRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVHRYVAQTSDITQKKASEKLIWQQANYDLLTGL 537
Cdd:COG2200 84 ALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 538 PNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDEFTVILS 617
Cdd:COG2200 164 LRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 618 ELVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNlGGNRFSRFTQDLQEA 697
Cdd:COG2200 244 LLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAG-GGRGRVVFFAAAEAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 698 AETRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATR 777
Cdd:COG2200 323 ARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 778 ELASWRKQLVPeFQISVNVSPVELRQnrEKVGAHWIRHLQALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAGIEVS 857
Cdd:COG2200 403 QLARWPERGLD-LRLSVNLSARSLLD--PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 858 IDDFGTGYSSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQG 937
Cdd:COG2200 480 LDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQG 559
|
570
....*....|....*.
gi 1833325744 938 WLYSKAVTAPDFFALL 953
Cdd:COG2200 560 YLFGRPLPLEELEALL 575
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
411-949 |
7.78e-111 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 356.68 E-value: 7.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 411 QHSSEAMSVA---DSTGAIVSINPAYTKVTGYTLEDAVGRNC-----SLHKANNHDRK---FFRAmwdeinaTGHWQGEI 479
Cdd:PRK10060 115 QVVSEANSVIvilDSRGNIQRFNRLCEEYTGLKEHDVIGQSVfklfmSRREAAASRRNirgFFRS-------GNAYEVER 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 480 WNWRKNGEAYLEW--------TTVNTIYLddgsvhryVAQTSDIT-QKKASEKLIwQQANYDLLTGLPNRHMFHDRLERA 550
Cdd:PRK10060 188 WIKTRKGQRLFLFrnkfvhsgSGKNEIFL--------ICSGTDITeERRAQERLR-ILANTDSITGLPNRNAIQELIDHA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 551 IkkSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDEFTViLSELVDINSAEHIAQ 630
Cdd:PRK10060 259 I--NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLV-LASHTSQAALEAMAS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 631 NIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGNRFSRFTQDLQEAAETRLRMMRDLRN 710
Cdd:PRK10060 336 RILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 711 ALAANQLEVYYQPIVEIaTGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATRELASWRKQLVpEF 790
Cdd:PRK10060 416 ALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 791 QISVNVSPVELRQnrEKVGAHWIRHLQALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAGIEVSIDDFGTGYSSLSY 870
Cdd:PRK10060 494 RVAVNVSARQLAD--QTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQ 571
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833325744 871 LKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKAVTAPDF 949
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
706-948 |
2.34e-104 |
|
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: 324.50 E-value: 2.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 706 RDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATRELASWRKQ 785
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 786 LvPEFQISVNVSPVELRQNRekVGAHWIRHLQALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAGIEVSIDDFGTGY 865
Cdd:cd01948 81 G-PDLRLSVNLSARQLRDPD--FLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 866 SSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKAVT 945
Cdd:cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 1833325744 946 APD 948
Cdd:cd01948 238 AEE 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
515-948 |
2.05e-94 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 316.33 E-value: 2.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 515 ITQKKaSEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRrsgfPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRI 594
Cdd:PRK11359 363 LEQEK-SRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRF 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 595 ATCVRESDTVARLGGDEFtVILSELVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLypDDSLDVETLIKNADQ 674
Cdd:PRK11359 438 REKLKPDQYLCRIEGTQF-VLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHN 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 675 AM-YVAKNlGGNRFSRFTQDLQEAAETRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQ 753
Cdd:PRK11359 515 AMdYIRKN-GGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSR 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 754 FIPLAEESRLIHDINDWVFHEATRELASWRKQLVPEFQISVNVSPVELRQN---REKVGAhwirhLQALGLPGKSLAIEI 830
Cdd:PRK11359 594 FIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNqlpNQVSDA-----MQAWGIDGHQLTVEI 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 831 TESILLNAESNVTDKLHLFRDAGIEVSIDDFGTGYSSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLG 910
Cdd:PRK11359 669 TESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLN 748
|
410 420 430
....*....|....*....|....*....|....*...
gi 1833325744 911 LKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKAVTAPD 948
Cdd:PRK11359 749 LTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
705-946 |
9.16e-89 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 283.34 E-value: 9.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 705 MRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATRELASWRK 784
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 785 QLVPEFQISVNVSPVELRQNREKVgahWIRH-LQALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAGIEVSIDDFGT 863
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVP---RVLElLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 864 GYSSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKA 943
Cdd:smart00052 158 GYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
...
gi 1833325744 944 VTA 946
Cdd:smart00052 238 LPL 240
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
701-958 |
8.87e-85 |
|
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: 282.58 E-value: 8.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 701 RLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATRELA 780
Cdd:COG4943 269 RLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 781 SWRKQlVPEFQISVNVSPVELRqnREKVGAHWIRHLQALGLPGKSLAIEITESILLNAESnVTDKLHLFRDAGIEVSIDD 860
Cdd:COG4943 349 DLLAA-DPDFHISINLSASDLL--SPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAK-ARAVIAALREAGHRIAIDD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 861 FGTGYSSLSYLKKFDIDYLKVDQSFVHNLvdGTDD---KVLcEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQG 937
Cdd:COG4943 425 FGTGYSSLSYLQTLPVDILKIDKSFVDAI--GTDSansAVV-PHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQG 501
|
250 260
....*....|....*....|.
gi 1833325744 938 WLYSKAVTAPDFFALLLKNVK 958
Cdd:COG4943 502 WLFAKPLPAEEFIAWLAAQRA 522
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
705-943 |
2.88e-78 |
|
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: 254.93 E-value: 2.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 705 MRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATRELASWRK 784
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 785 QlvPEFQISVNVSPvelRQNREKVGAHWIRHL-QALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAGIEVSIDDFGT 863
Cdd:pfam00563 81 G--PDIKLSINLSP---ASLADPGFLELLRALlKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 864 GYSSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKA 943
Cdd:pfam00563 156 GYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
415-954 |
6.83e-77 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 273.09 E-value: 6.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 415 EAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNC----------------SLHKANNHDRKFFramwdeINatghwQGE 478
Cdd:PRK09776 547 EAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLltvlhitfgdngplmeNIYSCLTSRSAAY------LE-----QDV 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 479 IWNWRkNGEAYLEWTTVNTIYLDDGSVHRYVAQTSDITQKKASEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRRSG 558
Cdd:PRK09776 616 VLHCR-SGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTH 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 559 FPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDEFTVILSElVDINSAEHIAQNIIKQLAA 638
Cdd:PRK09776 695 QRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPD-CNVESARFIATRIISAIND 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 639 -PFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGNRFSRFTQDlQEAAETRLRMM---RDLRNALAA 714
Cdd:PRK09776 774 yHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQ-QAAAHSEHRALslaEQWRMIKEN 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 715 NQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATRELASWRKQlvPEFQISV 794
Cdd:PRK09776 853 QLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS--KGLSIAL 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 795 NVSPVELrqNREKVGAHWIRHLQALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAGIEVSIDDFGTGYSSLSYLKKF 874
Cdd:PRK09776 931 PLSVAGL--SSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAF 1008
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 875 DIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWlyskAVTAPDFFALLL 954
Cdd:PRK09776 1009 MADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGY----AIARPQPLDLLL 1084
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
534-956 |
7.24e-74 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 256.18 E-value: 7.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 534 LTGLPNRHMFHDRLERAIkkSRRSGFpmALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDEFT 613
Cdd:PRK13561 236 VSDLPNKALLMALLEQVV--ARKQTT--ALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 614 VILSELVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYpDDSLDVETLIKNADQAMYVAKNLGGNRFSRFTQD 693
Cdd:PRK13561 312 IIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 694 LQEAAETRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFH 773
Cdd:PRK13561 391 QMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 774 EATRELASWRKQLVpEFQISVNVSPVELRQnrekvgAHWIRHLQALG-----LPGkSLAIEITESILLNAESNVTDKLHL 848
Cdd:PRK13561 471 ESCRLLAAWQERGI-MLPLSVNLSALQLMH------PNMVADMLELLtryriQPG-TLILEVTESRRIDDPHAAVAILRP 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 849 FRDAGIEVSIDDFGTGYSSLSYLKKFD---IDYLKVDQSFVHNLvdgTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLD 925
Cdd:PRK13561 543 LRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRD 619
|
410 420 430
....*....|....*....|....*....|.
gi 1833325744 926 LLTAYGCDYAQGWLYSKAVTAPDFFALLLKN 956
Cdd:PRK13561 620 WLLKAGVGIAQGFLFARALPIEIFEERYLEE 650
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
535-951 |
4.02e-69 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 243.31 E-value: 4.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 535 TGLPNRHMFHDRLERAIKKS-RRSGFpmALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDEFT 613
Cdd:PRK11829 238 TELPNRSLFISLLEKEIASStRTDHF--HLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 614 VILSELVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGNRFSRFTQD 693
Cdd:PRK11829 316 VLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPH 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 694 LQEAAETRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFH 773
Cdd:PRK11829 396 LIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 774 EATRELASWRKQLVpEFQISVNVSPVELRQNRekVGAHWIRHLQALGLPGKSLAIEITESILLNAESNVTDKLHLFRDAG 853
Cdd:PRK11829 476 EACRILADWKARGV-SLPLSVNISGLQVQNKQ--FLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 854 IEVSIDDFGTGYSSLSYL---KKFDIDYLKVDQSFVHNLvdgTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAY 930
Cdd:PRK11829 553 LLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEH 629
|
410 420
....*....|....*....|.
gi 1833325744 931 GCDYAQGWLYSKAVTAPDFFA 951
Cdd:PRK11829 630 GIQCGQGFLFSPPLPRAEFEA 650
|
|
| CHASE |
pfam03924 |
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ... |
115-305 |
1.28e-65 |
|
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 427591 Cd Length: 184 Bit Score: 218.31 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 115 VTRSEFQDYIASLNvkEHYPAIQGIGYAVHIPAADLELHKRKMRAEGFPDYDIYPTGERDQYTSIIYLEPFNlRNQRAFG 194
Cdd:pfam03924 3 VDREEFRRYAASLL--LRRPGIQGLGWAPRVPAAERAAFEAAVRAEGFPDFTIRPAGDRDEYFPIIYIEPLA-GNNRALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 195 FDMFSEPKRRAAMEVARDTGNTAVSTKVTLVQESGEkmQASILMYLPFYKNGKPrATLEERRSNLQGYVYSPFRLDKLMG 274
Cdd:pfam03924 80 FDMASEPVRREAIERARDTGEPVLSGPVTLVQDGDG--QPGFLLYLPVYRGGPP-DTVAERRAALLGFVYAPFRIDDLLE 156
|
170 180 190
....*....|....*....|....*....|.
gi 1833325744 275 GILNEAQTGvkaDINMEVYEDSQYSAENLLY 305
Cdd:pfam03924 157 AALLRLGED---GLDLALYDGTSASAPELLY 184
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
424-690 |
1.01e-64 |
|
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: 219.46 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 424 GAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDG 503
Cdd:COG2199 7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 504 SVH--RYVAQTSDITQKKASEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHA 581
Cdd:COG2199 87 LLAllLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 582 QGDVLLVEAARRIATCVRESDTVARLGGDEFTVILSElVDINSAEHIAQNIIKQLAA-PFELLQDVVFVQASVGITLYPD 660
Cdd:COG2199 167 AGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPG-TDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPE 245
|
250 260 270
....*....|....*....|....*....|
gi 1833325744 661 DSLDVETLIKNADQAMYVAKNLGGNRFSRF 690
Cdd:COG2199 246 DGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
530-687 |
1.56e-64 |
|
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: 214.34 E-value: 1.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 530 NYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGG 609
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833325744 610 DEFTVILSElVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGNRF 687
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
529-686 |
5.64e-58 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 195.93 E-value: 5.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 529 ANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLG 608
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 609 GDEFTVILSElVDINSAEHIAQNI---IKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGN 685
Cdd:pfam00990 81 GDEFAILLPE-TSLEGAQELAERIrrlLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
.
gi 1833325744 686 R 686
Cdd:pfam00990 160 R 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
527-688 |
5.47e-56 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 190.54 E-value: 5.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 527 QQANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVAR 606
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 607 LGGDEFTVILSElVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGNR 686
Cdd:smart00267 81 LGGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
..
gi 1833325744 687 FS 688
Cdd:smart00267 160 VA 161
|
|
| CHASE |
smart01079 |
This domain is found in the extracellular portion of receptor-like proteins - such as serine ... |
112-281 |
5.52e-53 |
|
This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.
Pssm-ID: 215015 Cd Length: 176 Bit Score: 182.53 E-value: 5.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 112 SDVVTRSEFQDYIASLNVKEHYPAIQGIGYAVHIPAADLELHKRKMRAEGFPDYDI--YPTGERDQYTSIIYLEPFNlRN 189
Cdd:smart01079 1 SESVSRAEFRRFALELQLNRRLPGIQGLGWAPRVPPAERAAFEAALRAGGPGLFNIrlAPDGERDEYFVITYIEPLA-GN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 190 QRAFGFDMFSEPKRRAAMEVARDTGNTAVSTKVTLVQESGekMQASILMYLPFYKNGkprATLEERRSNLQGYVYSPFRL 269
Cdd:smart01079 80 EAALGLDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTG--DGRGFLLRLPVYRGG---PPTSTRREALWGFVSAVFRL 154
|
170
....*....|..
gi 1833325744 270 DKLMGGILNEAQ 281
Cdd:smart01079 155 DDLLEGLLGALD 166
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
700-949 |
3.94e-47 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 176.72 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 700 TRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPMQFIPLAEESRLIHDINDWVFHEATREL 779
Cdd:PRK10551 260 LRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 780 ASWRKQLVPEFQISVNVSPVELRQN--REKVgahwiRHLQALgLPGK--SLAIEITESILLNaESNVTDKLHLFRDAGIE 855
Cdd:PRK10551 340 AELQKVLPVGAKLGINISPAHLHSDsfKADV-----QRLLAS-LPADhfQIVLEITERDMVQ-EEEATKLFAWLHSQGIE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 856 VSIDDFGTGYSSLSYLKKFDIDYLKVDQSFVHNLvdGTD---DKVLcEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGC 932
Cdd:PRK10551 413 IAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAI--GTEtvtSPVL-DAVLTLAKRLNMLTVAEGVETPEQARWLRERGV 489
|
250
....*....|....*..
gi 1833325744 933 DYAQGWLYSKAVTAPDF 949
Cdd:PRK10551 490 NFLQGYWISRPLPLEDF 506
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
528-686 |
2.87e-40 |
|
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: 145.94 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 528 QANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARL 607
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 608 GGDEFTVILSElVDINSAEHIAQNI---IKQLAAPFElLQDVVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGG 684
Cdd:TIGR00254 81 GGEEFVVILPG-TPLEDALSKAERLrdaINSKPIEVA-GSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGR 158
|
..
gi 1833325744 685 NR 686
Cdd:TIGR00254 159 NR 160
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
532-686 |
7.40e-33 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 133.10 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 532 DLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDE 611
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833325744 612 FTVILSElVDINSAEHIAQNIIKQLA-APFELLQD--VVFVQASVGITLYPDDSLDVETLIKNADQAMYVAKNLGGNR 686
Cdd:PRK09581 375 FVVVMPD-TDIEDAIAVAERIRRKIAeEPFIISDGkeRLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
529-686 |
2.77e-28 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 115.93 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 529 ANYDLLTGLPNRHMFHDRLERAIKksRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLG 608
Cdd:PRK09894 129 SNMDVLTGLPGRRVLDESFDHQLR--NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 609 GDEFTVILSELVDINS---AEHIAQNIIKQlaaPFELLQDVVFVQASVGIT-LYPDDSLDVetLIKNADQAMYVAKNLGG 684
Cdd:PRK09894 207 GEEFIICLKAATDEEAcraGERIRQLIANH---AITHSDGRINITATFGVSrAFPEETLDV--VIGRADRAMYEGKQTGR 281
|
..
gi 1833325744 685 NR 686
Cdd:PRK09894 282 NR 283
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
522-686 |
3.58e-28 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 120.50 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 522 EKLIWQqANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRES 601
Cdd:PRK15426 392 SSLQWQ-AWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQ 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 602 DTVARLGGDEFTVILSElVDINSAEHIAQNIIKQLAAPFELLQD--VVFVQASVGI-TLYPDDSLDVETLIKNADQAMYV 678
Cdd:PRK15426 471 DVAGRVGGEEFCVVLPG-ASLAEAAQVAERIRLRINEKEILVAKstTIRISASLGVsSAEEDGDYDFEQLQSLADRRLYL 549
|
....*...
gi 1833325744 679 AKNLGGNR 686
Cdd:PRK15426 550 AKQAGRNR 557
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
395-616 |
6.45e-27 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 110.88 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 395 ERKKAEEELRLAALMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGH 474
Cdd:COG2202 2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 475 WQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVHRYVAQTSDITQKKASEKLIWQQANYDLLTGLPNRHMFHDR-LERAIKK 553
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLdLDGRILY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833325744 554 SRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDEFTVIL 616
Cdd:COG2202 162 VNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVW 224
|
|
| CHASE |
COG3452 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
47-864 |
2.71e-21 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442675 [Multi-domain] Cd Length: 785 Bit Score: 100.00 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 47 WPVAWIILFISLLLTFLVWRSAQEDLARLQQVQLESRVSKVSDAVLRRVQAYEQVLRGGVGLLAASDVVTRSEFQDYIAs 126
Cdd:COG3452 14 LLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEFERLAR- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 127 lNVKEHYPAIQGIGYAvhipaadlelhkrkmraegfPDYDI---YPtgerdqytsiiyLEPfnlrNQRAFGFDMFSEPKR 203
Cdd:COG3452 93 -NLLEDYPGIRNIALA--------------------PDGVIryvYP------------LAG----NEAALGLDLRTDPEQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 204 RAAMEVARDTGNTAVSTKVTLVQesGEKmqaSILMYLPFYKNGKPRatleerrsNLQGYVYSPFRLDKLMGGI-LNEAQT 282
Cdd:COG3452 136 RAAALRARESGQLVLAGPVNLVQ--GGR---GLIGRLPVFLDGGDD--------RFWGFVSAVIDLDRLLDSAgLDDAQD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 283 GVKadinmevYE----DSQYSAENLLYDDNGIPDMRnaprsdslALTQSITVFGHTWSLYFTTRPAFHAAFDQNKPLRFL 358
Cdd:COG3452 203 GYQ-------IAlrgrDGDGAEGEVFYGDAALFDQD--------PVTLEVNLPGGSWQLAAAPKGGWLASPRNALPLRLA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 359 GFgtIFSVLLSALMWLFTKQRRRALVQASYMQEEIVERKKAEEELRLAALMYQhsseamsvadstgaivsinpaYTKVTG 438
Cdd:COG3452 268 GL--LISLLLALLVYLLRQLLLLRLLLLLLRLELIAAALLLLLLALDLLLELL---------------------LLLRLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 439 YTLEDAVGRNCSLHKAnNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVHR---YVAQTSDI 515
Cdd:COG3452 325 EALLQERLRALALLAA-LEDLLLLKFDRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVggvIDGRVAVI 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 516 TQKKASEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIA 595
Cdd:COG3452 404 LIIEALELAEARLAALDQERDASDVALGAALVVLEALLIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLLG 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 596 TCVRESDTVARLGGDEFTVILSELVDINSAEHIAQNIIKQLAAPFELLQDVVFVQASVGITLYPDDSLDVETLIKNADQA 675
Cdd:COG3452 484 DALRERIRRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLLRAE 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 676 MYVAKNLGGNRFSRFTQDLQE---AAETRLRMMRDLRNALAANQLEVYYQPIVEIATGKIYKAEALLRWKHPELGMVSPM 752
Cdd:COG3452 564 LILALLDAKSGLSALELSGLLagrAALDSLLLLLALALRQLDESALFILEELLLRLIIDLRIERLLLLLLGGEILLGELA 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 753 QFIPLAEESRLIHDINDWVFHEATRELASWRKQLVPEFQISVNVSPVELRQNREKVGAHWIRHLQALGLPGKSLAIEITE 832
Cdd:COG3452 644 LLLLLLVLIILILLSVEEAGLILALSLLLALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGLLAELVAEALRLALALA 723
|
810 820 830
....*....|....*....|....*....|..
gi 1833325744 833 SILLNAESNVTDKLHLFRDAGIEVSIDDFGTG 864
Cdd:COG3452 724 QLLLRLLLAELLQLLLLLLGLILLELLLRLDG 755
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
523-951 |
4.81e-21 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 98.78 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 523 KLIWQQANYDLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCV-RES 601
Cdd:PRK11059 222 TFIRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 602 DTV-ARLGGDEFTVIL--SELVDinsAEHIAQNIIKQLAA---PFELLQDVVFvqaSVGITLY-PDDSldVETLIKNADQ 674
Cdd:PRK11059 302 GALlARYSRSDFAVLLphRSLKE---ADSLASQLLKAVDAlppPKMLDRDDFL---HIGICAYrSGQS--TEQVMEEAEM 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 675 AMYVAKNLGGNRFSRF-TQDLQEAAETRLRMMRDLRNALAANQLEVYYQPIVEiATGKIYKAEALLRWKHPELGMVSPMQ 753
Cdd:PRK11059 374 ALRSAQLQGGNGWFVYdKAQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRDGQGELLSAEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 754 FIPLAEESRLIHDINDWVFHEATRELASWrkqlvPEFQISVNVSpVELRQNREKVgaHWIRH--LQALGLPGKSLAIEIT 831
Cdd:PRK11059 453 FMPMVQQLGLSEQYDRQVIERVLPLLRYW-----PEENLSINLS-VDSLLSRAFQ--RWLRDtlLQCPRSQRKRLIFELA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 832 ESILLNAESNVTDKLHLFRDAGIEVSIDDFGTGYSSLSYLKKFDIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGL 911
Cdd:PRK11059 525 EADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTET 604
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1833325744 912 KVIAEGVETQAQLDLLTAYGCDYAQGwlyskavtapDFFA 951
Cdd:PRK11059 605 QVFATGVESREEWQTLQELGVSGGQG----------DFFA 634
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
532-686 |
2.16e-16 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 82.18 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 532 DLLTGLPNRHMFHDRLERAIKKSRRSGFPMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRESDTVARLGGDE 611
Cdd:PRK10245 208 DGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 612 FTVILS-----ELVDINSAEHIAQNIIKQLAAPFELLqdvvfvQASVGIT-LYPDDSLDVETLiKNADQAMYVAKNLGGN 685
Cdd:PRK10245 288 FAVIMSgtpaeSAITAMSRVHEGLNTLRLPNAPQVTL------RISVGVApLNPQMSHYREWL-KSADLALYKAKNAGRN 360
|
.
gi 1833325744 686 R 686
Cdd:PRK10245 361 R 361
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
519-681 |
7.09e-16 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 80.82 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 519 KASEKLIWQQANYDLLTGLPNRHMFHDRLERAIKKS--RRSGfpmALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIAT 596
Cdd:PRK09966 238 QAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSdaRKTS---ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 597 CVRESDTVARLGGDEFTVILSELVDINSAEHIAQNIIKQLAAPFELLQ-DVVFVQASVGITLYPDDSlDVETLIKNADQA 675
Cdd:PRK09966 315 FGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNgHQTTMTLSIGYAMTIEHA-SAEKLQELADHN 393
|
....*.
gi 1833325744 676 MYVAKN 681
Cdd:PRK09966 394 MYQAKH 399
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
389-525 |
3.40e-13 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 70.82 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 389 MQEEIVERKKAEEELRLAALMYQ----HSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSLHkANNHDRKFFRA 464
Cdd:COG2202 118 IARDITERKRAEEALRESEERLRllveNAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDL-LHPEDRERLLE 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833325744 465 MWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDG-SVHRYVAQTSDITQKKASEKLI 525
Cdd:COG2202 197 LLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGgEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
393-522 |
1.69e-12 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 71.41 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 393 IVERKKAEEELRLAALMYQHSSEAMSVADST---GAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEI 469
Cdd:PRK13558 137 PISDLTVESDRRLKERALDEAPVGITIADATlpdEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAI 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1833325744 470 NATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVHRYVAQTSDITQKKASE 522
Cdd:PRK13558 217 DEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAE 269
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
411-528 |
1.47e-10 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 64.93 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 411 QHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYL 490
Cdd:TIGR02938 11 DQAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYL 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 1833325744 491 EWTTVNTIYLDDGSVHRYVAQTSDITQKKASEKLIWQQ 528
Cdd:TIGR02938 91 AELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQ 128
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
389-577 |
2.60e-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: 63.84 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 389 MQEEIVERKKAEEELRLAALMyQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCS--LHKANNHDRKFFRAMW 466
Cdd:COG5809 1 MKSSKMELQLRKSEQRFRSLF-ENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILdfLHPDDEKELREILKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 467 DEINATGHWQGEIWNwrKNGEaYLEWTTVNT-IYLDDGSVHRYVAQTSDITQKKASEKLIwqqanydlltglpnrHMFHD 545
Cdd:COG5809 80 KEGESRDELEFELRH--KNGK-RLEFSSKLSpIFDQNGDIEGMLAISRDITERKRMEEAL---------------RESEE 141
|
170 180 190
....*....|....*....|....*....|...
gi 1833325744 546 RLERAIKKSrrsgfPMALLLLDLD-RFKEVNDA 577
Cdd:COG5809 142 KFRLIFNHS-----PDGIIVTDLDgRIIYANPA 169
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
821-945 |
4.08e-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: 62.90 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 821 LPGKSLAIEITESILLNAEsnVTDKLHLFRDAGIEVSIDDFGTGYSSLSYLKKfdIDYLKVDqsfvhnlVDGTDDKVLcE 900
Cdd:COG3434 81 LPPERVVLEILEDVEPDEE--LLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID-------VLALDLEEL-A 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1833325744 901 AIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKAVT 945
Cdd:COG3434 149 ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
391-525 |
1.29e-09 |
|
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: 61.53 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 391 EEIVERKKAEEELRLAA----LMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNC----SLHKANNHDRKFF 462
Cdd:COG5809 124 RDITERKRMEEALRESEekfrLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSIleliHSDDQENVAAFIS 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833325744 463 RAMWDEINAtghwQGEIWNWRKNGEA-YLEWTTVNTIYldDGSVHRYVAQTSDITQKKASEKLI 525
Cdd:COG5809 204 QLLKDGGIA----QGEVRFWTKDGRWrLLEASGAPIKK--NGEVDGIVIIFRDITERKKLEELL 261
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
400-522 |
2.80e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 55.76 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 400 EEELRLaalMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSL----HKANNHDRKFFRAMWDEINATGHW 475
Cdd:TIGR00229 2 EERYRA---IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLElipeEDREEVRERIERRLEGEPEPVSEE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1833325744 476 QgeiWNWRKNG-EAYLEWTTvnTIYLDDGSVHRYVAQTSDITQKKASE 522
Cdd:TIGR00229 79 R---RVRRKDGsEIWVEVSV--SPIRTNGGELGVVGIVRDITERKEAE 121
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
560-655 |
2.92e-09 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 56.21 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 560 PMALLLLDLDRFKEVNDALGHAQGDVLLVEAARRIATCVRES-DTVARLGGDEFtVILSELVDINSAEHIAQNIIKQLAA 638
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEF-MVVSGLDHPAAAVAFAEDMREAVSA 79
|
90
....*....|....*..
gi 1833325744 639 pfELLQDVVFVQASVGI 655
Cdd:cd07556 80 --LNQSEGNPVRVRIGI 94
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
602-680 |
6.35e-09 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 56.46 E-value: 6.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833325744 602 DTVARLGGDEFTVILSElVDINSAEHIAQNIIKQLAAPFEllqdvVFVQASVGITlypddsldVETLIKNADqAMYVAK 680
Cdd:COG3706 116 DLVARYGGEEFAILLPG-TDLEGALAVAERIREAVAELPS-----LRVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
424-517 |
1.64e-08 |
|
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: 52.85 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 424 GAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATghWQGEIWNWRKNGEAYLEWTTVNTIYLDDG 503
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 1833325744 504 SVHRYVAQTSDITQ 517
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
399-676 |
5.75e-08 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 56.01 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 399 AEEELRLAALMyQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNcsLHKANNHDRKFFRAMWDEI-NATGHWQG 477
Cdd:COG3852 3 RESEELLRAIL-DSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRP--LAELFPEDSPLRELLERALaEGQPVTER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 478 EIWNWRKNGEAYLEWTTVNTIYLDDGSVHrYVAQTSDITQKKASEKLIWQQANYDLLTGLPnRHMFHDrleraIKKsrrs 557
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGEGG-VLLVLRDITERKRLERELRRAEKLAAVGELA-AGLAHE-----IRN---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 558 gfPMA-------LLLLDLDRfkevNDALGHAQgdvLLVEAARRIATCVRESDTVARLGGDEFtvilsELVDINsaehiaq 630
Cdd:COG3852 149 --PLTgirgaaqLLERELPD----DELREYTQ---LIIEEADRLNNLVDRLLSFSRPRPPER-----EPVNLH------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833325744 631 niikqlaapfELLQDVV-FVQASVG----ITLYPDDSL-DVET-----------LIKNADQAM 676
Cdd:COG3852 208 ----------EVLERVLeLLRAEAPknirIVRDYDPSLpEVLGdpdqliqvllnLVRNAAEAM 260
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
393-525 |
3.22e-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: 53.97 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 393 IVERKKAEEELRLAALMYQ----HSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNcSLHKANNHDRKFFRamwde 468
Cdd:COG5805 142 ITKKKKIEEILQEQEERLQtlieNSPDLICVIDTDGRILFINESIERLFGAPREELIGKN-LLELLHPCDKEEFK----- 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833325744 469 inatgHWQGEIWNWRKNGEAYLEWTTVNTIYL-----------DDGSVHRYVAQTSDITQKKASEKLI 525
Cdd:COG5805 216 -----ERIESITEVWQEFIIEREIITKDGRIRyfeavivplidTDGSVKGILVILRDITEKKEAEELM 278
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
406-531 |
2.71e-06 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 50.89 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 406 AALMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRN-CSLHKANNHDRKFFRAmwdEINATGHWQGEI-WNWR 483
Cdd:COG5805 36 LETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTiFDFLEKEYHYRVKTRI---ERLQKGYDVVMIeQIYC 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1833325744 484 KNGEAYLEWTTVNTIYldDGSVHRYVAQTSDITQKKASEKLIWQQANY 531
Cdd:COG5805 113 KDGELIYVEVKLFPIY--NQNGQAAILALRDITKKKKIEEILQEQEER 158
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
391-556 |
3.57e-06 |
|
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: 50.54 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 391 EEIVERKKAEEELRlaALMyQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSlhkannhdRKFFRAMWDEIN 470
Cdd:COG3829 1 AEELELKELEEELE--AIL-DSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVT--------ELIPNSPLLEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 471 ATG-HWQGEIWNWRKNGEAYLewTTVNTIYlDDGSVHRYVAQTSDITQKKaseKLIWQQANYDLLTGLPNRHMFHD---- 545
Cdd:COG3829 70 KTGkPVTGVIQKTGGKGKTVI--VTAIPIF-EDGEVIGAVETFRDITELK---RLERKLREEELERGLSAKYTFDDiigk 143
|
170
....*....|...
gi 1833325744 546 --RLERAIKKSRR 556
Cdd:COG3829 144 spAMKELLELAKR 156
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
409-515 |
5.89e-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 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: 46.26 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 409 MYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGHWQ-GEIWNWRKNGE 487
Cdd:pfam00989 6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRgFEVSFRVPDGR 85
|
90 100
....*....|....*....|....*...
gi 1833325744 488 AYLEWTTVNTIYLDDGSVHRYVAQTSDI 515
Cdd:pfam00989 86 PRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
426-527 |
1.37e-05 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 48.90 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 426 IVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSV 505
Cdd:PRK13557 55 IVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDL 134
|
90 100
....*....|....*....|..
gi 1833325744 506 HRYVAQTSDITQKKASEKLIWQ 527
Cdd:PRK13557 135 VYFFGSQLDVSRRRDAEDALRQ 156
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
426-524 |
2.71e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 47.51 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 426 IVSINPAYTKVTGYTLEDAVGRNCSLHKANNHDRKFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSV 505
Cdd:PRK13559 68 IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGRL 147
|
90
....*....|....*....
gi 1833325744 506 HRYVAQTSDITQKKASEKL 524
Cdd:PRK13559 148 LYFFGSQWDVTDIRAVRAL 166
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
391-530 |
9.17e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 46.59 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 391 EEIVERKKAE----EELRLAALMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRncSLHKANNHDR--KFFRA 464
Cdd:PRK13560 187 EDITERKRAEeridEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGM--SIHDFAPAQPadDYQEA 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833325744 465 MWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYLDDGSVH--RYVAQTSDITQKKASEKLIWQQAN 530
Cdd:PRK13560 265 DAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEFDDKENHcaGLVGAITDISGRRAAERELLEKED 332
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
721-944 |
1.32e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 44.61 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 721 YQPIVEIaTGKIYKAEALLRWKHPElgmvSPMQFIP-------LAEESRLIhdindwVFHEATRELASWRKQLVPE-FQI 792
Cdd:PRK11596 34 FQPIYRT-SGRLMAIELLTAVTHPS----NPSQRLSperyfaeITVSHRLD------VVKEQLDLLAQWADFFVRHgLLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 793 SVNV---SPVELRQNREkvgahwIRHLQAlGLPgkSLAIEITESILLNAESnvtdKLHLFRDAGiEVSIDDFGTG---YS 866
Cdd:PRK11596 103 SVNIdgpTLIALRQQPA------ILRLIE-RLP--WLRFELVEHIRLPKDS----PFASMCEFG-PLWLDDFGTGmanFS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833325744 867 SLSYLKkfdIDYLKVDQSFVHNLVDGTDDKVLCEAIIVMAHKLGLKVIAEGVETQAQLDLLTAYGCDYAQGWLYSKAV 944
Cdd:PRK11596 169 ALSEVR---YDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
413-515 |
2.82e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. 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: 41.08 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 413 SSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRNCS--LHKAnnhDRKFFRAMW-DEINATGHWQGEIWNWRKNGEAY 489
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLdlIHPE---DREELRERLeNLLSGGEPVTLEVRLRRKDGSVI 77
|
90 100
....*....|....*....|....*.
gi 1833325744 490 LEWTTVNTIYLDDGSVHRYVAQTSDI 515
Cdd:cd00130 78 WVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
426-510 |
4.63e-04 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 40.01 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833325744 426 IVSINPAYTKVTGYTLEDAVGRNCS----LHKAnnhDR-KFFRAMWDEINATGHWQGEIWNWRKNGEAYLEWTTVNTIYL 500
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESwldlVHPD---DReRVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD 77
|
90
....*....|
gi 1833325744 501 DDGSVHRYVA 510
Cdd:pfam08447 78 ENGKPVRVIG 87
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
407-448 |
1.68e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 37.76 E-value: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1833325744 407 ALMYQHSSEAMSVADSTGAIVSINPAYTKVTGYTLEDAVGRN 448
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
|
|
| |
