|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
12-649 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1263.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 12 IFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKGDIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPER 91
Cdd:PRK13561 14 IFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 92 PVPVMVTRLFELPVQISLGVYSLERPANPQPIAYLVLQADSFRMYKFVMSTLSTLVTIYLLLSLILTVAISWCINRLILH 171
Cdd:PRK13561 94 PVPVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILTVAISWCINRLIVH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 172 PLRNIARELNAIPAQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRHYEEQNENAMRFPVSDLPNKALLMEMLEQVV 251
Cdd:PRK13561 174 PLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 252 ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMILAQISGYDFAVIANGVQEPWHAITLGQQVLTI 331
Cdd:PRK13561 254 ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 332 MSERLPIERIQLRPHCSIGVAMFYGDLTAEQLYSRAISAAFTARHKGKNQIQFFDPQQMEAAQQRLTEESDILNALENHQ 411
Cdd:PRK13561 334 INERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 412 FAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLS 491
Cdd:PRK13561 414 FAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 492 ALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPI 571
Cdd:PRK13561 494 ALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPI 573
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508547379 572 DVLKIDKMFVEGLPEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLPIEIFEESYLEEK 649
Cdd:PRK13561 574 DVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEERYLEEK 651
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
236-643 |
2.69e-116 |
|
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: 362.55 E-value: 2.69e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 236 DLPNKALLMEMLEQVVAR----KQTTALMIITCE---TLRDTAG------VLKE-AQReillltlvekLKSVLSPRMILA 301
Cdd:COG5001 258 GLPNRRLFLDRLEQALARarrsGRRLALLFIDLDrfkEINDTLGhaagdeLLREvARR----------LRACLREGDTVA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 302 QISGYDFAVIANGVQEPWHAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMFYGD-LTAEQLYSRAISAAFTARHKGKN 380
Cdd:COG5001 328 RLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDgADAEELLRNADLAMYRAKAAGRN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 381 QIQFFDPQQMEAAQQRLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMV 460
Cdd:COG5001 408 RYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 461 TVGHWVLEESCRLLAAWQERGIM-LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILR 539
Cdd:COG5001 488 PLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLR 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 540 PLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVEGL---PEDSSMIAAIIMLAQSLNLQMIAEGVETEAQR 616
Cdd:COG5001 568 ALRALGVRIALDDFGTGYSSLSYL---KRLPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQL 644
|
410 420
....*....|....*....|....*..
gi 508547379 617 DWLAKAGVGIAQGFLFARPLPIEIFEE 643
Cdd:COG5001 645 EFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
400-640 |
1.40e-95 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 293.74 E-value: 1.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 400 ESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQE 479
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 480 RGI-MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYA 558
Cdd:smart00052 81 QGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 559 GlrqLQHMKSLPIDVLKIDKMFVEGL---PEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARP 635
Cdd:smart00052 161 S---LSYLKRLPVDLLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
....*
gi 508547379 636 LPIEI 640
Cdd:smart00052 238 LPLDD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
401-639 |
2.06e-89 |
|
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: 277.89 E-value: 2.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 401 SDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQER 480
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 481 GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGL 560
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 561 RQLqhmKSLPIDVLKIDKMFVEGLPEDS---SMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLP 637
Cdd:cd01948 161 SYL---KRLPVDYLKIDRSFVRDIETDPedrAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
..
gi 508547379 638 IE 639
Cdd:cd01948 238 AE 239
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
400-635 |
1.71e-64 |
|
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: 212.56 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 400 ESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQE 479
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 480 RGIMlPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAG 559
Cdd:pfam00563 81 GPDI-KLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508547379 560 LRQLQHmksLPIDVLKIDKMFVEGLPEDSS---MIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARP 635
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
229-386 |
6.81e-05 |
|
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: 43.86 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 229 AMRFPVSDLPNKALLMEMLEQVVARKQT----TALMIITCETLR---DTAG------VLKEAQReillltlveKLKSVLS 295
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRfqrsFSVLMIDIDNFKkinDTLGhdvgdeVLREVAR---------ILQSSVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 296 PRMILAQISGYDFAVIANGVqePWH-AITLGQQVLT-IMSERLPI-ERIQLRPHCSIGVAMFYGD-LTAEQLYSRAISAA 371
Cdd:TIGR00254 73 GSDVVGRYGGEEFVVILPGT--PLEdALSKAERLRDaINSKPIEVaGSETLTVTVSIGVACYPGHgLTLEELLKRADEAL 150
|
170
....*....|....*
gi 508547379 372 FTARHKGKNQIQFFD 386
Cdd:TIGR00254 151 YQAKKAGRNRVVVAD 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
12-649 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1263.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 12 IFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKGDIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPER 91
Cdd:PRK13561 14 IFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 92 PVPVMVTRLFELPVQISLGVYSLERPANPQPIAYLVLQADSFRMYKFVMSTLSTLVTIYLLLSLILTVAISWCINRLILH 171
Cdd:PRK13561 94 PVPVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILTVAISWCINRLIVH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 172 PLRNIARELNAIPAQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRHYEEQNENAMRFPVSDLPNKALLMEMLEQVV 251
Cdd:PRK13561 174 PLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 252 ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMILAQISGYDFAVIANGVQEPWHAITLGQQVLTI 331
Cdd:PRK13561 254 ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 332 MSERLPIERIQLRPHCSIGVAMFYGDLTAEQLYSRAISAAFTARHKGKNQIQFFDPQQMEAAQQRLTEESDILNALENHQ 411
Cdd:PRK13561 334 INERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 412 FAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLS 491
Cdd:PRK13561 414 FAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 492 ALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPI 571
Cdd:PRK13561 494 ALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPI 573
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508547379 572 DVLKIDKMFVEGLPEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLPIEIFEESYLEEK 649
Cdd:PRK13561 574 DVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEERYLEEK 651
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
12-645 |
0e+00 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 665.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 12 IFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKGDIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPER 91
Cdd:PRK11829 14 IFIILQLFHFVQQRKDDYANQLESIAYSVRQPLSEAILSVDIPQAKKILNSLLPIGILSRAEVILPNQIQVLHANFPTER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 92 PVPVMVTRLFELPVQISLGVYSLER-PANPQPIAYLVLQADSFRMYKFVMSTLSTLVTIYLLLSLILTVAISWCINRLIL 170
Cdd:PRK11829 94 PIPHWAKRVFSLPVQITVPLYALERvPANPQPLAHLVLRADSFRMYQFILSALSAMLSTYLLLALVLSVSIAWCINRLII 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 171 HPLRNIARELNAIPAQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRHYEEQNENAMRFPVSDLPNKALLMEMLEQV 250
Cdd:PRK11829 174 HPLRAMAKELEDIGDHGVLHHQLTLPAHHQDDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 251 VA---RKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMILAQISGYDFAVIANGVQEPWHAITLGQQ 327
Cdd:PRK11829 254 IAsstRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 328 VLTIMSERLPIERIQLRPHCSIGVAMFYGDL-TAEQLYSRAISAAFTARHKGKNQIQFFDPQQMEAAQQRLTEESDILNA 406
Cdd:PRK11829 334 IMSQVTQPLFFDEITLRPSASIGITRYQAQQdTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 407 LENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQERGIMLPL 486
Cdd:PRK11829 414 IENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPL 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 487 SVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHM 566
Cdd:PRK11829 494 SVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHL 573
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508547379 567 KSLPIDVLKIDKMFVEGLPEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLPIEIFEESY 645
Cdd:PRK11829 574 KSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEAQY 652
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
236-643 |
2.69e-116 |
|
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: 362.55 E-value: 2.69e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 236 DLPNKALLMEMLEQVVAR----KQTTALMIITCE---TLRDTAG------VLKE-AQReillltlvekLKSVLSPRMILA 301
Cdd:COG5001 258 GLPNRRLFLDRLEQALARarrsGRRLALLFIDLDrfkEINDTLGhaagdeLLREvARR----------LRACLREGDTVA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 302 QISGYDFAVIANGVQEPWHAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMFYGD-LTAEQLYSRAISAAFTARHKGKN 380
Cdd:COG5001 328 RLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDgADAEELLRNADLAMYRAKAAGRN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 381 QIQFFDPQQMEAAQQRLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMV 460
Cdd:COG5001 408 RYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 461 TVGHWVLEESCRLLAAWQERGIM-LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILR 539
Cdd:COG5001 488 PLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLR 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 540 PLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVEGL---PEDSSMIAAIIMLAQSLNLQMIAEGVETEAQR 616
Cdd:COG5001 568 ALRALGVRIALDDFGTGYSSLSYL---KRLPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQL 644
|
410 420
....*....|....*....|....*..
gi 508547379 617 DWLAKAGVGIAQGFLFARPLPIEIFEE 643
Cdd:COG5001 645 EFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
400-640 |
1.40e-95 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 293.74 E-value: 1.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 400 ESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQE 479
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 480 RGI-MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYA 558
Cdd:smart00052 81 QGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 559 GlrqLQHMKSLPIDVLKIDKMFVEGL---PEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARP 635
Cdd:smart00052 161 S---LSYLKRLPVDLLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
....*
gi 508547379 636 LPIEI 640
Cdd:smart00052 238 LPLDD 242
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
69-643 |
7.64e-95 |
|
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: 303.63 E-value: 7.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 69 VSRADVVLPNQFQALRKSFIPERPVPVMVTRLFELPVQISLGVYSLERPANPQPIAYLVLQADSFRMYKFVMSTLSTLVT 148
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 149 IYLLLSLILTVAISWCINRLILHPLRNIARELNAIPAQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRHYEEQNEN 228
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 229 AMRFPVSDLPNKALLMEMLEQVVARKQttALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMILAQISGYDF 308
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLAL--LLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 309 AVIANGVQEPWHAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMFYGDLTAEQLYSRAISAAFTARHKGKNQIQFFDPQ 388
Cdd:COG2200 239 LLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 389 QMEAAQQRLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLE 468
Cdd:COG2200 319 AEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 469 ESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRV 548
Cdd:COG2200 399 RALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 549 ALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVEGL---PEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVG 625
Cdd:COG2200 479 ALDDFGTGYSSLSYLKR---LPPDYLKIDRSFVRDIardPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCD 555
|
570
....*....|....*...
gi 508547379 626 IAQGFLFARPLPIEIFEE 643
Cdd:COG2200 556 YAQGYLFGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
401-639 |
2.06e-89 |
|
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: 277.89 E-value: 2.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 401 SDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQER 480
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 481 GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGL 560
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 561 RQLqhmKSLPIDVLKIDKMFVEGLPEDS---SMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLP 637
Cdd:cd01948 161 SYL---KRLPVDYLKIDRSFVRDIETDPedrAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
..
gi 508547379 638 IE 639
Cdd:cd01948 238 AE 239
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
292-647 |
1.21e-68 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 236.12 E-value: 1.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 292 SVLSPRMILAQISGYDFAVIA-NGVQEPWHAITlgQQVLTIMSERLPIERIQLRPHCSIGVAMF--YGDlTAEQLYSRAI 368
Cdd:PRK10060 302 SCLEEDQTLARLGGDEFLVLAsHTSQAALEAMA--SRILTRLRLPFRIGLIEVYTGCSIGIALApeHGD-DSESLIRSAD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 369 SAAFTARHKGKNQIQFFDPQQmeaaQQRLTE----ESDILNALENHQFAIWLQPQVEMTsGKLVSAEVLLRIQQPDGSWD 444
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEM----NQRVFEylwlDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 445 LPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTE 524
Cdd:PRK10060 454 PPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 525 SRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVEGLPEDS---SMIAAIIMLAQSL 601
Cdd:PRK10060 534 SCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLAR---FPIDAIKLDQSFVRDIHKQPvsqSLVRAIVAVAQAL 610
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 508547379 602 NLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLPIEIFEESYLE 647
Cdd:PRK10060 611 NLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
394-645 |
3.32e-68 |
|
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: 231.73 E-value: 3.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 394 QQRLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRL 473
Cdd:COG4943 267 RRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 474 LAAW--QERGIMLplSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTEsRRIDDPHAAVAILRPLRNAGVRVALD 551
Cdd:COG4943 347 LGDLlaADPDFHI--SINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITE-RGFIDPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 552 DFGMGYAGLRQLQhmkSLPIDVLKIDKMFVEGLPEDS---SMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQ 628
Cdd:COG4943 424 DFGTGYSSLSYLQ---TLPVDILKIDKSFVDAIGTDSansAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500
|
250
....*....|....*..
gi 508547379 629 GFLFARPLPIEIFEESY 645
Cdd:COG4943 501 GWLFAKPLPAEEFIAWL 517
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
400-635 |
1.71e-64 |
|
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: 212.56 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 400 ESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQE 479
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 480 RGIMlPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAG 559
Cdd:pfam00563 81 GPDI-KLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508547379 560 LRQLQHmksLPIDVLKIDKMFVEGLPEDSS---MIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARP 635
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
219-639 |
4.25e-60 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 215.02 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 219 QRHYEEQNENAMRF-PVSDLPNKALLMEMLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPR 297
Cdd:PRK11359 365 QEKSRQHIEQLIQFdPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 298 MILAQISGYDFAVIA--NGVQEpwhAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMFYGDlTAEQLYSRAISAAFTAR 375
Cdd:PRK11359 445 QYLCRIEGTQFVLVSleNDVSN---ITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDVGK-NRDYLLSTAHNAMDYIR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 376 HKGKNQIQFFDPQQMEAAQQRLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIEC 455
Cdd:PRK11359 521 KNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEE 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 456 CGLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAA 534
Cdd:PRK11359 601 IGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEI 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 535 VAILRPLRNAGVRVALDDFGMGYAGLRQLQhmkSLPIDVLKIDKMFVEGLPEDS---SMIAAIIMLAQSLNLQMIAEGVE 611
Cdd:PRK11359 681 FKRIQILRDMGVGLSVDDFGTGFSGLSRLV---SLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTVVAEGVE 757
|
410 420
....*....|....*....|....*...
gi 508547379 612 TEAQRDWLAKAGVGIAQGFLFARPLPIE 639
Cdd:PRK11359 758 TKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| GAPES3 |
pfam17154 |
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic ... |
23-142 |
1.26e-50 |
|
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases/phosphodiesterases, including the c-di-GMP phosphodiesterases PdeK (YhjK) of Escherichia coli and HmsP of Yersinia pestis.
Pssm-ID: 435753 [Multi-domain] Cd Length: 121 Bit Score: 171.46 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 23 QQNRYNTATQLESIARSVREPLSSAILKGDIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPERPVPVMVTRLFE 102
Cdd:pfam17154 1 QQRKDDYANQLENIAVSVRAPLTEALLSSDLNEAKSILITLRPSGILGRADVVLPNQIQVLHLNFATERPIPELAKRVFG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 508547379 103 LPVQISLGVYSLER-PANPQPIAYLVLQADSFRMYKFVMST 142
Cdd:pfam17154 81 LPVEISVPLYSYGVsPTNPQPLAHLVLQADSNRMYRFIIST 121
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
237-645 |
6.02e-36 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 145.20 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 237 LPNKAL----LMEMLEQVVARKQTTALMIITCETLR---DTAGvlkEAQREILLLTLVEKLKSVLSPRMILAQISGYDFA 309
Cdd:PRK09776 673 LANRASfekqLRRLLQTVNSTHQRHALVFIDLDRFKavnDSAG---HAAGDALLRELASLMLSMLRSSDVLARLGGDEFG 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 310 VIANGVQEPwHAITLGQQVL-TIMSERLPIERIQLRPHCSIGVAMFygDLTAEQ---LYSRAISAAFTARHKGKNQIQFF 385
Cdd:PRK09776 750 LLLPDCNVE-SARFIATRIIsAINDYHFPWEGRVYRVGASAGITLI--DANNHQaseVMSQADIACYAAKNAGRGRVTVY 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 386 DPQQMEAAQQR--LTEESDILNALENHQFAIWLQ---PQVEMTSGKLvsaEVLLRIQQPDGSWDLPDGLIDRIECCGLMV 460
Cdd:PRK09776 827 EPQQAAAHSEHraLSLAEQWRMIKENQLMMLAHGvasPRIPEARNHW---LISLRLWDPEGEIIDEGAFRPAAEDPALMH 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 461 TVGHWVLEESCRLLAAwQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRP 540
Cdd:PRK09776 904 ALDRRVIHEFFRQAAK-AVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQK 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 541 LRNAGVRVALDDFGmgyAGLRQLQHMKSLPIDVLKIDKMFVEGL---PEDSSMIAAIIMLAQSLNLQMIAEGVETEAQRD 617
Cdd:PRK09776 983 LRLAGCRVVLSDFG---RGLSSFNYLKAFMADYLKLDGELVANLhgnLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLD 1059
|
410 420
....*....|....*....|....*....
gi 508547379 618 WLAKAGVGIAQGFLFARPLPIEIF-EESY 645
Cdd:PRK09776 1060 TLSGIGVDLAYGYAIARPQPLDLLlNSSY 1088
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
227-385 |
4.85e-33 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 124.67 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 227 ENAMRFPVSDLPNKALLMEMLEQVVARKQT----TALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMILAQ 302
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 303 ISGYDFAVIANGVqEPWHAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMF-YGDLTAEQLYSRAISAAFTARHKGKNQ 381
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 508547379 382 IQFF 385
Cdd:smart00267 160 VAVY 163
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
396-648 |
3.04e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 128.19 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 396 RLTEESDILNALENHQFAIWLQPQVEMTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLA 475
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 476 AWQErgiMLP----LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTEsRRIDDPHAAVAILRPLRNAGVRVALD 551
Cdd:PRK10551 341 ELQK---VLPvgakLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITE-RDMVQEEEATKLFAWLHSQGIEIAID 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 552 DFGMGYAGLRQLQHMKslpIDVLKIDKMFVEGLPED---SSMIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQ 628
Cdd:PRK10551 417 DFGTGHSALIYLERFT---LDYLKIDRGFIQAIGTEtvtSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQ 493
|
250 260
....*....|....*....|
gi 508547379 629 GFLFARPLPIEIFEESYLEE 648
Cdd:PRK10551 494 GYWISRPLPLEDFVRWLKEP 513
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
121-385 |
5.73e-20 |
|
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: 90.42 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 121 QPIAYLVLQADSFRMYKFVMSTLSTLVTIYLLLSLILTVAISWCINRLILHPLRNIARELNAIPAQELVGHQLALPRLHQ 200
Cdd:COG2199 7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 201 DDEIGMLVRSYNLNQQLlQRHYEEQNENAMRFPVSDLPNKALLMEMLEQVVAR----KQTTALMIITC---ETLRDTAGv 273
Cdd:COG2199 87 LLALLLLLLALEDITEL-RRLEERLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLdhfKRINDTYG- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 274 lkEAQREILLLTLVEKLKSVLSPRMILAQISGYDFAVIANGVQEPwHAITLGQQVLTIMSE-RLPIERIQLRPHCSIGVA 352
Cdd:COG2199 165 --HAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQlPFELEGKELRVTVSIGVA 241
|
250 260 270
....*....|....*....|....*....|....
gi 508547379 353 MFYGD-LTAEQLYSRAISAAFTARHKGKNQIQFF 385
Cdd:COG2199 242 LYPEDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
499-639 |
5.65e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 74.07 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 499 NMVADMLELLTRYRIQPGTLILEVTESRRIDDphAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmkslpIDVLKIDk 578
Cdd:COG3434 67 NFTEELLLSDLPELLPPERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL-----ADIIKID- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508547379 579 mfVEGLPEDSsmIAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPLPIE 639
Cdd:COG3434 139 --VLALDLEE--LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
233-383 |
1.51e-13 |
|
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: 68.74 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 233 PVSDLPNKALLMEMLEQVVAR----KQTTALMIItcetlrD-------------TAG--VLKE-AQReillltlvekLKS 292
Cdd:cd01949 4 PLTGLPNRRAFEERLERLLARarrsGRPLALLLI------DidhfkqindtyghAAGdeVLKEvAER----------LRS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 293 VLSPRMILAQISGYDFAVIANGVQEPwHAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMF-YGDLTAEQLYSRAISAA 371
Cdd:cd01949 68 SLRESDLVARLGGDEFAILLPGTDLE-EAEALAERLREAIEEPFFIDGQEIRVTASIGIATYpEDGEDAEELLRRADEAL 146
|
170
....*....|..
gi 508547379 372 FTARHKGKNQIQ 383
Cdd:cd01949 147 YRAKRSGRNRVV 158
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
265-638 |
4.46e-12 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 69.12 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 265 ETLRDTAGvlkEAQREILLLTLVEKLKSVLS--PRMILAQISGYDFAVIA--NGVQEpwhAITLGQQVLTIMsERLPIER 340
Cdd:PRK11059 271 DLLQEEWG---ESQVEELLFELINLLSTFVMryPGALLARYSRSDFAVLLphRSLKE---ADSLASQLLKAV-DALPPPK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 341 IQLRPH-CSIGVAMFYGDLTAEQLYSRAISAAFTARHKGKNQIQFFD-PQQMEAAQQRLTEESDILNALENHQFAIWLQP 418
Cdd:PRK11059 344 MLDRDDfLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDkAQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 419 QVEmTSGKLVSAEVLLRIQQPDGSWDLPDGLIDRIECCGLMVTVGHWVLEESCRLLAAWQERgimlPLSVNLSALQLMHP 498
Cdd:PRK11059 424 AVT-RDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE----NLSINLSVDSLLSR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 499 NMVA---DmlELLTRYRIQPGTLILEVTES---RRIDdphAAVAILRPLRNAGVRVALDDFGmgyaglRQL---QHMKSL 569
Cdd:PRK11059 499 AFQRwlrD--TLLQCPRSQRKRLIFELAEAdvcQHIS---RLRPVLRMLRGLGCRLAVDQAG------LTVvstSYIKEL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 570 PIDVLK--------IDK-----MFVEglpedsSMIAAiimLAQSlNLQMIAEGVETEAQRDWLAKAGVGIAQGFLFARPL 636
Cdd:PRK11059 568 NVELIKlhpslvrnIHKrtenqLFVR------SLVGA---CAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFAESQ 637
|
..
gi 508547379 637 PI 638
Cdd:PRK11059 638 PL 639
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
233-381 |
2.55e-10 |
|
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: 59.57 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 233 PVSDLPNKALLMEMLEQVVAR--KQTTALMIITC-----ETLRDTAGvlkEAQREILLLTLVEKLKSVLSPRMILAQISG 305
Cdd:pfam00990 5 PLTGLPNRRYFEEQLEQELQRalREGSPVAVLLIdldnfKRINDTYG---HSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508547379 306 YDFAVIANGVQEPW--HAITLGQQVLTIMSERLPIERIQLRPHCSIGVAMFYGD-LTAEQLYSRAISAAFTARHKGKNQ 381
Cdd:pfam00990 82 DEFAILLPETSLEGaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
229-386 |
6.81e-05 |
|
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: 43.86 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 229 AMRFPVSDLPNKALLMEMLEQVVARKQT----TALMIITCETLR---DTAG------VLKEAQReillltlveKLKSVLS 295
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRfqrsFSVLMIDIDNFKkinDTLGhdvgdeVLREVAR---------ILQSSVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 296 PRMILAQISGYDFAVIANGVqePWH-AITLGQQVLT-IMSERLPI-ERIQLRPHCSIGVAMFYGD-LTAEQLYSRAISAA 371
Cdd:TIGR00254 73 GSDVVGRYGGEEFVVILPGT--PLEdALSKAERLRDaINSKPIEVaGSETLTVTVSIGVACYPGHgLTLEELLKRADEAL 150
|
170
....*....|....*
gi 508547379 372 FTARHKGKNQIQFFD 386
Cdd:TIGR00254 151 YQAKKAGRNRVVVAD 165
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
390-643 |
7.68e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 44.61 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 390 MEAAQQRLTEESDILNALENHQFaiWLQPQVEMT-------SGKLVSAEVLLRIQQPDGSWDL--PDGLIDRIEccglmv 460
Cdd:PRK11596 2 IRQVIQRISLPEASIESLQERRY--WLQCERAYTfqpiyrtSGRLMAIELLTAVTHPSNPSQRlsPERYFAEIT------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 461 tVGHW--VLEESCRLLAAWQERGIM--LPLSVNLSALQLMHPNMVADMLELLTRYriqPgTLILEVTESRRI--DDPHAA 534
Cdd:PRK11596 74 -VSHRldVVKEQLDLLAQWADFFVRhgLLASVNIDGPTLIALRQQPAILRLIERL---P-WLRFELVEHIRLpkDSPFAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 535 VAILRPLrnagvrvALDDFGMGYAGLRQLQHMKslpIDVLKIDK-MFV--EGLPEDSSMIAAIIMLAQSLNLQMIAEGVE 611
Cdd:PRK11596 149 MCEFGPL-------WLDDFGTGMANFSALSEVR---YDYIKVAReLFImlRQSEEGRNLFSQLLHLMNRYCRGVIVEGVE 218
|
250 260 270
....*....|....*....|....*....|..
gi 508547379 612 TEAQRDWLAKAGVGIAQGFLFARPLPIEIFEE 643
Cdd:PRK11596 219 TPEEWRDVQRSPAFAAQGYFLSRPAPFETLET 250
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
146-232 |
2.54e-04 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 43.80 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 146 LVTIYLLLSLILTVAISWCINRLILHPLRNIARELNAIPAQELvGHQLALPRlhqDDEIGMLVRSYN-LNQQLlqRHYEE 224
Cdd:COG5000 10 LLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDL-SVRLPVTG---DDEIGELARAFNrMTDQL--KEQRE 83
|
....*...
gi 508547379 225 QNENAMRF 232
Cdd:COG5000 84 ELEERRRY 91
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
140-228 |
2.60e-03 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 40.77 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508547379 140 MSTLSTLVTIYLLLSLILTVAISWCINRLILHPLRNIARELNAIPAQELVghqlaLPRLHQDDEIGMLVRSYNL----NQ 215
Cdd:COG2972 152 LFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLV-----RLEVSGNDEIGILARSFNEmverIK 226
|
90
....*....|...
gi 508547379 216 QLLQRHYEEQNEN 228
Cdd:COG2972 227 ELIEEVYELELEK 239
|
|
| |
