|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
265-909 |
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: 671.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 265 GAAARHASEDVAELAANEYLVVDGHDWTLAMSPQDDFKARFGRNAAWLIASIGTGLSLLLAFLTWLIMTGRGRAMRLASA 344
Cdd:COG5001 35 ALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 345 MTRELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMADFAGTLIHPDDQPRVAPEFQKGMLGA 424
Cdd:COG5001 115 LLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 425 RGDELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEERIKELAFFDALTHLPNRTLLLDRLKQAIT 504
Cdd:COG5001 195 RLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 505 ASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDEFVVVLGSLHEnheeaANQTEA 584
Cdd:COG5001 275 RARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDD-----PEDAEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 585 LGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEKGRNAVCFFDPDMQTVVLERAALEAA 664
Cdd:COG5001 350 VAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEAD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 665 LRQAIDENQFLLHYQAQVDGT--RVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWAcRPE 742
Cdd:COG5001 430 LRRALERGELELHYQPQVDLAtgRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQ-DAG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 743 MEHLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSL 822
Cdd:COG5001 509 LPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSL 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 823 SYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPIEG 902
Cdd:COG5001 589 SYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEE 668
|
....*..
gi 1716866594 903 FEEFLSR 909
Cdd:COG5001 669 LEALLRA 675
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
463-909 |
2.57e-128 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 401.75 E-value: 2.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 463 SGHDITERKIAEERIKELAFFDALTHLPNRTLLLDRLKQAITASARSEAcgALLFIDLDHFKTLNDTLGHDKGDMLLQQV 542
Cdd:PRK10060 219 SGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 543 AQRLAASVLESDTVARVGGDEFVVvlgsLHENHEEAAnqTEALGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASI 622
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLV----LASHTSQAA--LEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 623 DELLKQADLAMYKSKEKGRNAVCFFDPDMQTVVLERAALEAALRQAIDENQFLLHYQAQVDGT-RVTGAEALVRWQRPAR 701
Cdd:PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRgEVRSLEALVRWQSPER 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 702 GIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWacRPEMEHLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLK 781
Cdd:PRK10060 451 GLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW--RDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPID 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 782 LEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQ 861
Cdd:PRK10060 529 VELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQ 608
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1716866594 862 SLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPIEGFEEFLSR 909
Cdd:PRK10060 609 ALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
330-907 |
2.39e-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: 372.58 E-value: 2.39e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 330 LIMTGRGRAMRLASAMTRELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMADFAGTLIHPDD 409
Cdd:COG2200 3 LLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 410 QPRVAPEFQKGMLGARGDELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEERIKELAFFDALTHL 489
Cdd:COG2200 83 LALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 490 PNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDEFVVVLG 569
Cdd:COG2200 163 LLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 570 SLHENHEEAANQTEALgekiLAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEKGRNAVCFFDP 649
Cdd:COG2200 243 LLLAAAAAAAAALRLL----LLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 650 DMQtVVLERAALEAALRQAIDENQFLLHYQAQVD--GTRVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVL 727
Cdd:COG2200 319 AEA-RARRRLALESELREALEEGELRLYYQPIVDlrTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 728 EAACLQLAQWacRPEMEHLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTALRANG 807
Cdd:COG2200 398 ERALRQLARW--PERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 808 VVFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCH 887
Cdd:COG2200 476 VRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCD 555
|
570 580
....*....|....*....|
gi 1716866594 888 AYQGYYFCRPLPIEGFEEFL 907
Cdd:COG2200 556 YAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
663-901 |
1.19e-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: 348.00 E-value: 1.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 663 AALRQAIDENQFLLHYQAQVD--GTRVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWacR 740
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDlrTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 741 PEMEHLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYS 820
Cdd:cd01948 79 AGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 821 SLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPI 900
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
.
gi 1716866594 901 E 901
Cdd:cd01948 239 E 239
|
|
| CHASE1 |
COG3614 |
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms]; |
3-587 |
6.02e-108 |
|
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442832 [Multi-domain] Cd Length: 588 Bit Score: 345.52 E-value: 6.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 3 WARLVLLPIVVLSASLSVTWMLWDHERQAARHELQAQFDFSLGDAVSRIEQRMGTYELLLRGVQSMFAATGEMDRNRFRD 82
Cdd:COG3614 7 LLRRRLLPLLVLLLGLLLTALAWWAVRRAEEQRARARFERLADELASALEERLDAYEQVLRGLAGLFAASDDVTRAEFRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 83 YVATLDLDANFSGIQAVGMVPWVPAAQKDRHVAAMRGQGESSYAIEPAGVRDDYAPIIQREPYIGINRAPLGFDTWTDPT 162
Cdd:COG3614 87 YVASLDLLRRYPGIQGLGWAPRVPAAERAAFEAAARAEGFPDFRIRPAGERDEYFPITYIEPLDARNRRALGFDMASEPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 163 RRHAMEQARDSGMATLSGKVHLrVDATDKaRPGFILYLPIYTRGQSQDSVAQRRAHLLGWVYASFRMHDVMASLYGEQ-P 241
Cdd:COG3614 167 RRAAMERARDTGRPAASGPVTL-VQETDG-QPGFLLYLPVYRGGAPPDTVAERRAALRGFVYAPFRMDDLLAGVLGRLaD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 242 PGLSIAIYDGVEQSPATLLYKTPGAAARHASedvAELAANEYLVVDGHDWTLAMSPQDDFKARFGRNAAWLIASIGTGLS 321
Cdd:COG3614 245 RDLDLRLYDGTDPGPPQLLYDSSPAAPAAAA---PALSATRTLEVAGRTWTLEFRPTPAFEAALRSWLPWLVLLGGLLLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 322 LLLAFLTWLIMTGRGRAMRLASAMTRELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMADFA 401
Cdd:COG3614 322 LLLALLLLSLARRRRRAEALAAARAALRALRAAELRLRALLRRALLALLRNALALALLLAALLLLLARLLLLLAALLLLL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 402 GTLIHPDDQPRVAPEFQKGMLGARGDELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEERIKELA 481
Cdd:COG3614 402 ARALSAADLLLLQADLLLLRLLLLLRRRLLLVRDLRLGRGLGLGVVLLLDAILLDLLALAELELAAARAEVALAEALLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 482 FFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGG 561
Cdd:COG3614 482 LVVLLLALLLALLRLLLALAELAATAAREAAGAALLLDREAALLDAALEALLDLLGLLVLLLLAELLLRLGALLLGRALL 561
|
570 580
....*....|....*....|....*.
gi 1716866594 562 DEFVVVLGSLHENHEEAANQTEALGE 587
Cdd:COG3614 562 GGVGAGEGLVIIAELAALELELLRLE 587
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
662-901 |
2.82e-100 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 313.00 E-value: 2.82e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 662 EAALRQAIDENQFLLHYQAQVDGT--RVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWAC 739
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRtgRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 740 R-PEMEHltIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIG 818
Cdd:smart00052 81 QgPPPLL--ISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 819 YSSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPL 898
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
...
gi 1716866594 899 PIE 901
Cdd:smart00052 239 PLD 241
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
469-905 |
1.81e-98 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 322.43 E-value: 1.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 469 ERKIAEERIKELAFfdALTHLPNRTLLLDRLKQAItasARSEACgALLFIDLDhfkTLNDTLG---HDKGDMLLQQVAQR 545
Cdd:PRK13561 221 QRQYEEQSRNATRF--PVSDLPNKALLMALLEQVV---ARKQTT-ALMIITCE---TLRDTAGvlkEAQREILLLTLVEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 546 LAASVLESDTVARVGGDEFVVVLGSLhENHEEAANqteaLGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQaSIDEL 625
Cdd:PRK13561 292 LKSVLSPRMVLAQISGYDFAIIANGV-KEPWHAIT----LGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDL-TAEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 626 LKQADLAMYKSKEKGRNAVCFFDPDMQTVVLERAALEAALRQAIDENQFLLHYQAQVDGT--RVTGAEALVRWQRPARGI 703
Cdd:PRK13561 366 YSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRsgKLVSAEALLRMQQPDGSW 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 704 VPPADFIPLAEETGLIRALGSWVLEAACLQLAQWACRPEMehLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLE 783
Cdd:PRK13561 446 DLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIM--LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 784 ITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSLSYL---KRLPLDQLKIDRSFVrDVLvdPNDAVIAKAIVALA 860
Cdd:PRK13561 524 VTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFV-DGL--PEDDSMVAAIIMLA 600
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1716866594 861 QSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPIEGFEE 905
Cdd:PRK13561 601 QSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
469-901 |
1.18e-92 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 310.93 E-value: 1.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 469 ERKIAEERIKELAFFDALTHLPNRTLL---LDRLKQaitasarSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQR 545
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLhnyLDDLVD-------KAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 546 LAASVLESDTVARVGGDEFVVVlgslheNHEEAANQTEALGEKILAVLGTPYQLGEIEYRSTASVGATvfrgHQASIDE- 624
Cdd:PRK11359 437 FREKLKPDQYLCRIEGTQFVLV------SLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS----YDVGKNRd 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 625 -LLKQADLAMYKSKEKGRNAVCFFDPDMQTVVLERAALEAALRQAIDENQFLLHYQAQV--DGTRVTGAEALVRWQRPAR 701
Cdd:PRK11359 507 yLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIfaETGELYGIEALARWHDPLH 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 702 GIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWacRPEMEHL-TIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRL 780
Cdd:PRK11359 587 GHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEW--RSQNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQL 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 781 KLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALA 860
Cdd:PRK11359 665 TVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIG 744
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1716866594 861 QSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPIE 901
Cdd:PRK11359 745 QSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
487-904 |
1.65e-82 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 279.52 E-value: 1.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 487 THLPNRTLLLDRLKQAITASARSEAcGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDEFVV 566
Cdd:PRK11829 238 TELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 567 VLGslhenheEAANQTEA--LGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEKGRNAV 644
Cdd:PRK11829 317 LAR-------GTRRSFPAmqLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 645 CFFDPDMQTVVLERAALEAALRQAIDENQFLLHYQAQVD--GTRVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRAL 722
Cdd:PRK11829 390 MVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDmkRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 723 GSWVLEAACLQLAQWACRPEMehLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTA 802
Cdd:PRK11829 470 GNWVLEEACRILADWKARGVS--LPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 803 LRANGVVFSLDDFGIGYSSLSYL---KRLPLDQLKIDRSFVRDVlvdPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRD 879
Cdd:PRK11829 548 LQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQ 624
|
410 420
....*....|....*....|....*
gi 1716866594 880 FLAAAGCHAYQGYYFCRPLPIEGFE 904
Cdd:PRK11829 625 WLLEHGIQCGQGFLFSPPLPRAEFE 649
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
662-897 |
2.35e-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: 264.95 E-value: 2.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 662 EAALRQAIDENQFLLHYQAQVDGT--RVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWAC 739
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRtgRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 740 RPEMEhltIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGY 819
Cdd:pfam00563 81 GPDIK---LSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716866594 820 SSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRP 897
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
657-909 |
9.41e-77 |
|
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: 260.23 E-value: 9.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 657 ERAALEAALRQAIDENQFLLHYQAQVDGT--RVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQL 734
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIVDLKtgRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 735 AQW-ACRPemeHLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPDRLKLEITESVLVDnAQDVIQKMTALRANGVVFSLD 813
Cdd:COG4943 348 GDLlAADP---DFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 814 DFGIGYSSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYY 893
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|....*.
gi 1716866594 894 FCRPLPIEGFEEFLSR 909
Cdd:COG4943 504 FAKPLPAEEFIAWLAA 519
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
449-903 |
1.76e-69 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 250.75 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 449 PISDAKGDFIGFRTSGHDITERKIAEERIKELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLND 528
Cdd:PRK09776 633 PLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVND 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 529 TLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDEFVVVLgslhenHEEAANQTEALGEKIL-AVLGTPYQLGEIEYRST 607
Cdd:PRK09776 713 SAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLL------PDCNVESARFIATRIIsAINDYHFPWEGRVYRVG 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 608 ASVGATVFRGHQASIDELLKQADLAMYKSKEKGRNAVCFFDPDMQTVVLERAALEAA--LRQAIDENQFLLHYQAQVDGT 685
Cdd:PRK09776 787 ASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAeqWRMIKENQLMMLAHGVASPRI 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 686 --RVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWACRPEmehLTIAVNVSVQQFREPDFV 763
Cdd:PRK09776 867 peARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVASKG---LSIALPLSVAGLSSPTLL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 764 DNVLAIIRRAGARPDRLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDV 843
Cdd:PRK09776 944 PFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANL 1023
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 844 LVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPIEGF 903
Cdd:PRK09776 1024 HGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| CHASE |
pfam03924 |
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ... |
73-261 |
2.18e-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: 211.77 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 73 GEMDRNRFRDYVATLDLDANfsGIQAVGMVPWVPAAQKDRHVAAMRGQGESSYAIEPAGVRDDYAPIIQREPYIGINRAp 152
Cdd:pfam03924 1 DSVDREEFRRYAASLLLRRP--GIQGLGWAPRVPAAERAAFEAAVRAEGFPDFTIRPAGDRDEYFPIIYIEPLAGNNRA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 153 LGFDTWTDPTRRHAMEQARDSGMATLSGKVHLRVDAtdKARPGFILYLPIYtRGQSQDSVAQRRAHLLGWVYASFRMHDV 232
Cdd:pfam03924 78 LGFDMASEPVRREAIERARDTGEPVLSGPVTLVQDG--DGQPGFLLYLPVY-RGGPPDTVAERRAALLGFVYAPFRIDDL 154
|
170 180 190
....*....|....*....|....*....|
gi 1716866594 233 M-ASLYGEQPPGLSIAIYDGVEQSPATLLY 261
Cdd:pfam03924 155 LeAALLRLGEDGLDLALYDGTSASAPELLY 184
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
440-647 |
3.58e-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: 203.67 E-value: 3.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 440 LIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEERIKELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFID 519
Cdd:COG2199 73 ALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLID 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 520 LDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDEFVVVLgslhenHEEAANQTEALGEKILAVL-GTPYQ 598
Cdd:COG2199 153 LDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL------PGTDLEEAEALAERLREALeQLPFE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1716866594 599 LGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEKGRNAVCFF 647
Cdd:COG2199 227 LEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
482-645 |
2.11e-56 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 191.23 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 482 FFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGG 561
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 562 DEFVVVLgsLHENHEEAanqtEALGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEKGR 641
Cdd:cd01949 81 DEFAILL--PGTDLEEA----EALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGR 154
|
....
gi 1716866594 642 NAVC 645
Cdd:cd01949 155 NRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
481-642 |
6.23e-52 |
|
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: 178.99 E-value: 6.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 481 AFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVG 560
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 561 GDEFVVVLgsLHENHEEAANQTEALgEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEKG 640
Cdd:pfam00990 81 GDEFAILL--PETSLEGAQELAERI-RRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
..
gi 1716866594 641 RN 642
Cdd:pfam00990 158 RN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
479-647 |
1.13e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 175.51 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 479 ELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVAR 558
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 559 VGGDEFVVVLgsLHENHEEAanqtEALGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMYKSKE 638
Cdd:smart00267 81 LGGDEFALLL--PETSLEEA----IALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
|
....*....
gi 1716866594 639 KGRNAVCFF 647
Cdd:smart00267 155 AGRNQVAVY 163
|
|
| CHASE |
smart01079 |
This domain is found in the extracellular portion of receptor-like proteins - such as serine ... |
76-250 |
2.35e-50 |
|
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: 175.22 E-value: 2.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 76 DRNRFRDYVATLDLDANFSGIQAVGMVPWVPAAQKDRHVAAMRGQGESSYAI--EPAGVRDDYAPIIQREPYIGiNRAPL 153
Cdd:smart01079 5 SRAEFRRFALELQLNRRLPGIQGLGWAPRVPPAERAAFEAALRAGGPGLFNIrlAPDGERDEYFVITYIEPLAG-NEAAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 154 GFDTWTDPTRRHAMEQARDSGMATLSGKVHLRVDATDkaRPGFILYLPIYTRGQSQDSvaqRRAHLLGWVYASFRMHDVM 233
Cdd:smart01079 84 GLDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGD--GRGFLLRLPVYRGGPPTST---RREALWGFVSAVFRLDDLL 158
|
170
....*....|....*...
gi 1716866594 234 ASLYGE-QPPGLSIAIYD 250
Cdd:smart01079 159 EGLLGAlDLPGLDLALYD 176
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
480-648 |
9.61e-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: 141.71 E-value: 9.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 480 LAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARV 559
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 560 GGDEFVVVLgsLHENHEEAANQTEALGEKILAvLGTPYQLGEIeYRSTASVGATVFRGHQASIDELLKQADLAMYKSKEK 639
Cdd:TIGR00254 81 GGEEFVVIL--PGTPLEDALSKAERLRDAINS-KPIEVAGSET-LTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
....*....
gi 1716866594 640 GRNAVCFFD 648
Cdd:TIGR00254 157 GRNRVVVAD 165
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
662-908 |
1.26e-36 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 145.52 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 662 EAALRQAIDENQFLLHYQAQVDGT--RVTGAEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAaclqLAQWAc 739
Cdd:PRK10551 265 GKEILTGIKRGQFYVEYQPVVDTQtlRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFEL----IARDA- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 740 rPEMEHL-----TIAVNVSVQQFREPDFVDNVLAIirRAGARPD--RLKLEITESVLVDNaQDVIQKMTALRANGVVFSL 812
Cdd:PRK10551 340 -AELQKVlpvgaKLGINISPAHLHSDSFKADVQRL--LASLPADhfQIVLEITERDMVQE-EEATKLFAWLHSQGIEIAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 813 DDFGIGYSSLSYLKRLPLDQLKIDRSFVRDVLVDPNDAVIAKAIVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGY 892
Cdd:PRK10551 416 DDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGY 495
|
250
....*....|....*.
gi 1716866594 893 YFCRPLPIEGFEEFLS 908
Cdd:PRK10551 496 WISRPLPLEDFVRWLK 511
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
479-645 |
2.57e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 128.48 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 479 ELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVAR 558
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 559 VGGDEFVVVLgslhenHEEAANQTEALGEKI-LAVLGTPYQLGEIEYR--STASVGATVFRGHQASIDELLKQADLAMYK 635
Cdd:PRK09581 370 YGGEEFVVVM------PDTDIEDAIAVAERIrRKIAEEPFIISDGKERlnVTVSIGVAELRPSGDTIEALIKRADKALYE 443
|
170
....*....|
gi 1716866594 636 SKEKGRNAVC 645
Cdd:PRK09581 444 AKNTGRNRVV 453
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
347-568 |
5.64e-26 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 108.19 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 347 RELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMADFagTLIHPDDQPRVAPEFQKGMLGARG 426
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 427 DELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEERIKELAFFDALTHLPNRTLLLDRLKQAITAS 506
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1716866594 507 ARSEACGALLFIDLDHF-KTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDEFVVVL 568
Cdd:COG2202 162 VNPAAEELLGYSPEELLgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVW 224
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
484-652 |
2.67e-25 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 107.07 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 484 DALTHLPNRTLLLDRLKQAITASARSEACGALLfiDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDE 563
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLRNREPQNLYLALL--DIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 564 FVVVLgslhenheEAANQTEA--LGEKI-LAVLGTPYQLGEIEYRSTASVGATVFRGHQaSIDELLKQADLAMYKSKEKG 640
Cdd:PRK09894 210 FIICL--------KAATDEEAcrAGERIrQLIANHAITHSDGRINITATFGVSRAFPEE-TLDVVIGRADRAMYEGKQTG 280
|
170
....*....|..
gi 1716866594 641 RNAVCFFDPDMQ 652
Cdd:PRK09894 281 RNRVMFIDEQNV 292
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
475-650 |
8.90e-22 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 100.47 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 475 ERIKELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESD 554
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 555 TVARVGGDEFVVVLGSlhENHEEAANQTEAL-----GEKILAVLGTPyqlgeieYRSTASVG-ATVFRGHQASIDELLKQ 628
Cdd:PRK15426 472 VAGRVGGEEFCVVLPG--ASLAEAAQVAERIrlrinEKEILVAKSTT-------IRISASLGvSSAEEDGDYDFEQLQSL 542
|
170 180
....*....|....*....|..
gi 1716866594 629 ADLAMYKSKEKGRNAVCFFDPD 650
Cdd:PRK15426 543 ADRRLYLAKQAGRNRVCASDNA 564
|
|
| CHASE |
COG3452 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
3-832 |
2.15e-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: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 3 WARLVLLPIVVLSASLSVTWMLWDHERQAARHELQAQFDFSLGDAVSRIEQRMGTYELLLRGVQSMFAATGEMDRNRFRD 82
Cdd:COG3452 10 RRRPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEFER 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 83 YVATLdLDANfSGIQAVGMVP-WVpaaqkdrhvaamrgqgessyaiepagVRDDYapiiqrePYIGiNRAPLGFDTWTDP 161
Cdd:COG3452 90 LARNL-LEDY-PGIRNIALAPdGV--------------------------IRYVY-------PLAG-NEAALGLDLRTDP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 162 TRRHAMEQARDSGMATLSGKVHLRVDATdkarpGFILYLPIYTRGQSQdsvaqrraHLLGWVYASFRMHDVMA-SLYGEQ 240
Cdd:COG3452 134 EQRAAALRARESGQLVLAGPVNLVQGGR-----GLIGRLPVFLDGGDD--------RFWGFVSAVIDLDRLLDsAGLDDA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 241 PPGLSIAI--YDGVEQSPATLLYKTPGAAARHASEDVaelaaneylVVDGHDWTLAMSPQDDFKARfgRNAAWLIASIGT 318
Cdd:COG3452 201 QDGYQIALrgRDGDGAEGEVFYGDAALFDQDPVTLEV---------NLPGGSWQLAAAPKGGWLAS--PRNALPLRLAGL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 319 GLSLLLAFLTWLIMTG----RGRAMRLASAMTRELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEEC 394
Cdd:COG3452 270 LISLLLALLVYLLRQLlllrLLLLLLRLELIAAALLLLLLALDLLLELLLLLRLAEALLQERLRALALLAALEDLLLLKF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 395 MAMADFAGTLIHPDDQPRVAPEFQKGMLGARGDELEFRCIRKDGSLIWLSVswvpisdakgdfigfrtsgHDITERKIAE 474
Cdd:COG3452 350 DRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDGRV-------------------AVILIIEALE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 475 ERIKELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESD 554
Cdd:COG3452 411 LAEARLAALDQERDASDVALGAALVVLEALLIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLLGDALRERI 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 555 TVARVGGDEFVVVLGSLHENHEEAANQTEALGEKILAVLGTPYQLGEIEYRSTASVGATVFRGHQASIDELLKQADLAMY 634
Cdd:COG3452 491 RRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLLRAELILALLD 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 635 KSKEKGRNAVCFFDPDMQTVVLERAALEAALRQAIDENQFLLHYQAQVDGTRVTGAEALVRWQRPARGIVPPADFIPLAE 714
Cdd:COG3452 571 AKSGLSALELSGLLAGRAALDSLLLLLALALRQLDESALFILEELLLRLIIDLRIERLLLLLLGGEILLGELALLLLLLV 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 715 E----------------TGLIRALGSWVLEAACLQLAQWACRPEMEHLTIAVNVSVQQFREPDFVDNVLAIIRRAGARPD 778
Cdd:COG3452 651 LiilillsveeaglilaLSLLLALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGLLAELVAEALRLALALAQLLLRLL 730
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1716866594 779 RLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSLSYLKRLPLDQ 832
Cdd:COG3452 731 LAELLQLLLLLLGLILLELLLRLDGLLVELIALRLEILILTLLILDADEILADQ 784
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
468-642 |
1.43e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 85.65 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 468 TERKIAE--ERIKELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQR 545
Cdd:PRK10245 190 TATKLAEhkRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 546 LAASVLESDTVARVGGDEFVVVL-GSLHENHEEAANQTEAlGEKILAVLGTPYQLGEIeyrstaSVGATVFRGHQASIDE 624
Cdd:PRK10245 270 LQITLRGSDVIGRFGGDEFAVIMsGTPAESAITAMSRVHE-GLNTLRLPNAPQVTLRI------SVGVAPLNPQMSHYRE 342
|
170
....*....|....*...
gi 1716866594 625 LLKQADLAMYKSKEKGRN 642
Cdd:PRK10245 343 WLKSADLALYKAKNAGRN 360
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
347-477 |
3.59e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 82.38 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 347 RELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMADFAgtLIHPDDQPRVAPEFQKGMLGARG 426
Cdd:COG2202 130 EALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLD--LLHPEDRERLLELLRRLLEGGRE 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1716866594 427 D-ELEFRCIRKDGSLIWLSVSWVPISDAkGDFIGFRTSGHDITERKIAEERI 477
Cdd:COG2202 208 SyELELRLKDGDGRWVWVEASAVPLRDG-GEVIGVLGIVRDITERKRAEEAL 258
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
777-902 |
1.11e-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: 83.31 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 777 PDRLKLEITESVLVDnaQDVIQKMTALRANGVVFSLDDFGigySSLSYLKRLPL-DQLKIDrsfVRDVlvDPNDAviaKA 855
Cdd:COG3434 83 PERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFV---LDPEWDPLLPLaDIIKID---VLAL--DLEEL---AE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1716866594 856 IVALAQSLGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPIEG 902
Cdd:COG3434 150 LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
344-477 |
5.37e-16 |
|
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: 81.94 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 344 AMTRELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMADFagTLIHPDDQPRVAPEFQKGMLG 423
Cdd:COG5809 131 RMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSIL--ELIHSDDQENVAAFISQLLKD 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1716866594 424 ARGDELEFRCIRKDGSLIWLSVSWVPISDaKGDFIGFRTSGHDITERKIAEERI 477
Cdd:COG5809 209 GGIAQGEVRFWTKDGRWRLLEASGAPIKK-NGEVDGIVIIFRDITERKKLEELL 261
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
481-639 |
1.46e-15 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 80.05 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 481 AFFDALTHLPNRTllldRLKQAITA-----SARSeaCGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDT 555
Cdd:PRK09966 248 ALHDPLTGLANRA----AFRSGINTlmnnsDARK--TSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 556 VARVGGDEFVVVLGSLHENHEeaanqTEALGEKILAVLGTPYQLGEIEYRS-TASVGATVFRGHqASIDELLKQADLAMY 634
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSESE-----VQQICSALTQIFNLPFDLHNGHQTTmTLSIGYAMTIEH-ASAEKLQELADHNMY 395
|
....*
gi 1716866594 635 KSKEK 639
Cdd:PRK09966 396 QAKHQ 400
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
474-900 |
1.66e-15 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 81.06 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 474 EER------IKELAFFDALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVA---- 543
Cdd:PRK11059 215 EERsrfdtfIRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELInlls 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 544 ---QRLAASVLesdtvARVGGDEFVVVLGslHENHEEAanqtEALGEKIL-AVLGTPyqLGEIEYRSTA-SVGATVFRG- 617
Cdd:PRK11059 295 tfvMRYPGALL-----ARYSRSDFAVLLP--HRSLKEA----DSLASQLLkAVDALP--PPKMLDRDDFlHIGICAYRSg 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 618 --HQASIDEL---LKQADL------AMYKSK---EKGRNAVCFfdpdmqtvvleRAALEAALRQ---------AIDENQF 674
Cdd:PRK11059 362 qsTEQVMEEAemaLRSAQLqggngwFVYDKAqlpEKGRGSVRW-----------RTLLEQTLVRggprlyqqpAVTRDGK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 675 LLHYqaqvdgtrvtgaEALVRWQRPARGIVPPADFIPLAEETGLIRALGSWVLEAACLQLAQWAcrpemeHLTIAVNVSV 754
Cdd:PRK11059 431 VHHR------------ELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWP------EENLSINLSV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 755 QQFREPDFV----DNVLAIIRRAgaRPdRLKLEITESVLVDNAQDVIQKMTALRANGVVFSLDDFGIGYSSLSYLKRLPL 830
Cdd:PRK11059 493 DSLLSRAFQrwlrDTLLQCPRSQ--RK-RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNV 569
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1716866594 831 DQLKIDRSFVRDV-LVDPNDAVIAKAIVALAQSlGLGVIAEGVETEAQRDFLAAAGCHAYQGYYFCRPLPI 900
Cdd:PRK11059 570 ELIKLHPSLVRNIhKRTENQLFVRSLVGACAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
379-461 |
1.23e-14 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 70.06 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 379 INPSVQEYIGYTVEECMAMADFAGTLIHPDDQPRVAPEFQKGMLGARGDELEFRCIRKDGSLIWLSVSWVPISDAKGD-- 456
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKpv 83
|
....*.
gi 1716866594 457 -FIGFR 461
Cdd:pfam08447 84 rVIGVA 89
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
353-477 |
7.23e-14 |
|
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: 68.86 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 353 EEKFRAIADCTVN--WEVwwGQDGKPRWINPSVQEYIGYTVEECMAMADFagTLIHPDDQPRVApEFQKGMLGAR--GDE 428
Cdd:TIGR00229 2 EERYRAIFESSPDaiIVI--DLEGNILYVNPAFEEIFGYSAEELIGRNVL--ELIPEEDREEVR-ERIERRLEGEpePVS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1716866594 429 LEFRCIRKDGSLIWLSVSWVPISDAkGDFIGFRTSGHDITERKIAEERI 477
Cdd:TIGR00229 77 EERRVRRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
370-467 |
9.92e-14 |
|
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: 68.04 E-value: 9.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 370 WGQDGKPRWINPSVQEYIGYTVEECMAMADFAgtLIHPDDQPRVAPEFQKGMLGARGDELEFRCIRKDGSLIWLSVSWVP 449
Cdd:cd00130 8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLD--LIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTP 85
|
90
....*....|....*...
gi 1716866594 450 ISDAKGDFIGFRTSGHDI 467
Cdd:cd00130 86 IRDEGGEVIGLLGVVRDI 103
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
484-641 |
4.35e-13 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 72.68 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 484 DALTHLPNRTLLLDRLKQAITASARSEACGALLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLESDTVARVGGDE 563
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716866594 564 FVVVLgsLHENHEEAANQTEALGEKILAVlgtpyqlgEIEYRSTASVGATVFRGHQaSIDELLKQADLAMYKSKEKGR 641
Cdd:NF040885 424 FCIIL--IDYEEAEAQNLIERIRQHLRTI--------DPDKRVSFSWGAYQMQPGD-TLDDAYKAADERLYLNKKQKH 490
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
515-572 |
2.96e-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: 61.99 E-value: 2.96e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1716866594 515 LLFIDLDHFKTLNDTLGHDKGDMLLQQVAQRLAASVLES-DTVARVGGDEFVVVLGSLH 572
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDH 62
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
342-512 |
4.83e-11 |
|
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: 66.15 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 342 ASAMTRELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEEC--MAMADFagtlIHPDDQPRVAPEFQK 419
Cdd:COG5809 3 SSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELlgTNILDF----LHPDDEKELREILKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 420 GMLGARGDELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEERIKELA--FFDALTHLPNRTLLLD 497
Cdd:COG5809 79 LKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEekFRLIFNHSPDGIIVTD 158
|
170
....*....|....*
gi 1716866594 498 RLKQAITASARSEAC 512
Cdd:COG5809 159 LDGRIIYANPAACKL 173
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
348-475 |
3.71e-09 |
|
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: 60.13 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 348 ELRENEEKFRAIAD------CTVNwevwwgQDGKPRWINPSVQEYIGYTVEECMAMADFAgtLIHPDDQPRVAPEFQKGM 421
Cdd:COG5805 151 ILQEQEERLQTLIEnspdliCVID------TDGRILFINESIERLFGAPREELIGKNLLE--LLHPCDKEEFKERIESIT 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1716866594 422 LGARGDELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITERKIAEE 475
Cdd:COG5805 223 EVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEE 276
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
378-469 |
9.43e-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: 53.62 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 378 WINPSVQEYIGYTVEE--CMAMADFagtLIHPDDQPRVAPEFQkgmLGARGDELEFRCIRKDGSLIWLSVSWVPISDAKG 455
Cdd:pfam13426 6 YVNDAALRLLGYTREEllGKSITDL---FAEPEDSERLREALR---EGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 1716866594 456 DFIGFRTSGHDITE 469
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
734-910 |
1.69e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 56.55 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 734 LAQWACRPEMEHLTIAVNV------SVQQFREpdfvdnvlaiIRRAGARPDRLKLEITESVLVdnAQDVIqkMTALRANG 807
Cdd:PRK11596 88 LAQWADFFVRHGLLASVNIdgptliALRQQPA----------ILRLIERLPWLRFELVEHIRL--PKDSP--FASMCEFG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 808 VVFsLDDFGIGYSSLSYLKRLPLDQLKIDRS-FV--------RDVLVdpndaviakAIVALAQSLGLGVIAEGVETEAQR 878
Cdd:PRK11596 154 PLW-LDDFGTGMANFSALSEVRYDYIKVARElFImlrqseegRNLFS---------QLLHLMNRYCRGVIVEGVETPEEW 223
|
170 180 190
....*....|....*....|....*....|..
gi 1716866594 879 DFLAAAGCHAYQGYYFCRPLPIEGFEEFLSRL 910
Cdd:PRK11596 224 RDVQRSPAFAAQGYFLSRPAPFETLETLPLAL 255
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
428-470 |
6.53e-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: 49.49 E-value: 6.53e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1716866594 428 ELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSGHDITER 470
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
388-478 |
1.48e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 55.45 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 388 GYTVEECMAMADFAGTLIHPDDQPRVAPEFQKgmLGARGD---ELEFRCIRKDGSLIWLSVSWVPISDAKGDFIGFRTSG 464
Cdd:PRK13560 508 GYEPDEFISGKRMFAAIIHPADLEQVAAEVAE--FAAQGVdrfEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIV 585
|
90
....*....|....
gi 1716866594 465 HDITERKIAEERIK 478
Cdd:PRK13560 586 IDISERKHAEEKIK 599
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
359-479 |
3.05e-07 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 54.46 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 359 IADCTVnwevwwgQDGKPRWINPSVQEYIGYTVEECMamadfaGT----LIHPDDQPRVAPEFQKGMLGARGDELEFRCI 434
Cdd:PRK13558 163 IADATL-------PDEPLIYINDAFERITGYSPDEVL------GRncrfLQGEDTNEERVAELREAIDEERPTSVELRNY 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1716866594 435 RKDGSLIWLSVSWVPISDAKGD---FIGFRTsghDITERKIAEERIKE 479
Cdd:PRK13558 230 RKDGSTFWNQVDIAPIRDEDGTvthYVGFQT---DVTERKEAELALQR 274
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
348-489 |
6.42e-07 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 52.54 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 348 ELRENEEKFRAIADCTVNWEVWWGQDGKPRWINPSVQEYIGYTVEECMAMAdfAGTLIHPDDqpRVAPEFQKGML-GARG 426
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRP--LAELFPEDS--PLRELLERALAeGQPV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1716866594 427 DELEFRCIRKDGSLIWLSVSWVPISDAKGDfIGFRTSGHDITERKIAEERIKELAFFDALTHL 489
Cdd:COG3852 77 TEREVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
373-471 |
7.25e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 45.87 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 373 DGKPRWINPSVQEYIGYTVEECMAMADFAgtLIHPDDQPRVAPEFQKGMlgaRGDELEFRCIRK--DGSLIWLSVSWVPI 450
Cdd:pfam08448 14 DGRVRYANAAAAELFGLPPEELLGKTLAE--LLPPEDAARLERALRRAL---EGEEPIDFLEELllNGEERHYELRLTPL 88
|
90 100
....*....|....*....|.
gi 1716866594 451 SDAKGDFIGFRTSGHDITERK 471
Cdd:pfam08448 89 RDPDGEVIGVLVISRDITERR 109
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
373-467 |
2.32e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 44.33 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 373 DGKPRWINPSVQEYIGYTVEECMAMaDFAGTLIHPDDQPRVAPEFQKGMLGARGDELEFRCIRKDGSLIWLSVSWVPISD 452
Cdd:pfam00989 20 DGRILYVNAAAEELLGLSREEVIGK-SLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVRASPVRD 98
|
90
....*....|....*
gi 1716866594 453 AKGDFIGFRTSGHDI 467
Cdd:pfam00989 99 AGGEILGFLGVLRDI 113
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
554-637 |
4.65e-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: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716866594 554 DTVARVGGDEFVVVLgslhenHEEAANQTEALGEKILAVLGTPYQLgeieyRSTASVGatvfrghqASIDELLKQADlAM 633
Cdd:COG3706 116 DLVARYGGEEFAILL------PGTDLEGALAVAERIREAVAELPSL-----RVTVSIG--------VAGDSLLKRAD-AL 175
|
....
gi 1716866594 634 YKSK 637
Cdd:COG3706 176 YQAR 179
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
354-421 |
9.17e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 38.53 E-value: 9.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1716866594 354 EKFRAIADCTVNWeVW-WGQDGKPRWINPSVQEYIGYTVEECMAMadFAGTLIHPDDQPRVAPEFQKGM 421
Cdd:smart00091 1 ERLRAILESLPDG-IFvLDLDGRILYANPAAEELLGYSPEELIGK--SLLELIHPEDRERVQEALQRLL 66
|
|
| |
