|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
635-1194 |
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: 629.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 635 LAEEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSG 714
Cdd:COG5001 110 LALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 715 ELWNTHQNGELYAVIETISAVRNESGDITNYVSLVN----------DITLMKKHQDQLEHIAHYDVLTNLPNRSLLADRL 784
Cdd:COG5001 190 LALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLllvavlaiarLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 785 SQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGDEFVAVLAGLTNVEDCEQ 864
Cdd:COG5001 270 EQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 865 IIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRYYIFDTAQDDAVKVRRESLEA 944
Cdd:COG5001 350 VAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEAD 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 945 IRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAmAP 1024
Cdd:COG5001 430 LRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQD-AG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1025 NIPLSISVNIAAVQLQQADFANRLTLLLAAHpDVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGYSS 1104
Cdd:COG5001 509 LPDLRVAVNLSARQLRDPDLVDRVRRALAET-GLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSS 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1105 LTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMPAS 1184
Cdd:COG5001 588 LSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAE 667
|
570
....*....|
gi 2567559080 1185 NIPTWVSEWK 1194
Cdd:COG5001 668 ELEALLRARA 677
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
640-1192 |
2.52e-111 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 363.23 E-value: 2.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 640 LKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNpsmlnsdkqspefyeqLWRLL--KEQGHWSGE-L 716
Cdd:PRK10060 110 LSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQS----------------VFKLFmsRREAAASRRnI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 717 WNTHQNGELYAVIETISAV--------RNE---SGDITNYVSLV---NDITLMKKHQDQLEHIAHYDVLTNLPNRSLLAD 782
Cdd:PRK10060 174 RGFFRSGNAYEVERWIKTRkgqrlflfRNKfvhSGSGKNEIFLIcsgTDITEERRAQERLRILANTDSITGLPNRNAIQE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 783 RLSQAMLQCGRYQTslAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGDEFVaVLAGLTNVEDC 862
Cdd:PRK10060 254 LIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL-VLASHTSQAAL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 863 EQIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRYYIFDTAQDDAVKvrrESL 942
Cdd:PRK10060 331 EAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVF---EYL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 ---EAIRNALDNEQFVLYYQPKVNMRtGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQW 1019
Cdd:PRK10060 408 wldTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1020 QAMapNIPLSISVNIAAVQLQQADFANRLTLLLAaHPDVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFG 1099
Cdd:PRK10060 487 RDK--GINLRVAVNVSARQLADQTIFTALKQALQ-ELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFG 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1100 TGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIAR 1179
Cdd:PRK10060 564 TGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAK 643
|
570
....*....|...
gi 2567559080 1180 PMPASNIPTWVSE 1192
Cdd:PRK10060 644 PMPAVAFERWYKR 656
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
943-1185 |
2.22e-98 |
|
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: 312.56 E-value: 2.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 EAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAM 1022
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1023 APniPLSISVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGY 1102
Cdd:cd01948 81 GP--DLRLSVNLSARQLRDPDFLDRLLELLAETG-LPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1103 SSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMP 1182
Cdd:cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 2567559080 1183 ASN 1185
Cdd:cd01948 238 AEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
943-1183 |
1.44e-86 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 280.64 E-value: 1.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 EAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAM 1022
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1023 APNiPLSISVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGY 1102
Cdd:smart00052 82 GPP-PLLISINLSARQLISPDLVPRVLELLEETG-LPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1103 SSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMP 1182
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
.
gi 2567559080 1183 A 1183
Cdd:smart00052 240 L 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
943-1180 |
4.81e-75 |
|
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: 248.39 E-value: 4.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 EAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAm 1022
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1023 apNIPLSISVNIAAVQLQQADFANRLTLLLAAHPDVePRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGY 1102
Cdd:pfam00563 81 --GPDIKLSINLSPASLADPGFLELLRALLKQAGPP-PSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559080 1103 SSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARP 1180
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
766-928 |
3.89e-40 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 145.94 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 766 AHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIG 845
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 846 GDEFVAVLAGlTNVEDCEQIIERF-LLAASDPVTV-NNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNR 923
Cdd:TIGR00254 82 GEEFVVILPG-TPLEDALSKAERLrDAINSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 2567559080 924 YYIFD 928
Cdd:TIGR00254 161 VVVAD 165
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
504-764 |
1.63e-23 |
|
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: 105.83 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 504 EQAHNHLALKNKELRFNQLLQSIPSVSVQgYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPaaMQVDVRNAMQQM 583
Cdd:COG5809 2 KSSKMELQLRKSEQRFRSLFENAPDAILI-LDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHP--DDEKELREILKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 584 LKSKQPIPSGELTLMTKQGTEVNVFSShaYVHVPGQAPE---MFCIDVDLTKHKLAEEKLKLAA----SVFTHAREGIII 656
Cdd:COG5809 79 LKEGESRDELEFELRHKNGKRLEFSSK--LSPIFDQNGDiegMLAISRDITERKRMEEALRESEekfrLIFNHSPDGIIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 657 TDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELWNTHQNGELYaVIETISAVR 736
Cdd:COG5809 157 TDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWR-LLEASGAPI 235
|
250 260
....*....|....*....|....*...
gi 2567559080 737 NESGDITNYVSLVNDITLMKKHQDQLEH 764
Cdd:COG5809 236 KKNGEVDGIVIIFRDITERKKLEELLRK 263
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
167-526 |
2.93e-21 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 100.27 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 167 AAELQVFKFTQQLLMFLTLLVGAGMSFLLVRGNKRQVANINALTQSEDAHKKSKTQLLNVINGAKLGYWDWNYKTGEQIV 246
Cdd:COG2203 12 EVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILLIDALVLLSLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 247 NDEWLAMLGLSRHDINNHISDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVEYDEATQQP 326
Cdd:COG2203 92 TAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 327 LRLCGTHQDITERKLSELRD-KARTHVLELITSGESLSVVLTAIVNGIEQENPLMLCSVLLLDDEGKHLISGAAPSLPDF 405
Cdd:COG2203 172 GLILDIARLLTQRARLELERlALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 406 YNAaidgvEIGMGVGSCGTAAFTNQRVVVEDIATHPYWAPF-KAIANKAALGSCWSEPIRStQGKVLGTLAIYHRNSHKP 484
Cdd:COG2203 252 ELG-----RLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSlRELLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAF 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2567559080 485 TEANISLIEQTAYLASIAIEQAHNHLALKNKELRFNQLLQSI 526
Cdd:COG2203 326 TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALL 367
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
246-333 |
1.49e-17 |
|
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: 78.53 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNHISDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVEYDEAtqQ 325
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG--K 81
|
....*...
gi 2567559080 326 PLRLCGTH 333
Cdd:pfam08447 82 PVRVIGVA 89
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
764-921 |
4.54e-13 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 73.07 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 764 HIAHY---------DVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAV 834
Cdd:NF040885 330 HFRLYhnvsrenisDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISAS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 835 LREGDSLSRIGGDEFVAVLAGlTNVEDCEQIIERFL--LAASDPvtvNNImlnVSASIG-VTLYPQDNVdaDQLMRHADQ 911
Cdd:NF040885 410 IRKSDYGIRLGGDEFCIILID-YEEAEAQNLIERIRqhLRTIDP---DKR---VSFSWGaYQMQPGDTL--DDAYKAADE 480
|
170
....*....|
gi 2567559080 912 AMYAAKEAGK 921
Cdd:NF040885 481 RLYLNKKQKH 490
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
515-640 |
1.26e-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: 60.00 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 515 KELRFNQLLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQVDVRNaMQQMLKSKQPIPSGE 594
Cdd:TIGR00229 1 SEERYRAIFESSP-DAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRER-IERRLEGEPEPVSEE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2567559080 595 LTLMTKQGT----EVNVFSSHAYVHVPGqapeMFCIDVDLTKHKLAEEKL 640
Cdd:TIGR00229 79 RRVRRKDGSeiwvEVSVSPIRTNGGELG----VVGIVRDITERKEAEEAL 124
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
382-507 |
3.00e-09 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 57.01 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 382 CSVLLLDDEGKH-LISGAAPSLPDFYNaaidGVEIGMGVGSCGTAAFTNQRVVVEDIATHPYWAPFKAIANKAAlGSCWS 460
Cdd:smart00065 22 VLIYLVDENDRGeLVLVAADGLTLPTL----GIRFPLDEGLAGRVAETGRPLNIPDVEADPLFAEDLLGRYQGV-RSFLA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2567559080 461 EPIRStQGKVLGTLAIYHRNSHKP-TEANISLIEQTAYLASIAIEQAH 507
Cdd:smart00065 97 VPLVA-DGELVGVLALHNKKSPRPfTEEDEELLQALANQLAIALANAQ 143
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
233-336 |
3.27e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. 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: 55.33 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 233 GYWDWNYKTGEQIVNDEWLAMLGLSRHDINNHisDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQG 312
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
|
90 100
....*....|....*....|....
gi 2567559080 313 SGSVVeyDEATQQPLRLCGTHQDI 336
Cdd:cd00130 82 SLTPI--RDEGGEVIGLLGVVRDI 103
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
535-628 |
3.95e-08 |
|
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: 52.25 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 535 DYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQvDVRNAMQQmLKSKQPIPSGELTLMTKQGTEVNVFSSHAYV 614
Cdd:cd00130 9 DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLEN-LLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86
|
90
....*....|....
gi 2567559080 615 HVPGQAPEMFCIDV 628
Cdd:cd00130 87 RDEGGEVIGLLGVV 100
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
246-524 |
4.24e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 57.47 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNHISDwDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVeYDEATQQ 325
Cdd:PRK11359 161 CNRAFTEMFGYCISEASGMQPD-TLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV-YDVLAHL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 326 PlRLCGTHQDITERKlsELRDKARtHVLELITSGESLSVVLTAIVNGIEQENPLMLCSVLLLDDegKHLISGAAPSLPDF 405
Cdd:PRK11359 239 Q-NLVMTFSDITEER--QIRQLEG-NILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRN--GMPIHWASSSHGAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 406 YNAAidgveigmgvgscgtaaftnqrvvvediathpywapfkaiankaalgSCWSEPIRSTQGKVLGTLAIYHRNSHKPT 485
Cdd:PRK11359 313 YQNA-----------------------------------------------QSWSATIRQRDGAPAGTLQIKTSSGAETS 345
|
250 260 270
....*....|....*....|....*....|....*....
gi 2567559080 486 EANISLIEQTAYLASIAIEQAhnhlalKNKElRFNQLLQ 524
Cdd:PRK11359 346 AFIERVADISQHLAALALEQE------KSRQ-HIEQLIQ 377
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
518-585 |
3.50e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 48.55 E-value: 3.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559080 518 RFNQLLQSIPSVSVQgYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQvDVRNAMQQMLK 585
Cdd:smart00091 2 RLRAILESLPDGIFV-LDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRE-RVQEALQRLLS 67
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
518-605 |
1.74e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 47.80 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 518 RFNQLLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMqVDVRNAMQQMLKSKQPIPSGELTL 597
Cdd:pfam00989 2 DLRAILESLP-DGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDD-AEVAELLRQALLQGEESRGFEVSF 79
|
....*...
gi 2567559080 598 MTKQGTEV 605
Cdd:pfam00989 80 RVPDGRPR 87
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
246-345 |
2.49e-06 |
|
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: 47.67 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNHisDWDKLIHPNDKTLAMDVVQQHIhTKENYVV--EFRMQHSDDRWIWIQGSGSVVEYDeat 323
Cdd:TIGR00229 28 VNPAFEEIFGYSAEELIGR--NVLELIPEEDREEVRERIERRL-EGEPEPVseERRVRRKDGSEIWVEVSVSPIRTN--- 101
|
90 100
....*....|....*....|..
gi 2567559080 324 QQPLRLCGTHQDITERKLSELR 345
Cdd:TIGR00229 102 GGELGVVGIVRDITERKEAEEA 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
635-1194 |
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: 629.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 635 LAEEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSG 714
Cdd:COG5001 110 LALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 715 ELWNTHQNGELYAVIETISAVRNESGDITNYVSLVN----------DITLMKKHQDQLEHIAHYDVLTNLPNRSLLADRL 784
Cdd:COG5001 190 LALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLllvavlaiarLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 785 SQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGDEFVAVLAGLTNVEDCEQ 864
Cdd:COG5001 270 EQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 865 IIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRYYIFDTAQDDAVKVRRESLEA 944
Cdd:COG5001 350 VAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEAD 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 945 IRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAmAP 1024
Cdd:COG5001 430 LRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQD-AG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1025 NIPLSISVNIAAVQLQQADFANRLTLLLAAHpDVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGYSS 1104
Cdd:COG5001 509 LPDLRVAVNLSARQLRDPDLVDRVRRALAET-GLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSS 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1105 LTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMPAS 1184
Cdd:COG5001 588 LSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAE 667
|
570
....*....|
gi 2567559080 1185 NIPTWVSEWK 1194
Cdd:COG5001 668 ELEALLRARA 677
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
635-1190 |
4.96e-114 |
|
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: 367.57 E-value: 4.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 635 LAEEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSG 714
Cdd:COG2200 24 LALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 715 ELWNTHQNGELYAVIETISAVRNESGDITNYVSLVNDITLMKKHQDQLEHIAHYDVLTNLPNRSLLADRLSQAMLQCGRY 794
Cdd:COG2200 104 ALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 795 QTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGDEFVAVLAGLTNVEDCEQIIERFLLAAS 874
Cdd:COG2200 184 LLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 875 DPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRYYIFDTAQDDAVKvRRESLEAIRNALDNEQF 954
Cdd:COG2200 264 EPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARR-RLALESELREALEEGEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 955 VLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAMapNIPLSISVNI 1034
Cdd:COG2200 343 RLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPER--GLDLRLSVNL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1035 AAVQLQQADFANRLTLLLAAHpDVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGYSSLTYFRRLPVN 1114
Cdd:COG2200 421 SARSLLDPDFLERLLELLAEY-GLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPD 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559080 1115 LIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMPASNIPTWV 1190
Cdd:COG2200 500 YLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
640-1192 |
2.52e-111 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 363.23 E-value: 2.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 640 LKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNpsmlnsdkqspefyeqLWRLL--KEQGHWSGE-L 716
Cdd:PRK10060 110 LSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQS----------------VFKLFmsRREAAASRRnI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 717 WNTHQNGELYAVIETISAV--------RNE---SGDITNYVSLV---NDITLMKKHQDQLEHIAHYDVLTNLPNRSLLAD 782
Cdd:PRK10060 174 RGFFRSGNAYEVERWIKTRkgqrlflfRNKfvhSGSGKNEIFLIcsgTDITEERRAQERLRILANTDSITGLPNRNAIQE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 783 RLSQAMLQCGRYQTslAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGDEFVaVLAGLTNVEDC 862
Cdd:PRK10060 254 LIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL-VLASHTSQAAL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 863 EQIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRYYIFDTAQDDAVKvrrESL 942
Cdd:PRK10060 331 EAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVF---EYL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 ---EAIRNALDNEQFVLYYQPKVNMRtGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQW 1019
Cdd:PRK10060 408 wldTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1020 QAMapNIPLSISVNIAAVQLQQADFANRLTLLLAaHPDVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFG 1099
Cdd:PRK10060 487 RDK--GINLRVAVNVSARQLADQTIFTALKQALQ-ELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFG 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1100 TGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIAR 1179
Cdd:PRK10060 564 TGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAK 643
|
570
....*....|...
gi 2567559080 1180 PMPASNIPTWVSE 1192
Cdd:PRK10060 644 PMPAVAFERWYKR 656
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
943-1185 |
2.22e-98 |
|
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: 312.56 E-value: 2.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 EAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAM 1022
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1023 APniPLSISVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGY 1102
Cdd:cd01948 81 GP--DLRLSVNLSARQLRDPDFLDRLLELLAETG-LPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1103 SSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMP 1182
Cdd:cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 2567559080 1183 ASN 1185
Cdd:cd01948 238 AEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
943-1183 |
1.44e-86 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 280.64 E-value: 1.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 EAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAM 1022
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1023 APNiPLSISVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGY 1102
Cdd:smart00052 82 GPP-PLLISINLSARQLISPDLVPRVLELLEETG-LPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1103 SSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMP 1182
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
.
gi 2567559080 1183 A 1183
Cdd:smart00052 240 L 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
542-1192 |
2.04e-83 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 290.13 E-value: 2.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 542 YWNKASEYLYGYTAEEAIGQSLYDLIIPaamqvDVRNAMQQML-------KSKQPIPSGELTLMTKQGTEVNVFSSHAYV 614
Cdd:PRK11359 36 FFNPAAEKLWGYKREEVIGNNIDMLIPR-----DLRPAHPEYIrhnreggKARVEGMSRELQLEKKDGSKIWTRFALSKV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 615 HVPGQAPEMFCIDvDLTKHKLAEEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNP-SMLNSDK 693
Cdd:PRK11359 111 SAEGKVYYLALVR-DASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPdTLLNIPE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 694 QSPEFYEQLWRLLKEQGHWSGELWNTHQNGELYAVIETISAVRNESGDITNYVSLVNDIT-------------------- 753
Cdd:PRK11359 190 FPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITeerqirqlegnilaamcssp 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 754 -----------------------LM------------------------------------------------------- 755
Cdd:PRK11359 270 pfhemgeiicrniesvlneshvsLFalrngmpihwassshgaeyqnaqswsatirqrdgapagtlqiktssgaetsafie 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 756 ----------------KKHQDQLEHIAHYDVLTNLPNRSLLADRLSQAMlqcgRYQTSLAVVFLDLDGFKSVNDTYGHAV 819
Cdd:PRK11359 350 rvadisqhlaalaleqEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV----DKAVSPVVYLIGVDHFQDVIDSLGYAW 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 820 GDELLIALSVRMKAVLREGDSLSRIGGDEFVAVlAGLTNVEDCEQIIERFLLAASDPVTVNNIMLNVSASIGVTLypQDN 899
Cdd:PRK11359 426 ADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV-SLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVG 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 900 VDADQLMRHADQAMYAAKEAGKNRYYIFDTAQDDAVKVRRESLEAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQ 979
Cdd:PRK11359 503 KNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWH 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 980 HPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAMAPNIPlSISVNIAAVQLQQADFANRLTLLLAAHpDVE 1059
Cdd:PRK11359 583 DPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIP-ALSVNLSALHFRSNQLPNQVSDAMQAW-GID 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1060 PRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGV 1139
Cdd:PRK11359 661 GHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAI 740
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 2567559080 1140 IVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMPASNIPTWVSE 1192
Cdd:PRK11359 741 TSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSS 793
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
754-1184 |
2.41e-77 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 268.89 E-value: 2.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 754 LMKKHQDQLEHIAHYDVLTNLPNRSLLADRLSQAMLQCGRyqTSLAVVFLDldgfkSVNDTYG---HAVGDELLIALSVR 830
Cdd:PRK13561 219 LLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQT--TALMIITCE-----TLRDTAGvlkEAQREILLLTLVEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 831 MKAVLREGDSLSRIGGDEFVAVLAGLTNVEDCEQIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDnVDADQLMRHAD 910
Cdd:PRK13561 292 LKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGD-LTAEQLYSRAI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 911 QAMYAAKEAGKNRYYIFDTAQDDAVKVRRESLEAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLE 990
Cdd:PRK13561 371 SAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 991 FLPIIENNPMIVDIGEWVIDTALAQISQWQAMAPNIPLsiSVNIAAVQLQQADFANRLTLLLAAHpDVEPRYLELEVLET 1070
Cdd:PRK13561 451 LIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPL--SVNLSALQLMHPNMVADMLELLTRY-RIQPGTLILEVTES 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1071 SAIDDVNHVSTIMNACVALGVTFALDDFGTGYSSLTY---FRRLPVNLIKIDQSFVrdmLDDADDLAIVEGVIVLAKSFK 1147
Cdd:PRK13561 528 RRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQlqhMKSLPIDVLKIDKMFV---DGLPEDDSMVAAIIMLAQSLN 604
|
410 420 430
....*....|....*....|....*....|....*..
gi 2567559080 1148 RDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMPAS 1184
Cdd:PRK13561 605 LQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE 641
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
943-1180 |
4.81e-75 |
|
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: 248.39 E-value: 4.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 943 EAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQISQWQAm 1022
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1023 apNIPLSISVNIAAVQLQQADFANRLTLLLAAHPDVePRYLELEVLETSAIDDVNHVSTIMNACVALGVTFALDDFGTGY 1102
Cdd:pfam00563 81 --GPDIKLSINLSPASLADPGFLELLRALLKQAGPP-PSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559080 1103 SSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARP 1180
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
750-1182 |
8.12e-72 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 253.33 E-value: 8.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 750 NDITLMKKHQDqLEHIAHYDVLTNLPNRSLLADRLSQAMLQCGRYQtSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSV 829
Cdd:PRK11829 217 NQQLLADAYAD-MGRISHRFPVTELPNRSLFISLLEKEIASSTRTD-HFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 830 RMKAVLREGDSLSRIGGDEFVAVLAGLTNVEDCEQIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHA 909
Cdd:PRK11829 295 RIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 910 DQAMYAAKEAGKNRYYIFDTAQDDAVKVRRESLEAIRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPL 989
Cdd:PRK11829 375 STAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPS 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 990 EFLPIIENNPMIVDIGEWVIDTALAQISQWQAMAPNIPLsiSVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLE 1069
Cdd:PRK11829 455 GFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPL--SVNISGLQVQNKQFLPHLKTLISHYH-IDPQQLLLEITE 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1070 TSAIDDVNHVSTIMNACVALGVTFALDDFGTGYSSLTYFR---RLPVNLIKIDQSFVRDMLDDADDLAIVEGVivlAKSF 1146
Cdd:PRK11829 532 TAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLPEDDAIARIISCV---SDVL 608
|
410 420 430
....*....|....*....|....*....|....*.
gi 2567559080 1147 KRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMP 1182
Cdd:PRK11829 609 KVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
618-1184 |
1.53e-66 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 245.35 E-value: 1.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 618 GQAPEMFCIDVDLTKHK-----LAEEKLKLAASVFTHArEGIIITDENATIIDVNQAFTNITGYTREQAIG--------- 683
Cdd:PRK09776 509 GEVERLLGINMDMTEVRqlneaLFQEKERLHITLDSIG-EAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGvplltvlhi 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 684 ----HNPSMLNSDK----QSPEFYEQLWRLlkeqghwsgelwnTHQNGELYAVIETISAVRNESGDITNYVSLVNDITLM 755
Cdd:PRK09776 588 tfgdNGPLMENIYScltsRSAAYLEQDVVL-------------HCRSGGSYDVHYSITPLSTLDGENIGSVLVIQDVTES 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 756 KKHQDQLEHIAHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVL 835
Cdd:PRK09776 655 RKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSML 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 836 REGDSLSRIGGDEFvAVLAGLTNVEDCEQIIERFLLAASD-PVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMY 914
Cdd:PRK09776 735 RSSDVLARLGGDEF-GLLLPDCNVESARFIATRIISAINDyHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACY 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 915 AAKEAGKNRYYIFDTAQDDAVKVRRESL--EAIRNALDNEQFVLYYQ---PKVNMRTGVItgfEALIRWQHPQRGLLSPL 989
Cdd:PRK09776 814 AAKNAGRGRVTVYEPQQAAAHSEHRALSlaEQWRMIKENQLMMLAHGvasPRIPEARNHW---LISLRLWDPEGEIIDEG 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 990 EFLPIIENNPMIVDIGEWVIDTALAQISQWQAmAPNipLSISVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLE 1069
Cdd:PRK09776 891 AFRPAAEDPALMHALDRRVIHEFFRQAAKAVA-SKG--LSIALPLSVAGLSSPTLLPFLLEQLENSP-LPPRLLHLEITE 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1070 TSAIDDVNHVSTIMNACVALGVTFALDDFGTGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRD 1149
Cdd:PRK09776 967 TALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMK 1046
|
570 580 590
....*....|....*....|....*....|....*
gi 2567559080 1150 VIAEGVETIEHGTALLQLGCDLAQGYGIARPMPAS 1184
Cdd:PRK09776 1047 TIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLD 1081
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
698-927 |
5.50e-66 |
|
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: 224.47 E-value: 5.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 698 FYEQLWRLLKEQGHWSGELWNTHQNGELYAVIETISAVRNESGDITNYVSL--VNDITLMKKHQDQLEHIAHYDVLTNLP 775
Cdd:COG2199 44 LLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLlaLEDITELRRLEERLRRLATHDPLTGLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 776 NRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGDEFVAVLAG 855
Cdd:COG2199 124 NRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPG 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559080 856 lTNVEDCEQIIERFLLA-ASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRYYIF 927
Cdd:COG2199 204 -TDLEEAEALAERLREAlEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
938-1190 |
9.69e-65 |
|
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: 229.42 E-value: 9.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 938 RRESLEA-IRNALDNEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVDIGEWVIDTALAQI 1016
Cdd:COG4943 268 RRLSPRRrLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1017 SQWQAMAPniPLSISVNIAAVQLQQADFANRLTLLLAAHPdVEPRYLELEVLETSAIDdVNHVSTIMNACVALGVTFALD 1096
Cdd:COG4943 348 GDLLAADP--DFHISINLSASDLLSPRFLDDLERLLARTG-VAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1097 DFGTGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYG 1176
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|....
gi 2567559080 1177 IARPMPASNIPTWV 1190
Cdd:COG4943 504 FAKPLPAEEFIAWL 517
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
767-924 |
1.15e-63 |
|
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: 212.80 E-value: 1.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 767 HYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGG 846
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559080 847 DEFVAVLAGlTNVEDCEQIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNRY 924
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
766-923 |
2.58e-57 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 195.16 E-value: 2.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 766 AHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIG 845
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 846 GDEFVAVLAGLTNVEDCE--QIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNR 923
Cdd:pfam00990 81 GDEFAILLPETSLEGAQElaERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
764-927 |
7.82e-57 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 193.62 E-value: 7.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 764 HIAHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSR 843
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 844 IGGDEFVAVLAGlTNVEDCEQIIERFLLAASDPVTVNNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNR 923
Cdd:smart00267 81 LGGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 2567559080 924 YYIF 927
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
766-928 |
3.89e-40 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 145.94 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 766 AHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIG 845
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 846 GDEFVAVLAGlTNVEDCEQIIERF-LLAASDPVTV-NNIMLNVSASIGVTLYPQDNVDADQLMRHADQAMYAAKEAGKNR 923
Cdd:TIGR00254 82 GEEFVVILPG-TPLEDALSKAERLrDAINSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 2567559080 924 YYIFD 928
Cdd:TIGR00254 161 VVVAD 165
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
752-936 |
3.83e-34 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 139.38 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 752 ITLMKKH----QDQLEHIAHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIAL 827
Cdd:PRK15426 380 IRRMVSNmfvlQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 828 SVRMKAVLREGDSLSRIGGDEFVAVLAGlTNVEDCEQIIERFLLAASDP--VTVNNIMLNVSASIGV-TLYPQDNVDADQ 904
Cdd:PRK15426 460 AGLISSSLRAQDVAGRVGGEEFCVVLPG-ASLAEAAQVAERIRLRINEKeiLVAKSTTIRISASLGVsSAEEDGDYDFEQ 538
|
170 180 190
....*....|....*....|....*....|..
gi 2567559080 905 LMRHADQAMYAAKEAGKNRYYIFDTAQDDAVK 936
Cdd:PRK15426 539 LQSLADRRLYLAKQAGRNRVCASDNAHEREVK 570
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
510-762 |
8.81e-34 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 131.30 E-value: 8.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 510 LALKNKELRFNQLLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAaMQVDVRNAMQQMLKSKQP 589
Cdd:COG2202 4 EALEESERRLRALVESSP-DAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPE-DDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 590 IpSGELTLMTKQGTEVNVFSSHAYVHVP-GQAPEMFCIDVDLTKHKLAEEKLKLAA----SVFTHAREGIIITDENATII 664
Cdd:COG2202 82 W-RGELRNRRKDGSLFWVELSISPVRDEdGEITGFVGIARDITERKRAEEALRESEerlrLLVENAPDGIFVLDLDGRIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 665 DVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLkEQGHWSGELWNTHQNGE-LYAVIETISAVRNESGDIT 743
Cdd:COG2202 161 YVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLL-EGGRESYELELRLKDGDgRWVWVEASAVPLRDGGEVI 239
|
250
....*....|....*....
gi 2567559080 744 NYVSLVNDITLMKKHQDQL 762
Cdd:COG2202 240 GVLGIVRDITERKRAEEAL 258
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
924-1198 |
1.36e-33 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 137.05 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 924 YYIFDTAQddavKVRRESLEAIRNaldnEQFVLYYQPKVNMRTGVITGFEALIRWQHPQRGLLSPLEFLPIIENNPMIVD 1003
Cdd:PRK10551 255 YYLLSLRM----RPGKEILTGIKR----GQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1004 IG----EWVI-DTALAQisqwQAMAPNIPLSIsvNIAAVQLQQADFANRLTLLLAAHPdvePRYLELeVLETSAIDDVNH 1078
Cdd:PRK10551 327 LTqhlfELIArDAAELQ----KVLPVGAKLGI--NISPAHLHSDSFKADVQRLLASLP---ADHFQI-VLEITERDMVQE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1079 vstiMNAcVAL-------GVTFALDDFGTGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVI 1151
Cdd:PRK10551 397 ----EEA-TKLfawlhsqGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTV 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2567559080 1152 AEGVETIEHGTALLQLGCDLAQGYGIARPMPASNIPTWVSEWKTDDN 1198
Cdd:PRK10551 472 AEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTPQW 518
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
631-764 |
3.75e-31 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 123.60 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 631 TKHKLAEEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQG 710
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2567559080 711 HWSGELWNTHQNGELYAVIETISAVRNESGDITNYVSLVNDITLMKKHQDQLEH 764
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRE 134
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
756-923 |
5.49e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 128.09 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 756 KKHQDQLE-------HIAHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALS 828
Cdd:PRK09581 275 KRYQDALRnnleqsiEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 829 VRMKAVLREGDSLSRIGGDEFVAVLAGlTNVEDCEQIIERFLLA-ASDPVTVNNI--MLNVSASIGVTLYPQDNVDADQL 905
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVVVMPD-TDIEDAIAVAERIRRKiAEEPFIISDGkeRLNVTVSIGVAELRPSGDTIEAL 433
|
170
....*....|....*...
gi 2567559080 906 MRHADQAMYAAKEAGKNR 923
Cdd:PRK09581 434 IKRADKALYEAKNTGRNR 451
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
768-932 |
1.48e-27 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 114.01 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 768 YDVLTNLPNRSLLADRLSQAMLQcgRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDSLSRIGGD 847
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQLRN--REPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 848 EFVAVLAGLTNVEDCEqIIERFLLA-ASDPVTVNNIMLNVSASIGVTLYPQDnVDADQLMRHADQAMYAAKEAGKNRYYI 926
Cdd:PRK09894 209 EFIICLKAATDEEACR-AGERIRQLiANHAITHSDGRINITATFGVSRAFPE-ETLDVVIGRADRAMYEGKQTGRNRVMF 286
|
....*.
gi 2567559080 927 FDTAQD 932
Cdd:PRK09894 287 IDEQNV 292
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
504-764 |
1.63e-23 |
|
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: 105.83 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 504 EQAHNHLALKNKELRFNQLLQSIPSVSVQgYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPaaMQVDVRNAMQQM 583
Cdd:COG5809 2 KSSKMELQLRKSEQRFRSLFENAPDAILI-LDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHP--DDEKELREILKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 584 LKSKQPIPSGELTLMTKQGTEVNVFSShaYVHVPGQAPE---MFCIDVDLTKHKLAEEKLKLAA----SVFTHAREGIII 656
Cdd:COG5809 79 LKEGESRDELEFELRHKNGKRLEFSSK--LSPIFDQNGDiegMLAISRDITERKRMEEALRESEekfrLIFNHSPDGIIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 657 TDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELWNTHQNGELYaVIETISAVR 736
Cdd:COG5809 157 TDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWR-LLEASGAPI 235
|
250 260
....*....|....*....|....*...
gi 2567559080 737 NESGDITNYVSLVNDITLMKKHQDQLEH 764
Cdd:COG5809 236 KKNGEVDGIVIIFRDITERKKLEELLRK 263
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
649-789 |
1.94e-23 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 105.76 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 649 HAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELWNTHQNGELYAV 728
Cdd:TIGR02938 12 QAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLA 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559080 729 IETISAVRNESGDITNYVSLVNDITLMKKHQDQLEHIAHY--DVLTNLPNRSLLADRLSQAML 789
Cdd:TIGR02938 92 ELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLieSVVDAAPVAFVLLDPTGRVIL 154
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
167-526 |
2.93e-21 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 100.27 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 167 AAELQVFKFTQQLLMFLTLLVGAGMSFLLVRGNKRQVANINALTQSEDAHKKSKTQLLNVINGAKLGYWDWNYKTGEQIV 246
Cdd:COG2203 12 EVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILLIDALVLLSLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 247 NDEWLAMLGLSRHDINNHISDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVEYDEATQQP 326
Cdd:COG2203 92 TAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 327 LRLCGTHQDITERKLSELRD-KARTHVLELITSGESLSVVLTAIVNGIEQENPLMLCSVLLLDDEGKHLISGAAPSLPDF 405
Cdd:COG2203 172 GLILDIARLLTQRARLELERlALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 406 YNAaidgvEIGMGVGSCGTAAFTNQRVVVEDIATHPYWAPF-KAIANKAALGSCWSEPIRStQGKVLGTLAIYHRNSHKP 484
Cdd:COG2203 252 ELG-----RLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSlRELLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAF 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2567559080 485 TEANISLIEQTAYLASIAIEQAHNHLALKNKELRFNQLLQSI 526
Cdd:COG2203 326 TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALL 367
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
753-923 |
2.65e-20 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 94.13 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 753 TLMKKHQDQLEHIAHYDVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMK 832
Cdd:PRK10245 192 TKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 833 AVLREGDSLSRIGGDEFVAVLAGlTNVEDCEQIIERF---LLAASDPVTvNNIMLNVsaSIGVT-LYPQDNvDADQLMRH 908
Cdd:PRK10245 272 ITLRGSDVIGRFGGDEFAVIMSG-TPAESAITAMSRVhegLNTLRLPNA-PQVTLRI--SVGVApLNPQMS-HYREWLKS 346
|
170
....*....|....*
gi 2567559080 909 ADQAMYAAKEAGKNR 923
Cdd:PRK10245 347 ADLALYKAKNAGRNR 361
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
769-1174 |
2.69e-20 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 96.86 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 769 DVLTNLPNRSLLADRLsQAMLQCGRYQTSLAVVFL-DLDGFKSVNDTYGHAVGDELLIAL-SVRMKAVLREGDS-LSRIG 845
Cdd:PRK11059 231 DAKTGLGNRLFFDNQL-ATLLEDQEMVGAHGVVMLiRLPDFDLLQEEWGESQVEELLFELiNLLSTFVMRYPGAlLARYS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 846 GDEFVAVLAGLTnVEDCEQIIERFL-----LAASDPVTVNNIMlnvsaSIGVTLYpQDNVDADQLMRHADQAMYAAKEAG 920
Cdd:PRK11059 310 RSDFAVLLPHRS-LKEADSLASQLLkavdaLPPPKMLDRDDFL-----HIGICAY-RSGQSTEQVMEEAEMALRSAQLQG 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 921 KNRYYIFDTAQD-DAVK--VRRESLeaIRNALDNEQFVLYYQPKVNmRTGVITGFEALIRWQHPQRGLLSPLEFLPIIEN 997
Cdd:PRK11059 383 GNGWFVYDKAQLpEKGRgsVRWRTL--LEQTLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRDGQGELLSAELFMPMVQQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 998 NPMIVDIGEWVIDTALAQISQWQamapniPLSISVNIAAVQLQQADFANRL-TLLLAAHPDVEPRyLELEVLEtsaiDDV 1076
Cdd:PRK11059 460 LGLSEQYDRQVIERVLPLLRYWP------EENLSINLSVDSLLSRAFQRWLrDTLLQCPRSQRKR-LIFELAE----ADV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1077 -NHVS---TIMNACVALGVTFALDDFGTGYSSLTYFRRLPVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIA 1152
Cdd:PRK11059 529 cQHISrlrPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFA 608
|
410 420
....*....|....*....|..
gi 2567559080 1153 EGVETIEHGTALLQLGCDLAQG 1174
Cdd:PRK11059 609 TGVESREEWQTLQELGVSGGQG 630
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
637-762 |
1.09e-17 |
|
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: 80.41 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 637 EEKLKlaaSVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHW-SGE 715
Cdd:TIGR00229 2 EERYR---AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPvSEE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2567559080 716 LWNTHQNGELYAVIETISAVRnESGDITNYVSLVNDITLMKKHQDQL 762
Cdd:TIGR00229 79 RRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
246-333 |
1.49e-17 |
|
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: 78.53 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNHISDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVEYDEAtqQ 325
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG--K 81
|
....*...
gi 2567559080 326 PLRLCGTH 333
Cdd:pfam08447 82 PVRVIGVA 89
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
360-504 |
3.49e-17 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 79.43 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 360 ESLSVVLTAIVNGIEQENPLMLCSVLLLDDEGKHLISGAAPSlpdfynAAIDGVEIGMGVGSCGTAAFTNQRVVVEDIAT 439
Cdd:pfam13185 2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAAD------ELSAALDDPPGEGLVGEALRTGRPVIVNDLAA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559080 440 HPYWAPFKAIAnkAALGSCWSEPIRStQGKVLGTLAIYHRNSHKPTEANISLIEQTAYLASIAIE 504
Cdd:pfam13185 76 DPAKKGLPAGH--AGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
761-917 |
7.41e-17 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 84.29 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 761 QLEHIAHYDVLTNLPNRSLLADRLSqAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLREGDS 840
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559080 841 LSRIGGDEFVAVLAGLTNVEDCEQIIERFLLAASDPVTVNN-IMLNVSASIGVTLyPQDNVDADQLMRHADQAMYAAK 917
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNgHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAK 398
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
522-762 |
2.32e-16 |
|
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: 83.63 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 522 LLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPaAMQVDVRNAMQQMLKSKQPIpsGELTLMTKQ 601
Cdd:COG5805 39 ILENLP-DAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEK-EYHYRVKTRIERLQKGYDVV--MIEQIYCKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 602 GTEVNVFSSHAYVHVPGQAPEMFCIDvDLTKHKLAEEKLKLAA----SVFTHAREGIIITDENATIIDVNQAFTNITGYT 677
Cdd:COG5805 115 GELIYVEVKLFPIYNQNGQAAILALR-DITKKKKIEEILQEQEerlqTLIENSPDLICVIDTDGRILFINESIERLFGAP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 678 REQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELWNTHQNGELYAVIETISAVRNESGDITNYVSLVNDITlMKK 757
Cdd:COG5805 194 REELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDIT-EKK 272
|
....*
gi 2567559080 758 HQDQL 762
Cdd:COG5805 273 EAEEL 277
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
662-753 |
8.13e-16 |
|
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: 74.03 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 662 TIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQghWSGELWNTHQNGELYAVIETISAVRNESGD 741
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
|
90
....*....|..
gi 2567559080 742 ITNYVSLVNDIT 753
Cdd:pfam13426 81 LVGIIAILRDIT 92
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
339-507 |
8.93e-16 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 76.86 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 339 RKLSELRDkarthVLELITSGESLSVVLTAIVNGIEQenpLM---LCSVLLLDDEGKHLISGAAPSLPDfynAAIDGVEI 415
Cdd:COG3605 1 EMLKALRR-----ISEAVASALDLDEALDRIVRRIAE---ALgvdVCSIYLLDPDGGRLELRATEGLNP---EAVGKVRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 416 GMGVGSCGTAAFTNQRVVVEDIATHPYWAPFKAIAN---KAALGScwsePIRStQGKVLGTLAIYHRNSHKPTEANISLI 492
Cdd:COG3605 70 PLGEGLVGLVAERGEPLNLADAASHPRFKYFPETGEegfRSFLGV----PIIR-RGRVLGVLVVQSREPREFTEEEVEFL 144
|
170
....*....|....*
gi 2567559080 493 EQTAYLASIAIEQAH 507
Cdd:COG3605 145 VTLAAQLAEAIANAE 159
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
650-752 |
5.07e-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: 69.20 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 650 AREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELWNTHQNGELYAVI 729
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 2567559080 730 ETISAVRNESGDITNYVSLVNDI 752
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
626-765 |
1.48e-13 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 75.26 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 626 IDVDLTkhklAEEKLKLAASVFTHAREGIII---TDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQL 702
Cdd:PRK13558 137 PISDLT----VESDRRLKERALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAEL 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559080 703 WRLLKEQGHWSGELWNTHQNGELYAVIETISAVRNESGDITNYVSLVNDITLMK-----------KHQDQLEHI 765
Cdd:PRK13558 213 REAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKeaelalqrerrKLQRLLERV 286
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
637-767 |
1.66e-13 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 73.34 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 637 EEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDkqSPEFYEQLWRLLKE-QGHWSGE 715
Cdd:COG3852 3 RESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPE--DSPLRELLERALAEgQPVTERE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559080 716 LWNTHQNGELYAVIETISAVRNESGDiTNYVSLVNDITLMKKHQDQLEH-------------IAH 767
Cdd:COG3852 81 VTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRaeklaavgelaagLAH 144
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
511-644 |
1.75e-13 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 73.34 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 511 ALKNKELRFNQLLQSIPSvSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAmqvDVRNAMQQMLKSKQPI 590
Cdd:COG3852 1 ALRESEELLRAILDSLPD-AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS---PLRELLERALAEGQPV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2567559080 591 PSGELTLMTKQGTEVNVFSSHAYVHVPGQAPEMFCIDVDLTKHKLAEEKLKLAA 644
Cdd:COG3852 77 TEREVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
764-921 |
4.54e-13 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 73.07 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 764 HIAHY---------DVLTNLPNRSLLADRLSQAMLQCGRYQTSLAVVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAV 834
Cdd:NF040885 330 HFRLYhnvsrenisDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISAS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 835 LREGDSLSRIGGDEFVAVLAGlTNVEDCEQIIERFL--LAASDPvtvNNImlnVSASIG-VTLYPQDNVdaDQLMRHADQ 911
Cdd:NF040885 410 IRKSDYGIRLGGDEFCIILID-YEEAEAQNLIERIRqhLRTIDP---DKR---VSFSWGaYQMQPGDTL--DDAYKAADE 480
|
170
....*....|
gi 2567559080 912 AMYAAKEAGK 921
Cdd:NF040885 481 RLYLNKKQKH 490
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
462-640 |
7.99e-13 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 70.05 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 462 PIRSTQGKVLGTLAIYHrnshkpteaNISliEQtaylasIAIEQahnhlALKNKELRFNQLLQSIPsVSVQGYDYEGNTR 541
Cdd:COG2202 104 PVRDEDGEITGFVGIAR---------DIT--ER------KRAEE-----ALRESEERLRLLVENAP-DGIFVLDLDGRIL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 542 YWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQvDVRNAMQQMLKSKQPIPSGELTLMTKQGTEVNVFSSHAYVHVPGQAP 621
Cdd:COG2202 161 YVNPAAEELLGYSPEELLGKSLLDLLHPEDRE-RLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGGEVI 239
|
170
....*....|....*....
gi 2567559080 622 EMFCIDVDLTKHKLAEEKL 640
Cdd:COG2202 240 GVLGIVRDITERKRAEEAL 258
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
649-752 |
1.16e-12 |
|
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: 65.52 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 649 HAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGE--LWNTHQNGELY 726
Cdd:pfam00989 9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFevSFRVPDGRPRH 88
|
90 100
....*....|....*....|....*.
gi 2567559080 727 AVIETiSAVRNESGDITNYVSLVNDI 752
Cdd:pfam00989 89 VEVRA-SPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
211-345 |
1.64e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 68.90 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 211 QSEDAHKKSKTQLLNVINGAKLGYWDWNYKTGEQIVNDEWLAMLGLSRHDINNHisDWDKLIHPNDKTLAMDVVQQHIHT 290
Cdd:COG2202 127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEG 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559080 291 -KENYVVEFRMQHSDDRWIWIQGSGSVVEYDeatQQPLRLCGTHQDITERKLSELR 345
Cdd:COG2202 205 gRESYELELRLKDGDGRWVWVEASAVPLRDG---GEVIGVLGIVRDITERKRAEEA 257
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
361-503 |
2.44e-11 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 62.50 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 361 SLSVVLTAIVNGIEQENPLMLCSVLLLDDEGKHLISgaapslPDFYNAAIDGVEIGMGVGscGTAAFTNQRVVVEDIATH 440
Cdd:pfam01590 1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLP------PGARWLKAAGLEIPPGTG--VTVLRTGRPLVVPDAAGD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559080 441 PYWAPFKAIANKAALGSCWSEPIRStQGKVLGTLAIYHRnSHKPTEANISLIEQTAYLASIAI 503
Cdd:pfam01590 73 PRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP-RPPFTEEELELLEVLADQVAIAL 133
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
515-640 |
1.26e-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: 60.00 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 515 KELRFNQLLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQVDVRNaMQQMLKSKQPIPSGE 594
Cdd:TIGR00229 1 SEERYRAIFESSP-DAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRER-IERRLEGEPEPVSEE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2567559080 595 LTLMTKQGT----EVNVFSSHAYVHVPGqapeMFCIDVDLTKHKLAEEKL 640
Cdd:TIGR00229 79 RRVRRKDGSeiwvEVSVSPIRTNGGELG----VVGIVRDITERKEAEEAL 124
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
211-411 |
4.93e-10 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 61.58 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 211 QSEDAHKKSKTQLLNVINGAKLGYWDWNYKTGEQIVNDEWLAMLGLSRHDINNHisDWDKLIHPNDKTLAMDVVQQHIHT 290
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 291 KENYVVEFRMQHSDDRWIWIQGSGSVVeYDEAtQQPLRLCGTHQDITERKLSELRDKARTHVLELITSGESLSVVLTAIV 370
Cdd:COG2202 79 GGVWRGELRNRRKDGSLFWVELSISPV-RDED-GEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2567559080 371 NGIEQENPLMLCSVLLLDDE--GKHLISGAAPSLPDFYNAAID 411
Cdd:COG2202 157 GRILYVNPAAEELLGYSPEEllGKSLLDLLHPEDRERLLELLR 199
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
1050-1185 |
1.07e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 62.13 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1050 LLLAAHPDVEP-RYLELEVLETSAIDDvnhvsTIMNACVAL---GVTFALDDF--GTGYSSLtyfrrLP-VNLIKIDQSf 1122
Cdd:COG3434 72 LLLSDLPELLPpERVVLEILEDVEPDE-----ELLEALKELkekGYRIALDDFvlDPEWDPL-----LPlADIIKIDVL- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559080 1123 vrdMLDDADDLAIVEgvivLAKSFKRDVIAEGVETIEHGTALLQLGCDLAQGYGIARPMPASN 1185
Cdd:COG3434 141 ---ALDLEELAELVA----RLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
800-892 |
1.50e-09 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 57.37 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 800 VVFLDLDGFKSVNDTYGHAVGDELLIALSVRMKAVLRE-GDSLSRIGGDEFVAVLaGLTNVEDCEQIIERFLLAASdpvT 878
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVS-GLDHPAAAVAFAEDMREAVS---A 79
|
90
....*....|....*
gi 2567559080 879 VN-NIMLNVSASIGV 892
Cdd:cd07556 80 LNqSEGNPVRVRIGI 94
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
382-507 |
3.00e-09 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 57.01 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 382 CSVLLLDDEGKH-LISGAAPSLPDFYNaaidGVEIGMGVGSCGTAAFTNQRVVVEDIATHPYWAPFKAIANKAAlGSCWS 460
Cdd:smart00065 22 VLIYLVDENDRGeLVLVAADGLTLPTL----GIRFPLDEGLAGRVAETGRPLNIPDVEADPLFAEDLLGRYQGV-RSFLA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2567559080 461 EPIRStQGKVLGTLAIYHRNSHKP-TEANISLIEQTAYLASIAIEQAH 507
Cdd:smart00065 97 VPLVA-DGELVGVLALHNKKSPRPfTEEDEELLQALANQLAIALANAQ 143
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
233-336 |
3.27e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. 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: 55.33 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 233 GYWDWNYKTGEQIVNDEWLAMLGLSRHDINNHisDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQG 312
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
|
90 100
....*....|....*....|....
gi 2567559080 313 SGSVVeyDEATQQPLRLCGTHQDI 336
Cdd:cd00130 82 SLTPI--RDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
663-749 |
9.30e-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: 53.50 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 663 IIDVNQAFTNITGYTREQAIGHNPSMLNS----DKqsPEFYEQLWRLLKEQGHWSGELWNTHQNGELYAVIETISAVRNE 738
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhpdDR--ERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|.
gi 2567559080 739 SGDITNYVSLV 749
Cdd:pfam08447 79 NGKPVRVIGVA 89
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
202-379 |
1.01e-08 |
|
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: 59.22 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 202 QVANINALTQSEDAHKKSKTQLLNVINGAKLGYWDWNYKtgEQI--VNDEWLAMLGLSRHD-INNHISDwdkLIHPNDKT 278
Cdd:COG5809 122 ISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLD--GRIiyANPAACKLLGISIEElIGKSILE---LIHSDDQE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 279 LAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVEYDEatqQPLRLCGTHQDITERKLSElrdkarthvlELITS 358
Cdd:COG5809 197 NVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNG---EVDGIVIIFRDITERKKLE----------ELLRK 263
|
170 180
....*....|....*....|....*
gi 2567559080 359 GESLSVV--LTAivnGIEQE--NPL 379
Cdd:COG5809 264 SEKLSVVgeLAA---GIAHEirNPL 285
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
637-764 |
1.11e-08 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 59.01 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 637 EEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDkqspefyEQLWRLLKEQGHWSGEL 716
Cdd:COG3829 7 KELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPN-------SPLLEVLKTGKPVTGVI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2567559080 717 WNThqNGELYAVIETISAVRnESGDITNYVSLVNDITLMKKHQDQLEH 764
Cdd:COG3829 80 QKT--GGKGKTVIVTAIPIF-EDGEVIGAVETFRDITELKRLERKLRE 124
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
644-707 |
2.30e-08 |
|
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: 52.02 E-value: 2.30e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559080 644 ASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLK 707
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
839-917 |
3.36e-08 |
|
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: 54.53 E-value: 3.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2567559080 839 DSLSRIGGDEFVAVLAGlTNVEDCEQIIERFLLAASDPVTVnnimlNVSASIGVTlypqdnvdADQLMRHADqAMYAAK 917
Cdd:COG3706 116 DLVARYGGEEFAILLPG-TDLEGALAVAERIREAVAELPSL-----RVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
535-628 |
3.95e-08 |
|
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: 52.25 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 535 DYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQvDVRNAMQQmLKSKQPIPSGELTLMTKQGTEVNVFSSHAYV 614
Cdd:cd00130 9 DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLEN-LLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86
|
90
....*....|....
gi 2567559080 615 HVPGQAPEMFCIDV 628
Cdd:cd00130 87 RDEGGEVIGLLGVV 100
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
246-524 |
4.24e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 57.47 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNHISDwDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVeYDEATQQ 325
Cdd:PRK11359 161 CNRAFTEMFGYCISEASGMQPD-TLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV-YDVLAHL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 326 PlRLCGTHQDITERKlsELRDKARtHVLELITSGESLSVVLTAIVNGIEQENPLMLCSVLLLDDegKHLISGAAPSLPDF 405
Cdd:PRK11359 239 Q-NLVMTFSDITEER--QIRQLEG-NILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRN--GMPIHWASSSHGAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 406 YNAAidgveigmgvgscgtaaftnqrvvvediathpywapfkaiankaalgSCWSEPIRSTQGKVLGTLAIYHRNSHKPT 485
Cdd:PRK11359 313 YQNA-----------------------------------------------QSWSATIRQRDGAPAGTLQIKTSSGAETS 345
|
250 260 270
....*....|....*....|....*....|....*....
gi 2567559080 486 EANISLIEQTAYLASIAIEQAhnhlalKNKElRFNQLLQ 524
Cdd:PRK11359 346 AFIERVADISQHLAALALEQE------KSRQ-HIEQLIQ 377
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
518-585 |
3.50e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 48.55 E-value: 3.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559080 518 RFNQLLQSIPSVSVQgYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMQvDVRNAMQQMLK 585
Cdd:smart00091 2 RLRAILESLPDGIFV-LDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRE-RVQEALQRLLS 67
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
1008-1188 |
7.93e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 51.93 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1008 VIDTALAQISQWQAMAPNIPLSISVNI---AAVQLQQADFANRLtllLAAHPdveprYLELEVLEtsaiddvnHVSTIMN 1084
Cdd:PRK11596 80 VVKEQLDLLAQWADFFVRHGLLASVNIdgpTLIALRQQPAILRL---IERLP-----WLRFELVE--------HIRLPKD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 1085 ACVA----LGvTFALDDFGTG---YSSLTYFRrlpVNLIKIDQSFVRDMLDDADDLAIVEGVIVLAKSFKRDVIAEGVET 1157
Cdd:PRK11596 144 SPFAsmceFG-PLWLDDFGTGmanFSALSEVR---YDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVET 219
|
170 180 190
....*....|....*....|....*....|.
gi 2567559080 1158 IEHGTALLQLGCDLAQGYGIARPMPASNIPT 1188
Cdd:PRK11596 220 PEEWRDVQRSPAFAAQGYFLSRPAPFETLET 250
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
202-352 |
1.60e-06 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 52.75 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 202 QVANINALTQSEDAHKK--SKTQLLNVINGakLGYWDWNYKTGEQivndEWLA-MLGLsrHDINNHI----SDWDKLIHP 274
Cdd:PRK09776 391 QIEDINELKRTEQVNERlmERITLANEAGG--IGIWEWDLKPNII----SWDKrMFEL--YEIPPHIkptwQVWYACLHP 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 275 NDKTLAMDVVQQHIHTKENYVVEFRMQHSDdRWIWIQGSGSVVEYDEATqqPLRLCGTHQDITE-RKLSE--LRDKARTH 351
Cdd:PRK09776 463 EDRQRVEKEIRDALQGRSPFKLEFRIVVKD-GVRHIRALANRVLNKDGE--VERLLGINMDMTEvRQLNEalFQEKERLH 539
|
.
gi 2567559080 352 V 352
Cdd:PRK09776 540 I 540
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
647-753 |
1.69e-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: 47.79 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 647 FTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELwNTHQNGELY 726
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEER 79
|
90 100
....*....|....*....|....*..
gi 2567559080 727 AVIETISAVRNESGDITNYVSLVNDIT 753
Cdd:pfam08448 80 HYELRLTPLRDPDGEVIGVLVISRDIT 106
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
518-605 |
1.74e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 47.80 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 518 RFNQLLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLIIPAAMqVDVRNAMQQMLKSKQPIPSGELTL 597
Cdd:pfam00989 2 DLRAILESLP-DGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDD-AEVAELLRQALLQGEESRGFEVSF 79
|
....*...
gi 2567559080 598 MTKQGTEV 605
Cdd:pfam00989 80 RVPDGRPR 87
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
246-345 |
2.49e-06 |
|
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: 47.67 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNHisDWDKLIHPNDKTLAMDVVQQHIhTKENYVV--EFRMQHSDDRWIWIQGSGSVVEYDeat 323
Cdd:TIGR00229 28 VNPAFEEIFGYSAEELIGR--NVLELIPEEDREEVRERIERRL-EGEPEPVseERRVRRKDGSEIWVEVSVSPIRTN--- 101
|
90 100
....*....|....*....|..
gi 2567559080 324 QQPLRLCGTHQDITERKLSELR 345
Cdd:TIGR00229 102 GGELGVVGIVRDITERKEAEEA 123
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
542-615 |
3.74e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 46.18 E-value: 3.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559080 542 YWNKASEYLYGYTAEEAIG--QSLYDLIIPaAMQVDVRNAMQQMLKSKQPIpSGELTLMTKQGTEVNVFSSHAYVH 615
Cdd:pfam08447 3 YWSPRFEEILGYTPEELLGkgESWLDLVHP-DDRERVREALWEALKGGEPY-SGEYRIRRKDGEYRWVEARARPIR 76
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
508-690 |
1.07e-05 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 49.38 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 508 NHLALKNKELRFNQLLQSIPsVSVQGYDYEGNTRYWNKASEYLYGYTAEEAIGQSLYDlIIPAAMqvdvrnaMQQMLKSK 587
Cdd:COG3829 2 EELELKELEEELEAILDSLD-DGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTE-LIPNSP-------LLEVLKTG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 588 QPIpsgELTLMTKQGTEVNVFSSHAYVHVPGqapemfcidvdltkhklaeeKLKLAASVFTHAREgiiITDENATIIDVN 667
Cdd:COG3829 73 KPV---TGVIQKTGGKGKTVIVTAIPIFEDG--------------------EVIGAVETFRDITE---LKRLERKLREEE 126
|
170 180
....*....|....*....|...
gi 2567559080 668 QAFTNITGYTREQAIGHNPSMLN 690
Cdd:COG3829 127 LERGLSAKYTFDDIIGKSPAMKE 149
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
296-339 |
1.69e-05 |
|
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: 42.94 E-value: 1.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2567559080 296 VEFRMQHSDDRWIWIQGSGSVVEYDeaTQQPLRLCGTHQDITER 339
Cdd:smart00086 2 VEYRLRRKDGSYIWVLVSASPIRDE--DGEVEGILGVVRDITER 43
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
637-759 |
1.92e-05 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 48.42 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 637 EEKLKLAASVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDkqsPEFYEQLWRLLkeQGHWSGEL 716
Cdd:COG5000 86 EERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPE---LDLAELLREAL--ERGWQEEI 160
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2567559080 717 WNTHQNGELYAVieTISAVRNEsgditNYVSLVNDITLMKKHQ 759
Cdd:COG5000 161 ELTRDGRRTLLV--RASPLRDD-----GYVIVFDDITELLRAE 196
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
464-646 |
2.30e-05 |
|
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: 48.57 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 464 RSTQGKVLGTL-AIYHRNS-HKPTEANISLI----EQTAYLASIAIEQAHN-HLALKNKELRFNQLLQSIPSVsVQGYDY 536
Cdd:COG5805 97 RLQKGYDVVMIeQIYCKDGeLIYVEVKLFPIynqnGQAAILALRDITKKKKiEEILQEQEERLQTLIENSPDL-ICVIDT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 537 EGNTRYWNKASEYLYGYTAEEAIGQSLYDlIIPAAMQVDVRNAMQQMLKSKQPIPSgELTLMTKQG----TEVNVFSsha 612
Cdd:COG5805 176 DGRILFINESIERLFGAPREELIGKNLLE-LLHPCDKEEFKERIESITEVWQEFII-EREIITKDGriryFEAVIVP--- 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2567559080 613 YVHVPGQAPEMFCIDVDLTKHKLAE------EKL----KLAASV 646
Cdd:COG5805 251 LIDTDGSVKGILVILRDITEKKEAEelmarsEKLsiagQLAAGI 294
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
542-605 |
3.51e-05 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 43.60 E-value: 3.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559080 542 YWNKASEYLYGYTAEEAIGQSLYDLIIPAamqvDVRNAMQQMLKSKQPIPSGELTLMTKQGTEV 605
Cdd:pfam13426 6 YVNDAALRLLGYTREELLGKSITDLFAEP----EDSERLREALREGKAVREFEVVLYRKDGEPF 65
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
644-742 |
4.96e-05 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 47.36 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 644 ASVFThAREGIIITDENAT---IIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWRLLKEQGHWSGELWNTH 720
Cdd:PRK13557 34 AAVET-TRMPMIVTDPNQPdnpIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYR 112
|
90 100
....*....|....*....|..
gi 2567559080 721 QNGELYAVIETISAVRNESGDI 742
Cdd:PRK13557 113 KDGSSFWNALFVSPVYNDAGDL 134
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
535-590 |
1.25e-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: 42.40 E-value: 1.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559080 535 DYEGNTRYWNKASEYLYGYTAEEAIGQSLYDLiIPAAMQVDVRNAMQQMLKSKQPI 590
Cdd:pfam08448 12 DPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLERALRRALEGEEPI 66
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
246-373 |
3.37e-04 |
|
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: 44.58 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 246 VNDEWLAMLGLSRHDINNhiSDWDKLIHPNDKTLAMDVVQQHIHTKENYVVEFRMQHSDDRWIWIQGSGSVVEYDEAtqQ 325
Cdd:COG5809 40 VNPAAERIFGYTEDELLG--TNILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQNG--D 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2567559080 326 PLRLCGTHQDITERKLSElrdkarthvLELITSGESLSVVLTAIVNGI 373
Cdd:COG5809 116 IEGMLAISRDITERKRME---------EALRESEEKFRLIFNHSPDGI 154
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
645-684 |
3.50e-04 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 39.84 E-value: 3.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2567559080 645 SVFTHAREGIIITDENATIIDVNQAFTNITGYTREQAIGH 684
Cdd:pfam13188 5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLG 44
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
629-807 |
8.61e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 43.51 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 629 DLTKHKLAEEKLKLAASVFTHAREGIIIT----DENATIIDVNQAFTNITGYTREQAIGHNPSMLNSDKQSPEFYEQLWR 704
Cdd:PRK13560 188 DITERKRAEERIDEALHFLQQLLDNIADPafwkDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 705 LLKEQGHWSGELWNTHQNGELYAVIETISAVR--NESGDITNYVSLVNDITLMKKHQDQLehiahydvltnlpnrsllad 782
Cdd:PRK13560 268 KFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAEREL-------------------- 327
|
170 180
....*....|....*....|....*
gi 2567559080 783 RLSQAMLQCGRYQTSLAVVFLDLDG 807
Cdd:PRK13560 328 LEKEDMLRAIIEAAPIAAIGLDADG 352
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
245-338 |
2.79e-03 |
|
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: 38.21 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 245 IVNDEWLAMLGLSRHDINNHiSDWDKLIHPNDKTLAMDVVQQHIHTKEnyvVEFRMQHSDDRWIWIQGSGSVVEYDEatQ 324
Cdd:pfam13426 6 YVNDAALRLLGYTREELLGK-SITDLFAEPEDSERLREALREGKAVRE---FEVVLYRKDGEPFPVLVSLAPIRDDG--G 79
|
90
....*....|....
gi 2567559080 325 QPLRLCGTHQDITE 338
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
221-336 |
3.51e-03 |
|
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: 38.55 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 221 TQLLNVINGAKLGYWDWNYKTGEQIVNDEWLAMLGLSRHD-INNHISDwdkLIHPNDKTLAMDVVQQHIHTKENYV-VEF 298
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEvIGKSLLD---LIPEEDDAEVAELLRQALLQGEESRgFEV 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 2567559080 299 RMQHSDDRWIWIQgsGSVVEYDEATQQPLRLCGTHQDI 336
Cdd:pfam00989 78 SFRVPDGRPRHVE--VRASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
666-766 |
4.27e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 41.58 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559080 666 VNQAFTNITGYTRE-------QAIGHnPSMLNSDkqspefYEQLWRLLkeQGH---WSGELWNTHQNGELYAVIETISAV 735
Cdd:PRK09776 308 VNKALCQFLGYSQEelrgltfQQLTW-PEDLNKD------LQQVEKLL--SGEinsYSMEKRYYRRDGEVVWALLAVSLV 378
|
90 100 110
....*....|....*....|....*....|.
gi 2567559080 736 RNESGDITNYVSLVNDITLMKKHQDQLEHIA 766
Cdd:PRK09776 379 RDTDGTPLYFIAQIEDINELKRTEQVNERLM 409
|
|
| |
