|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
286-902 |
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: 655.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 286 HDWMLTMTARDGFKARFGRDGATLIAITGTGLSLLLALLTWLMLTGRSRAMRLASSMTRELRENEEKFRAIADCTVNWEI 365
Cdd:COG5001 57 LALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 366 WWSPEGKPRWINSAVEEYIGYTVDECMVMDDFACTVIYPGDAALVAPQFRNAQQGSRGDNLEFRCIRKDGSLMWLSVSWV 445
Cdd:COG5001 137 LAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 446 PITDSRGEFIG--FRTSGRDITERKIADEKIKELAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTL 523
Cdd:COG5001 217 LLLGLLLLLLLvaVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 524 NDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVVVVGNLnpdrcEAARQTEALGETILSVLGSPYHLDEIDYRS 603
Cdd:COG5001 297 NDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDL-----DDPEDAEAVAERILAALAEPFELDGHELYV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 604 SASIGATVFNGYQVSTDDLMKQADLAMYKSKERGRNAVRLFDPEMQTVVVERAALEAALRDAIENDQFLLHYQAQID--G 681
Cdd:COG5001 372 SASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDlaT 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 682 ERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQLARWAERpDLEHLTIAVNVSVQQLHKPDFVD 761
Cdd:COG5001 452 GRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDA-GLPDLRVAVNLSARQLRDPDLVD 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 762 TVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGYSSLSYLKRLPLAQLKIDRSFVRDVL 841
Cdd:COG5001 531 RVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLA 610
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423782230 842 VDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVGVEEFEA 902
Cdd:COG5001 611 EDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
460-902 |
3.37e-119 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 377.48 E-value: 3.37e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 460 SGRDITERKIADEKIKELAFYDALTGLPNRTLLLDNLRQALAvsARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEV 539
Cdd:PRK10060 219 SGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAIN--AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 540 AKRLAASIPRSDTVARVGGDEFVVvvgnLNPDRCEAArqTEALGETILSVLGSPYHLDEIDYRSSASIGATVFNGYQVST 619
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLV----LASHTSQAA--LEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 620 DDLMKQADLAMYKSKERGRNAVRLFDPEMQTVVVERAALEAALRDAIENDQFLLHYQAQIDGE-RVTGAEALVRWSHPAR 698
Cdd:PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRgEVRSLEALVRWQSPER 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 699 GLVYPADFIPVAEDTGLIAELGAWVLHAACMQLARWAERPdlEHLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLK 778
Cdd:PRK10060 451 GLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKG--INLRVAVNVSARQLADQTIFTALKQALQELNFEYCPID 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 779 LELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGYSSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAH 858
Cdd:PRK10060 529 VELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQ 608
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1423782230 859 SLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVGVEEFEA 902
Cdd:PRK10060 609 ALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
333-902 |
3.23e-118 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 372.20 E-value: 3.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 333 SRAMRLASSMTRELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDECMVMDDFActVIYPGDAALVAP 412
Cdd:COG2200 11 RLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLL--LLLLLLLALLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 413 QFRNAQQGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKELAFYDALTGLPNRTLL 492
Cdd:COG2200 89 LLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 493 LDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVVVVGNLNPDR 572
Cdd:COG2200 169 LLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 573 CEAARQTEALgetiLSVLGSPYHLDEIDYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKERGRNAVRLFDPEMQtVV 652
Cdd:COG2200 249 AAAAAALRLL----LLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEA-RA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 653 VERAALEAALRDAIENDQFLLHYQAQID--GERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQ 730
Cdd:COG2200 324 RRRLALESELREALEEGELRLYYQPIVDlrTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 731 LARWAERpdLEHLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALD 810
Cdd:COG2200 404 LARWPER--GLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 811 DFGIGYSSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYL 890
Cdd:COG2200 482 DFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYL 561
|
570
....*....|..
gi 1423782230 891 FCRPVGVEEFEA 902
Cdd:COG2200 562 FGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
660-899 |
3.06e-113 |
|
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: 346.84 E-value: 3.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 660 AALRDAIENDQFLLHYQAQID--GERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQLARWAER 737
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDlrTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 738 PDleHLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGYS 817
Cdd:cd01948 81 GP--DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 818 SLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVGV 897
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
..
gi 1423782230 898 EE 899
Cdd:cd01948 239 EE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
659-899 |
3.23e-101 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 315.31 E-value: 3.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 659 EAALRDAIENDQFLLHYQAQIDGE--RVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQLARWAE 736
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRtgRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 737 RpDLEHLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGY 816
Cdd:smart00052 81 Q-GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 817 SSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVG 896
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
...
gi 1423782230 897 VEE 899
Cdd:smart00052 240 LDD 242
|
|
| CHASE1 |
COG3614 |
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms]; |
21-584 |
2.39e-96 |
|
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442832 [Multi-domain] Cd Length: 588 Bit Score: 314.70 E-value: 2.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 21 TWALWNHERQATRHEILSQFDFSLGDVVSRVEQRMGTYELLLRGVQSLFAASGEVNRDQFRAYVDSLNLDANFSGIQAIG 100
Cdd:COG3614 25 TALAWWAVRRAEEQRARARFERLADELASALEERLDAYEQVLRGLAGLFAASDDVTRAEFRRYVASLDLLRRYPGIQGLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 101 IVEWVPATQKAAHIASMHRRGLPDYVIQPDGPRDNYAPIIQREPHIGANRAAAGFDAWADPVRRRAMEQARDTGMATITG 180
Cdd:COG3614 105 WAPRVPAAERAAFEAAARAEGFPDFRIRPAGERDEYFPITYIEPLDARNRRALGFDMASEPVRRAAMERARDTGRPAASG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 181 KVRLSVDTDPgaKPGFVMYMPVYAGGQMPDNATERREQLLGWVYASFRMHDVVASLYGE-EPPGLSIAIYDGVESSPDAL 259
Cdd:COG3614 185 PVTLVQETDG--QPGFLLYLPVYRGGAPPDTVAERRAALRGFVYAPFRMDDLLAGVLGRlADRDLDLRLYDGTDPGPPQL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 260 LYKTSGPAGHNVSADLTAREYLVVCGHDWMLTMTARDGFKARFGRDGATLIAITGTGLSLLLALLTWLMLTGRSRAMRLA 339
Cdd:COG3614 263 LYDSSPAAPAAAAPALSATRTLEVAGRTWTLEFRPTPAFEAALRSWLPWLVLLGGLLLSLLLALLLLSLARRRRRAEALA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 340 SSMTRELRENEEKFRAIADCTVNWEIwwspegkpRWINSAVEEYIGYTVDECMVMDDFACTVIYPGDAALVAPQFRNAQQ 419
Cdd:COG3614 343 AARAALRALRAAELRLRALLRRALLA--------LLRNALALALLLAALLLLLARLLLLLAALLLLLARALSAADLLLLQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 420 GSRGDNLEFRCIR--------KDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKELAFYDALTGLPNRTL 491
Cdd:COG3614 415 ADLLLLRLLLLLRrrlllvrdLRLGRGLGLGVVLLLDAILLDLLALAELELAAARAEVALAEALLALLVVLLLALLLALL 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 492 LLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVVVVGNLNPD 571
Cdd:COG3614 495 RLLLALAELAATAAREAAGAALLLDREAALLDAALEALLDLLGLLVLLLLAELLLRLGALLLGRALLGGVGAGEGLVIIA 574
|
570
....*....|...
gi 1423782230 572 RCEAARQTEALGE 584
Cdd:COG3614 575 ELAALELELLRLE 587
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
472-902 |
2.49e-90 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 300.48 E-value: 2.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 472 EKIKELAFYDALTGLPNRTLLLDNLRQALAvsaRKGTSgALLFIDLDhfkTLNDTLG---HDKGDLLLQEVAKRLAASIP 548
Cdd:PRK13561 225 EEQSRNATRFPVSDLPNKALLMALLEQVVA---RKQTT-ALMIITCE---TLRDTAGvlkEAQREILLLTLVEKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 549 RSDTVARVGGDEFVVVV-GNLNPDRceAARqteaLGETILSVLGSPYHLDEIDYRSSASIGATVFNGYQvSTDDLMKQAD 627
Cdd:PRK13561 298 PRMVLAQISGYDFAIIAnGVKEPWH--AIT----LGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDL-TAEQLYSRAI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 628 LAMYKSKERGRNAVRLFDPEMQTVVVERAALEAALRDAIENDQFLLHYQAQIDGE--RVTGAEALVRWSHPARGLVYPAD 705
Cdd:PRK13561 371 SAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRsgKLVSAEALLRMQQPDGSWDLPEG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 706 FIPVAEDTGLIAELGAWVLHAACMQLARWAERPDLehLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESV 785
Cdd:PRK13561 451 LIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIM--LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESR 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 786 LVNNVQEIIEKMEALKAKGIVFALDDFGIGYSSLSYL---KRLPLAQLKIDRSFVrDVLvdPNDAVIARTIVALAHSLGI 862
Cdd:PRK13561 529 RIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFV-DGL--PEDDSMVAAIIMLAQSLNL 605
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1423782230 863 GVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVGVEEFEA 902
Cdd:PRK13561 606 QVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
466-899 |
5.85e-88 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 297.84 E-value: 5.85e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 466 ERKIADEKIKELAFYDALTGLPNRtlllDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAA 545
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNR----NNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 546 SIPRSDTVARVGGDEFVVVVgnlnPDrCEAARQTEaLGETILSVLGSPYHLDEIDYRSSASIGATvfngYQVSTD--DLM 623
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVS----LE-NDVSNITQ-IADELRNVVSKPIMIDDKPFPLTLSIGIS----YDVGKNrdYLL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 624 KQADLAMYKSKERGRNAVRLFDPEMQTVVVERAALEAALRDAIENDQFLLHYQAQI---DGErVTGAEALVRWSHPARGL 700
Cdd:PRK11359 510 STAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIfaeTGE-LYGIEALARWHDPLHGH 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 701 VYPADFIPVAEDTGLIAELGAWVLHAACMQLARWaerpDLEHL---TIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRL 777
Cdd:PRK11359 589 VPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEW----RSQNIhipALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQL 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 778 KLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGYSSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALA 857
Cdd:PRK11359 665 TVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIG 744
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1423782230 858 HSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVGVEE 899
Cdd:PRK11359 745 QSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
659-894 |
1.10e-82 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 266.11 E-value: 1.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 659 EAALRDAIENDQFLLHYQAQID--GERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQLARWAE 736
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDlrTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 737 RPDLEhltIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGY 816
Cdd:pfam00563 81 GPDIK---LSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423782230 817 SSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRP 894
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
484-902 |
2.61e-78 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 267.96 E-value: 2.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 484 TGLPNRTLLLDNLRQALAVSARKgTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVV 563
Cdd:PRK11829 238 TELPNRSLFISLLEKEIASSTRT-DHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 564 VVGNlnpdrceAARQTEA--LGETILSVLGSPYHLDEIDYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKERGRNAV 641
Cdd:PRK11829 317 LARG-------TRRSFPAmqLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 642 RLFDPEMQTVVVERAALEAALRDAIENDQFLLHYQAQID--GERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAEL 719
Cdd:PRK11829 390 MVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDmkRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 720 GAWVLHAACMQLARWAERPDLehLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEA 799
Cdd:PRK11829 470 GNWVLEEACRILADWKARGVS--LPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 800 LKAKGIVFALDDFGIGYSSLSYL---KRLPLAQLKIDRSFVRDVlvdPNDAVIARTIVALAHSLGIGVIAEGVETEEQRA 876
Cdd:PRK11829 548 LQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQ 624
|
410 420
....*....|....*....|....*.
gi 1423782230 877 FLASAGCYAYQGYLFCRPVGVEEFEA 902
Cdd:PRK11829 625 WLLEHGIQCGQGFLFSPPLPRAEFEA 650
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
654-902 |
1.28e-71 |
|
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: 245.98 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 654 ERAALEAALRDAIENDQFLLHYQAQIDGE--RVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQL 731
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIVDLKtgRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 732 ARW-AERPDLehlTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNnVQEIIEKMEALKAKGIVFALD 810
Cdd:COG4943 348 GDLlAADPDF---HISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 811 DFGIGYSSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAG-CYAyQGY 889
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGvQYG-QGW 502
|
250
....*....|...
gi 1423782230 890 LFCRPVGVEEFEA 902
Cdd:COG4943 503 LFAKPLPAEEFIA 515
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
446-903 |
8.35e-71 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 254.60 E-value: 8.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 446 PITDSRGEFIGFRTSGRDITE-RKIadekIKELAF---YDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFK 521
Cdd:PRK09776 633 PLSTLDGENIGSVLVIQDVTEsRKM----LRQLSYsasHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFK 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 522 TLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFvvvvGNLNPDrCEAArQTEALGETILSVLGSpYHLDEID- 600
Cdd:PRK09776 709 AVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEF----GLLLPD-CNVE-SARFIATRIISAIND-YHFPWEGr 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 601 -YRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKERGRNAVRLFDPEMQTVVVERAALEAA--LRDAIENDQFLLHYQ- 676
Cdd:PRK09776 782 vYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAeqWRMIKENQLMMLAHGv 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 677 -AQIDGERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAAcmqLARWAERPDLEHLTIAVNVSVQQLH 755
Cdd:PRK09776 862 aSPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF---FRQAAKAVASKGLSIALPLSVAGLS 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 756 KPDFVDTVLATLQRTGARPDRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGYSSLSYLKRLPLAQLKIDRS 835
Cdd:PRK09776 939 SPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGE 1018
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423782230 836 FVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVGVEEFEAT 903
Cdd:PRK09776 1019 LVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNS 1086
|
|
| CHASE |
pfam03924 |
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ... |
73-261 |
1.57e-63 |
|
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: 212.15 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 73 GEVNRDQFRAYVDSLNLDANfsGIQAIGIVEWVPATQKAAHIASMHRRGLPDYVIQPDGPRDNYAPIIQREPhIGANRAA 152
Cdd:pfam03924 1 DSVDREEFRRYAASLLLRRP--GIQGLGWAPRVPAAERAAFEAAVRAEGFPDFTIRPAGDRDEYFPIIYIEP-LAGNNRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 153 AGFDAWADPVRRRAMEQARDTGMATITGKVRLSVDTDPGakPGFVMYMPVYAGGqMPDNATERREQLLGWVYASFRMHDV 232
Cdd:pfam03924 78 LGFDMASEPVRREAIERARDTGEPVLSGPVTLVQDGDGQ--PGFLLYLPVYRGG-PPDTVAERRAALLGFVYAPFRIDDL 154
|
170 180 190
....*....|....*....|....*....|
gi 1423782230 233 V-ASLYGEEPPGLSIAIYDGVESSPDALLY 261
Cdd:pfam03924 155 LeAALLRLGEDGLDLALYDGTSASAPELLY 184
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
437-644 |
8.11e-59 |
|
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: 202.52 E-value: 8.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 437 LMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKELAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFID 516
Cdd:COG2199 73 ALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLID 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 517 LDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVVVVGNLNPDrceaarQTEALGETILSVLGS-PYH 595
Cdd:COG2199 153 LDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE------EAEALAERLREALEQlPFE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1423782230 596 LDEIDYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKERGRNAVRLF 644
Cdd:COG2199 227 LEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
479-642 |
1.11e-55 |
|
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: 189.30 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 479 FYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGG 558
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 559 DEFVVVVGNLNPDRCeaarqtEALGETILSVLGSPYHLDEIDYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKERGR 638
Cdd:cd01949 81 DEFAILLPGTDLEEA------EALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGR 154
|
....
gi 1423782230 639 NAVR 642
Cdd:cd01949 155 NRVV 158
|
|
| CHASE |
smart01079 |
This domain is found in the extracellular portion of receptor-like proteins - such as serine ... |
72-250 |
1.47e-54 |
|
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: 186.77 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 72 SGEVNRDQFRAYVDSLNLDANFSGIQAIGIVEWVPATQKAAHIASMHRRGLPDYVIQ--PDGPRDNYAPIIQREPHIGaN 149
Cdd:smart01079 1 SESVSRAEFRRFALELQLNRRLPGIQGLGWAPRVPPAERAAFEAALRAGGPGLFNIRlaPDGERDEYFVITYIEPLAG-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 150 RAAAGFDAWADPVRRRAMEQARDTGMATITGKVRLSVDTDPGakPGFVMYMPVYAGGQMPdnaTERREQLLGWVYASFRM 229
Cdd:smart01079 80 EAALGLDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGDG--RGFLLRLPVYRGGPPT---STRREALWGFVSAVFRL 154
|
170 180
....*....|....*....|..
gi 1423782230 230 HDVVASLYGEE-PPGLSIAIYD 250
Cdd:smart01079 155 DDLLEGLLGALdLPGLDLALYD 176
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
478-639 |
2.94e-53 |
|
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: 182.45 E-value: 2.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 478 AFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVG 557
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 558 GDEFVVVVGNLNPdrcEAARQTEALGETILSVLGSPYHLDEIDYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKERG 637
Cdd:pfam00990 81 GDEFAILLPETSL---EGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
..
gi 1423782230 638 RN 639
Cdd:pfam00990 158 RN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
476-644 |
6.48e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 173.20 E-value: 6.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 476 ELAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVAR 555
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 556 VGGDEFVVVVGNLNPDRCeaarqtEALGETILSVLGSPYHLDEIDYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKE 635
Cdd:smart00267 81 LGGDEFALLLPETSLEEA------IALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
|
....*....
gi 1423782230 636 RGRNAVRLF 644
Cdd:smart00267 155 AGRNQVAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
477-645 |
6.01e-39 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 142.09 E-value: 6.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 477 LAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARV 556
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 557 GGDEFVVVVgnLNPDRCEAARQTEALGETILSvLGSPYHLDEIdYRSSASIGATVFNGYQVSTDDLMKQADLAMYKSKER 636
Cdd:TIGR00254 81 GGEEFVVIL--PGTPLEDALSKAERLRDAINS-KPIEVAGSET-LTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
....*....
gi 1423782230 637 GRNAVRLFD 645
Cdd:TIGR00254 157 GRNRVVVAD 165
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
665-900 |
5.24e-37 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 146.68 E-value: 5.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 665 AIENDQFLLHYQAQIDGE--RVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELgawVLHaaCMQL-ARWAerPDLE 741
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQtlRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPL---TQH--LFELiARDA--AELQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 742 HL-----TIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLKLELTESVLVNNvQEIIEKMEALKAKGIVFALDDFGIGY 816
Cdd:PRK10551 344 KVlpvgaKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFGTGH 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 817 SSLSYLKRLPLAQLKIDRSFVRDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPVG 896
Cdd:PRK10551 423 SALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLP 502
|
....
gi 1423782230 897 VEEF 900
Cdd:PRK10551 503 LEDF 506
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
476-641 |
4.75e-32 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 130.79 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 476 ELAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVAR 555
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 556 VGGDEFVVVVgnlnPDRC-EAARQTealGETI-LSVLGSPYHLDEIDYRSS--ASIGATVFNGYQVSTDDLMKQADLAMY 631
Cdd:PRK09581 370 YGGEEFVVVM----PDTDiEDAIAV---AERIrRKIAEEPFIISDGKERLNvtVSIGVAELRPSGDTIEALIKRADKALY 442
|
170
....*....|
gi 1423782230 632 KSKERGRNAV 641
Cdd:PRK09581 443 EAKNTGRNRV 452
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
480-649 |
8.43e-25 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 105.53 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 480 YDALTGLPNRTLLLDNLRQALAvsARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGD 559
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQLR--NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 560 EFVVVVGNLNPDrcEAARQTEALGETIlsvLGSPYHLDEIDYRSSASIGATVFNGyQVSTDDLMKQADLAMYKSKERGRN 639
Cdd:PRK09894 209 EFIICLKAATDE--EACRAGERIRQLI---ANHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTGRN 282
|
170
....*....|
gi 1423782230 640 AVRLFDPEMQ 649
Cdd:PRK09894 283 RVMFIDEQNV 292
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
344-564 |
1.10e-24 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 104.34 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 344 RELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDECMVMDDFacTVIYPGDAALVAPQFRNAQQGSRG 423
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 424 DNLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKELAFYDALTGLPNRTLLLDNLRQALAVS 503
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423782230 504 ARKGTSGALLFIDLDHF-KTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVVV 564
Cdd:COG2202 162 VNPAAEELLGYSPEELLgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWV 223
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
466-895 |
2.31e-23 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 106.10 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 466 ERKIADEKIKELAFYDALTGLPNRtLLLDN-LRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLA 544
Cdd:PRK11059 216 ERSRFDTFIRSNAFQDAKTGLGNR-LFFDNqLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 545 ASIPR-SDTV-ARVGGDEFVVVVgnlnPDRC--EAARQTEALGETILSvLGSPYHLDEIDYrssASIGATVFNGYQvSTD 620
Cdd:PRK11059 295 TFVMRyPGALlARYSRSDFAVLL----PHRSlkEADSLASQLLKAVDA-LPPPKMLDRDDF---LHIGICAYRSGQ-STE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 621 DLMKQADLA-------------MYKSK---ERGRNAVRLfdpemqtvvveRAALEAALrdaiENDQFLLHYQAQIDGE-R 683
Cdd:PRK11059 366 QVMEEAEMAlrsaqlqggngwfVYDKAqlpEKGRGSVRW-----------RTLLEQTL----VRGGPRLYQQPAVTRDgK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 684 VTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAACMQLARWAERpdlehlTIAVNVSVQQLHKPDFV--- 760
Cdd:PRK11059 431 VHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE------NLSINLSVDSLLSRAFQrwl 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 761 -DTVLAT--LQRTgarpdRLKLELTESVLVNNVQEIIEKMEALKAKGIVFALDDFGIGYSSLSYLKRLPLAQLKIDRSFV 837
Cdd:PRK11059 505 rDTLLQCprSQRK-----RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLV 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423782230 838 RDVLVDPNDAVIARTIVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPV 895
Cdd:PRK11059 580 RNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQ 637
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
472-641 |
3.12e-20 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 95.85 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 472 EKIKELAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSD 551
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 552 TVARVGGDEFVVVVGNLNPDrcEAArqteALGETILSVLGSPyhldEIDYRSSASIGATVFNGyqVST---------DDL 622
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASLA--EAA----QVAERIRLRINEK----EILVAKSTTIRISASLG--VSSaeedgdydfEQL 539
|
170
....*....|....*....
gi 1423782230 623 MKQADLAMYKSKERGRNAV 641
Cdd:PRK15426 540 QSLADRRLYLAKQAGRNRV 558
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
481-638 |
1.32e-18 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 90.02 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 481 DALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDE 560
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 561 FVVVVGNLNPDrcEAARQTEALGETIlsvlgspyHLDEIDYRSSASIGAtvfngYQV----STDDLMKQADLAMYKSKER 636
Cdd:NF040885 424 FCIILIDYEEA--EAQNLIERIRQHL--------RTIDPDKRVSFSWGA-----YQMqpgdTLDDAYKAADERLYLNKKQ 488
|
..
gi 1423782230 637 GR 638
Cdd:NF040885 489 KH 490
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
465-639 |
3.83e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 84.11 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 465 TERKIADEK--IKELAFYDALTGLPNRTLLLDNLRQALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKR 542
Cdd:PRK10245 190 TATKLAEHKrrLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 543 LAASIPRSDTVARVGGDEFVVVVGNLNPDRCEAARQTEALGETILSVLGSPYHLDEIdyrssaSIGATVFNGYQVSTDDL 622
Cdd:PRK10245 270 LQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRI------SVGVAPLNPQMSHYREW 343
|
170
....*....|....*..
gi 1423782230 623 MKQADLAMYKSKERGRN 639
Cdd:PRK10245 344 LKSADLALYKAKNAGRN 360
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
478-636 |
3.24e-16 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 81.98 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 478 AFYDALTGLPNRTLLLDNLRQALAVSARKGTSgALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVG 557
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 558 GDEFVVVVGNLnpdrceaarQTEALGETILSVLGSPYHLdEIDYRSSASIGATVFNGY-----QVSTDDLMKQADLAMYK 632
Cdd:PRK09966 327 GDEFAMVLYDV---------QSESEVQQICSALTQIFNL-PFDLHNGHQTTMTLSIGYamtieHASAEKLQELADHNMYQ 396
|
....
gi 1423782230 633 SKER 636
Cdd:PRK09966 397 AKHQ 400
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
774-895 |
8.35e-16 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 80.62 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 774 PDRLKLELTESVLVNnvQEIIEKMEALKAKGIVFALDDFGigySSLSYLKRLPLAQ-LKIDrsfVRDVlvDPNDAviaRT 852
Cdd:COG3434 83 PERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFV---LDPEWDPLLPLADiIKID---VLAL--DLEEL---AE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1423782230 853 IVALAHSLGIGVIAEGVETEEQRAFLASAGCYAYQGYLFCRPV 895
Cdd:COG3434 150 LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPE 192
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
344-474 |
1.36e-15 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 77.76 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 344 RELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDECMVMDDFActVIYPGDAALVAPQFRNAQQGSRG 423
Cdd:COG2202 130 EALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLD--LLHPEDRERLLELLRRLLEGGRE 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1423782230 424 D-NLEFRCIRKDGSLMWLSVSWVPITDsRGEFIGFRTSGRDITERKIADEKI 474
Cdd:COG2202 208 SyELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
|
|
| CHASE |
COG3452 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
21-806 |
2.70e-15 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442675 [Multi-domain] Cd Length: 785 Bit Score: 80.36 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 21 TWALWNHERQATRHEILSQFDFSLGDVVSRVEQRMGTYELLLRGVQSLFAASGEVNRDQFRAYVDslNLDANFSGIQAIG 100
Cdd:COG3452 28 GAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEFERLAR--NLLEDYPGIRNIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 101 IVewvpatqkaahiasmhrrglPDYVIQPDGPRDnyapiiqrephigANRAAAGFDAWADPVRRRAMEQARDTGMATITG 180
Cdd:COG3452 106 LA--------------------PDGVIRYVYPLA-------------GNEAALGLDLRTDPEQRAAALRARESGQLVLAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 181 KVRLSvdtdPGAKpGFVMYMPVYAGGQmpdnaterREQLLGWVYASFRMHDVVA-SLYGEEPPGLSIAI--YDGVESSPD 257
Cdd:COG3452 153 PVNLV----QGGR-GLIGRLPVFLDGG--------DDRFWGFVSAVIDLDRLLDsAGLDDAQDGYQIALrgRDGDGAEGE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 258 ALLYKTSGPAGHNVSADLTareylvVCGHDWMLTMTARDGFKARFGRDGATLIAITGTGLSLLLALLTWLMLTGRSRAMR 337
Cdd:COG3452 220 VFYGDAALFDQDPVTLEVN------LPGGSWQLAAAPKGGWLASPRNALPLRLAGLLISLLLALLVYLLRQLLLLRLLLL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 338 LASSMTRELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDecmvmDDFACTVIYPGDAALVAPQFRNA 417
Cdd:COG3452 294 LLRLELIAAALLLLLLALDLLLELLLLLRLAEALLQERLRALALLAALEDLL-----LLKFDRDLLDLLLLLELEAILAL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 418 QQGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKELAFYDALTGLPNRTLLLDNLR 497
Cdd:COG3452 369 LLLLRRLLRSREARGGLGGDLVRVGGVIDGRVAVILIIEALELAEARLAALDQERDASDVALGAALVVLEALLIIALLRE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 498 QALAVSARKGTSGALLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRSDTVARVGGDEFVVVVGNLNPDRCEAAR 577
Cdd:COG3452 449 LALLAGALLARKSLLLALDLAAESERLRYLELLLGDALRERIRRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDAR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 578 QTEALGETILSVLGSPYHLDEIDYRSSASIgatvfngyqvstDDLMKQADLAMYKSKERGRNAVRLFDPEMQTVVVERAA 657
Cdd:COG3452 529 ILEAERLELALVAGEVALEELLLRLLGEIL------------LLRAELILALLDAKSGLSALELSGLLAGRAALDSLLLL 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 658 LEAALRDAIENDQFLLHYQAQIDGERVTGAEALVRWSHPARGLVYPADFIPVAEDTGLIAELGAWVLHAacmqLARWAER 737
Cdd:COG3452 597 LALALRQLDESALFILEELLLRLIIDLRIERLLLLLLGGEILLGELALLLLLLVLIILILLSVEEAGLI----LALSLLL 672
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423782230 738 PDLEHLTIAVNVSVQQLHKPDFVDTVLATLQRTGARPDRLkLELTESVLVNNVQEIIEKMEALKAKGIV 806
Cdd:COG3452 673 ALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGLLAELV-AEALRLALALAQLLLRLLLAELLQLLLL 740
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
342-468 |
1.15e-13 |
|
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: 74.63 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 342 MTRELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDECMVMDDFacTVIYPGDAALVAPQFRNAQQGS 421
Cdd:COG5809 132 MEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSIL--ELIHSDDQENVAAFISQLLKDG 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1423782230 422 RGDNLEFRCIRKDGSLMWLSVSWVPITDSrGEFIGFRTSGRDITERK 468
Cdd:COG5809 210 GIAQGEVRFWTKDGRWRLLEASGAPIKKN-GEVDGIVIIFRDITERK 255
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
367-464 |
5.94e-12 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 63.04 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 367 WSPEGKPRWINSAVEEYIGYTVDECMVMDDFActVIYPGDAALVAPQFRNAQQGSRGDNLEFRCIRKDGSLMWLSVSWVP 446
Cdd:cd00130 8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLD--LIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTP 85
|
90
....*....|....*...
gi 1423782230 447 ITDSRGEFIGFRTSGRDI 464
Cdd:cd00130 86 IRDEGGEVIGLLGVVRDI 103
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
339-477 |
7.47e-12 |
|
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: 68.85 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 339 ASSMTRELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDEcmVMDDFACTVIYPGDAALVAPQFRNAQ 418
Cdd:COG5809 3 SSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDE--LLGTNILDFLHPDDEKELREILKLLK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423782230 419 QGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKEL 477
Cdd:COG5809 81 EGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRES 139
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
512-573 |
9.50e-11 |
|
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: 60.45 E-value: 9.50e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423782230 512 LLFIDLDHFKTLNDTLGHDKGDLLLQEVAKRLAASIPRS-DTVARVGGDEFVVVVGNLNPDRC 573
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAA 66
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
350-474 |
7.27e-10 |
|
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: 57.69 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 350 EEKFRAIADCTVnwEIWWS--PEGKPRWINSAVEEYIGYTVDECMVMDDFacTVIYPGDAALVAPQFRNAQQGSRGDN-L 426
Cdd:TIGR00229 2 EERYRAIFESSP--DAIIVidLEGNILYVNPAFEEIFGYSAEELIGRNVL--ELIPEEDREEVRERIERRLEGEPEPVsE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1423782230 427 EFRCIRKDGSLMWLSVSWVPITDSrGEFIGFRTSGRDITERKIADEKI 474
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
375-466 |
1.03e-09 |
|
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: 56.32 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 375 WINSAVEEYIGYTVDEcmVMD-DFACTVIYPGDAALVAPQFRnaqQGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGE 453
Cdd:pfam13426 6 YVNDAALRLLGYTREE--LLGkSITDLFAEPEDSERLREALR---EGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
|
90
....*....|...
gi 1423782230 454 FIGFRTSGRDITE 466
Cdd:pfam13426 81 LVGIIAILRDITE 93
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
376-458 |
2.15e-09 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 55.04 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 376 INSAVEEYIGYTVDECMVMDDFACTVIYPGDAALVAPQFRNAQQGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGE-- 453
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKpv 83
|
....*.
gi 1423782230 454 -FIGFR 458
Cdd:pfam08447 84 rVIGVA 89
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
345-486 |
5.15e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 59.09 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 345 ELRENEEKFRAIADCTVNWEIWWSPEGKPRWINSAVEEYIGYTVDECMVMDdfaCTVIYPGDAALVAPQFRNAQQGSRGD 424
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRP---LAELFPEDSPLRELLERALAEGQPVT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423782230 425 NLEFRCIRKDGSLMWLSVSWVPITDSRGEfIGFRTSGRDITERKIADEKIKELAFYDALTGL 486
Cdd:COG3852 78 EREVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
425-467 |
8.65e-08 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 49.10 E-value: 8.65e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1423782230 425 NLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITER 467
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
293-476 |
3.28e-07 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 54.07 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 293 TARDGFKARFGRDG--ATLIAITGTGLSLLLALLTWLMLTGRSRAmRLASSMTRELRENEE---KFRA---------IAD 358
Cdd:PRK13558 87 TAGDEAVARRAVDAdaAAYVPAVSDDATAAIAERIESAVPEHSRD-TEARMPISDLTVESDrrlKERAldeapvgitIAD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 359 CTvnweiwwSPEGKPRWINSAVEEYIGYTVDECMVMDdfaCTVIY-PGDAALVAPQFRNAQQGSRGDNLEFRCIRKDGSL 437
Cdd:PRK13558 166 AT-------LPDEPLIYINDAFERITGYSPDEVLGRN---CRFLQgEDTNEERVAELREAIDEERPTSVELRNYRKDGST 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423782230 438 MWLSVSWVPITDSRGE---FIGFRTsgrDITERKIADEKIKE 476
Cdd:PRK13558 236 FWNQVDIAPIRDEDGTvthYVGFQT---DVTERKEAELALQR 274
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
731-902 |
4.31e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 52.31 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 731 LARWAERPDLEHLTIAVNVSVQQLH----KPDfvdtvlatLQRTGARPDRLKLELTESVLVNNvQEIIEKMEALKAkgiv 806
Cdd:PRK11596 88 LAQWADFFVRHGLLASVNIDGPTLIalrqQPA--------ILRLIERLPWLRFELVEHIRLPK-DSPFASMCEFGP---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 807 FALDDFGIGYSSLSYLKRLPLAQLKIDRS-FV--------RDVLVdpndaviarTIVALAHSLGIGVIAEGVETEEQRAF 877
Cdd:PRK11596 155 LWLDDFGTGMANFSALSEVRYDYIKVARElFImlrqseegRNLFS---------QLLHLMNRYCRGVIVEGVETPEEWRD 225
|
170 180
....*....|....*....|....*
gi 1423782230 878 LASAGCYAYQGYLFCRPVGVEEFEA 902
Cdd:PRK11596 226 VQRSPAFAAQGYFLSRPAPFETLET 250
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
345-472 |
6.48e-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: 49.73 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 345 ELRENEEKFRAIAD------CTVNweiwwsPEGKPRWINSAVEEYIGYTVDEcmVMDDFACTVIYPGDAALVAPQFRNAQ 418
Cdd:COG5805 151 ILQEQEERLQTLIEnspdliCVID------TDGRILFINESIERLFGAPREE--LIGKNLLELLHPCDKEEFKERIESIT 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1423782230 419 QGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADE 472
Cdd:COG5805 223 EVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEE 276
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
367-464 |
4.17e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 43.56 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 367 WSPEGKPRWINSAVEEYIGYTVDECM---VMDDfactVIYPGDAALVAPQFRNAQQGSRGDNLEFRCIRKDGSLMWLSVS 443
Cdd:pfam00989 17 VDEDGRILYVNAAAEELLGLSREEVIgksLLDL----IPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVR 92
|
90 100
....*....|....*....|.
gi 1423782230 444 WVPITDSRGEFIGFRTSGRDI 464
Cdd:pfam00989 93 ASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
366-475 |
4.93e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 47.36 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 366 WWSPEGKPRWINSAVEEYIGYTVDECMVMDDFACTVIYPGDAALVAPQFRN-AQQGSRGDNLEFRCIRKDGSLMWLSVSW 444
Cdd:PRK13560 489 WKAEEGWPVELVSKNITQFGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEfAAQGVDRFEQEYRILGKGGAVCWIDDQS 568
|
90 100 110
....*....|....*....|....*....|.
gi 1423782230 445 VPITDSRGEFIGFRTSGRDITERKIADEKIK 475
Cdd:PRK13560 569 AAERDEEGQISHFEGIVIDISERKHAEEKIK 599
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
551-634 |
5.43e-05 |
|
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: 44.90 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 551 DTVARVGGDEFVVVVGNLNPDrceaarQTEALGETILSVLGSPYHLdeidyRSSASIGatvfngyqVSTDDLMKQADlAM 630
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLE------GALAVAERIREAVAELPSL-----RVTVSIG--------VAGDSLLKRAD-AL 175
|
....
gi 1423782230 631 YKSK 634
Cdd:COG3706 176 YQAR 179
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
332-478 |
2.35e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 45.05 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 332 RSRAMRlassmtRELRENEEKFR------AIADCTVnweiwwSPEGKPRWINSAVEEYIGYTVDECMVMDDFACTviYPG 405
Cdd:PRK09776 270 AFRAER------KHISESETRFRnameysAIGMALV------GTEGQWLQVNKALCQFLGYSQEELRGLTFQQLT--WPE 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423782230 406 DAALVAPQFRNAQQGS-RGDNLEFRCIRKDGSLMW--LSVSWVpiTDSRGEFIGFRTSGRDITERKIADEKIKELA 478
Cdd:PRK09776 336 DLNKDLQQVEKLLSGEiNSYSMEKRYYRRDGEVVWalLAVSLV--RDTDGTPLYFIAQIEDINELKRTEQVNERLM 409
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
367-468 |
8.07e-04 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 39.70 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 367 WSPEGKPRWINSAVEEYIGYTVDECMVMDDFActVIYPGDAALVAPQFRNAQQGsrGDNLEF-RCIRKDGSLMWLSVSWV 445
Cdd:pfam08448 11 LDPDGRVRYANAAAAELFGLPPEELLGKTLAE--LLPPEDAARLERALRRALEG--EEPIDFlEELLLNGEERHYELRLT 86
|
90 100
....*....|....*....|...
gi 1423782230 446 PITDSRGEFIGFRTSGRDITERK 468
Cdd:pfam08448 87 PLRDPDGEVIGVLVISRDITERR 109
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
344-476 |
1.67e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 42.35 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 344 RELRENEEKFRAIADCTVNWEIWWSPEGKPRWI-NSAVEEYIGYTVDECMVM----------DDFACTVI---YPGD--- 406
Cdd:PRK13560 325 RELLEKEDMLRAIIEAAPIAAIGLDADGNICFVnNNAAERMLGWSAAEVMGKplpgmdpelnEEFWCGDFqewYPDGrpm 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782230 407 AALVAPQFRNAQQGSRGDNLEFRCIRKDGSLMWLSVSWVPITDSRGEFIGFRTSGRDITERKIADEKIKE 476
Cdd:PRK13560 405 AFDACPMAKTIKGGKIFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLL 474
|
|
| |
