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Conserved domains on  [gi|505396784|ref|WP_015583886|]
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EAL domain-containing protein [Raoultella ornithinolytica]

Protein Classification

EAL domain-containing protein( domain architecture ID 11471819)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase, similar to Escherichia coli putative cyclic-di-GMP phosphodiesterases YjcC and YlaB

Gene Ontology:  GO:0007165

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
3-509 2.89e-156

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: 455.53  E-value: 2.89e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   3 FIHKTKWLLTGGGVAVLLSVLLTNAVMLNNQRAQLDMLSHELLAHAEDVTTQIISSIDHAQKRHLDGCNKQAIAALREVI 82
Cdd:COG4943    9 LSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALRRLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  83 WKYASVEDIGIVENGKLACTAnWGRLDKPLPLPAEKYVVPNGYRIYPGVKNYLPYGVVLDMTQQGNIISFTSSFAFSTFS 162
Cdd:COG4943   89 FSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAAFIDVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 163 RQHHGFNFSLTSLNGEHVFLNNMKSAIGARSSISVSLCSS--------------KFDICTHLTERKQGFLSLSPLLIVLM 228
Cdd:COG4943  168 SPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWfiqgdrlyasacspQYPICVVAAAPLAGLLALWRQLLLLL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 229 VGAAFILGAAIVYSILSYLSERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAE 308
Cdd:COG4943  248 LPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAE 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 309 QLNVYHDLSQLVMEKATSELKTILLADACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIA 388
Cdd:COG4943  328 QSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 389 AFSLQAMNRGLRIALDDFGTGSSNLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKAD 467
Cdd:COG4943  408 AVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIgTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQ 487
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 505396784 468 FEFVKSFDENaLIQGWYFYRSMPIEKLTALLLPVSPSHPAAN 509
Cdd:COG4943  488 ADYLRARGVQ-YGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
 
Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
3-509 2.89e-156

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: 455.53  E-value: 2.89e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   3 FIHKTKWLLTGGGVAVLLSVLLTNAVMLNNQRAQLDMLSHELLAHAEDVTTQIISSIDHAQKRHLDGCNKQAIAALREVI 82
Cdd:COG4943    9 LSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALRRLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  83 WKYASVEDIGIVENGKLACTAnWGRLDKPLPLPAEKYVVPNGYRIYPGVKNYLPYGVVLDMTQQGNIISFTSSFAFSTFS 162
Cdd:COG4943   89 FSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAAFIDVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 163 RQHHGFNFSLTSLNGEHVFLNNMKSAIGARSSISVSLCSS--------------KFDICTHLTERKQGFLSLSPLLIVLM 228
Cdd:COG4943  168 SPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWfiqgdrlyasacspQYPICVVAAAPLAGLLALWRQLLLLL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 229 VGAAFILGAAIVYSILSYLSERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAE 308
Cdd:COG4943  248 LPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAE 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 309 QLNVYHDLSQLVMEKATSELKTILLADACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIA 388
Cdd:COG4943  328 QSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 389 AFSLQAMNRGLRIALDDFGTGSSNLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKAD 467
Cdd:COG4943  408 AVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIgTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQ 487
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 505396784 468 FEFVKSFDENaLIQGWYFYRSMPIEKLTALLLPVSPSHPAAN 509
Cdd:COG4943  488 ADYLRARGVQ-YGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
256-492 1.65e-63

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: 206.63  E-value: 1.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 256 RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTILLAD 335
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 336 ACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIAAFSLQAM-NRGLRIALDDFGTGSSNLQ 414
Cdd:cd01948   82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLrALGVRIALDDFGTGYSSLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 415 WLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKS--FDenaLIQGWYFYRSMPI 491
Cdd:cd01948  162 YLKRLPVDYLKIDRSFVRDIeTDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRElgCD---YVQGYLFSRPLPA 238

                 .
gi 505396784 492 E 492
Cdd:cd01948  239 E 239
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
256-492 4.84e-55

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 184.73  E-value: 4.84e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   256 RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTIL-LA 334
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQaQG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   335 DACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIAAFSLQAMNR-GLRIALDDFGTGSSNL 413
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRElGVRIALDDFGTGYSSL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   414 QWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENaLIQGWYFYRSMPIE 492
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLqTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCD-YGQGYLFSRPLPLD 241
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
256-485 7.78e-54

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: 181.36  E-value: 7.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  256 RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTILLaD 335
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL-G 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  336 ACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKkiaAFSLQAMNR----GLRIALDDFGTGSS 411
Cdd:pfam00563  82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARL---EALREVLKRlralGIRIALDDFGTGYS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505396784  412 NLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENaLIQGWYF 485
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIdKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCD-LVQGYYF 232
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
248-505 6.25e-33

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 133.36  E-value: 6.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 248 SERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSE 327
Cdd:PRK11359 539 KERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQ 618
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 328 LKTILLADACF-TLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITE-----RSGEYYKKIAAfsLQAMNRGLRI 401
Cdd:PRK11359 619 LAEWRSQNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITEsmmmeHDTEIFKRIQI--LRDMGVGLSV 696
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 402 alDDFGTGSSNLQWLTEVFYDEIKLDKFFVNGLKNEYK-RAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFdENALI 480
Cdd:PRK11359 697 --DDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRiLALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKI-HCRVI 773
                        250       260
                 ....*....|....*....|....*
gi 505396784 481 QGWYFYRSMPIEKLTALLLPVSPSH 505
Cdd:PRK11359 774 QGYFFSRPLPAEEIPGWMSSVLPLK 798
 
Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
3-509 2.89e-156

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: 455.53  E-value: 2.89e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   3 FIHKTKWLLTGGGVAVLLSVLLTNAVMLNNQRAQLDMLSHELLAHAEDVTTQIISSIDHAQKRHLDGCNKQAIAALREVI 82
Cdd:COG4943    9 LSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLAALRRLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  83 WKYASVEDIGIVENGKLACTAnWGRLDKPLPLPAEKYVVPNGYRIYPGVKNYLPYGVVLDMTQQGNIISFTSSFAFSTFS 162
Cdd:COG4943   89 FSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPGRPMLIVGRGNYVVVIDPAAFIDVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 163 RQHHGFNFSLTSLNGEHVFLNNMKSAIGARSSISVSLCSS--------------KFDICTHLTERKQGFLSLSPLLIVLM 228
Cdd:COG4943  168 SPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWfiqgdrlyasacspQYPICVVAAAPLAGLLALWRQLLLLL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 229 VGAAFILGAAIVYSILSYLSERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAE 308
Cdd:COG4943  248 LPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAE 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 309 QLNVYHDLSQLVMEKATSELKTILLADACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIA 388
Cdd:COG4943  328 QSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 389 AFSLQAMNRGLRIALDDFGTGSSNLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKAD 467
Cdd:COG4943  408 AVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIgTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQ 487
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 505396784 468 FEFVKSFDENaLIQGWYFYRSMPIEKLTALLLPVSPSHPAAN 509
Cdd:COG4943  488 ADYLRARGVQ-YGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
256-492 1.65e-63

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: 206.63  E-value: 1.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 256 RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTILLAD 335
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 336 ACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIAAFSLQAM-NRGLRIALDDFGTGSSNLQ 414
Cdd:cd01948   82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLrALGVRIALDDFGTGYSSLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 415 WLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKS--FDenaLIQGWYFYRSMPI 491
Cdd:cd01948  162 YLKRLPVDYLKIDRSFVRDIeTDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRElgCD---YVQGYLFSRPLPA 238

                 .
gi 505396784 492 E 492
Cdd:cd01948  239 E 239
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
247-498 3.80e-63

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: 215.80  E-value: 3.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 247 LSERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATS 326
Cdd:COG2200  323 ARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALR 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 327 ELKTILLADACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSG-EYYKKIAAFSLQAMNRGLRIALDD 405
Cdd:COG2200  403 QLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALlEDLEAAIELLARLRALGVRIALDD 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 406 FGTGSSNLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKS--FDenaLIQG 482
Cdd:COG2200  483 FGTGYSSLSYLKRLPPDYLKIDRSFVRDIaRDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRElgCD---YAQG 559
                        250
                 ....*....|....*.
gi 505396784 483 WYFYRSMPIEKLTALL 498
Cdd:COG2200  560 YLFGRPLPLEELEALL 575
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
247-498 1.49e-55

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: 197.30  E-value: 1.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 247 LSERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATS 326
Cdd:COG5001  420 ARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACR 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 327 ELKTILLAD-ACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERS--GEYYKKIAAFS-LQAMnrGLRIA 402
Cdd:COG5001  500 QLAAWQDAGlPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESAllEDPEEALETLRaLRAL--GVRIA 577
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 403 LDDFGTGSSNLQWLTE--VfyDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENaL 479
Cdd:COG5001  578 LDDFGTGYSSLSYLKRlpV--DTLKIDRSFVRDLaEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCD-Y 654
                        250
                 ....*....|....*....
gi 505396784 480 IQGWYFYRSMPIEKLTALL 498
Cdd:COG5001  655 AQGYLFSRPLPAEELEALL 673
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
256-492 4.84e-55

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 184.73  E-value: 4.84e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   256 RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTIL-LA 334
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQaQG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   335 DACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIAAFSLQAMNR-GLRIALDDFGTGSSNL 413
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRElGVRIALDDFGTGYSSL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   414 QWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENaLIQGWYFYRSMPIE 492
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLqTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCD-YGQGYLFSRPLPLD 241
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
256-485 7.78e-54

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: 181.36  E-value: 7.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  256 RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTILLaD 335
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL-G 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  336 ACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKkiaAFSLQAMNR----GLRIALDDFGTGSS 411
Cdd:pfam00563  82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARL---EALREVLKRlralGIRIALDDFGTGYS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505396784  412 NLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENaLIQGWYF 485
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIdKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCD-LVQGYYF 232
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
248-505 6.25e-33

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 133.36  E-value: 6.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 248 SERRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSE 327
Cdd:PRK11359 539 KERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQ 618
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 328 LKTILLADACF-TLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITE-----RSGEYYKKIAAfsLQAMNRGLRI 401
Cdd:PRK11359 619 LAEWRSQNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITEsmmmeHDTEIFKRIQI--LRDMGVGLSV 696
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 402 alDDFGTGSSNLQWLTEVFYDEIKLDKFFVNGLKNEYK-RAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFdENALI 480
Cdd:PRK11359 697 --DDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRiLALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKI-HCRVI 773
                        250       260
                 ....*....|....*....|....*
gi 505396784 481 QGWYFYRSMPIEKLTALLLPVSPSH 505
Cdd:PRK11359 774 QGYFFSRPLPAEEIPGWMSSVLPLK 798
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
223-496 2.16e-32

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 130.11  E-value: 2.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 223 LLIVLMVGaafILGAAIVYSILSYlseRRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPEL 302
Cdd:PRK10551 240 LLLGLLSG---ILVGLLCYYLLSL---RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDA 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 303 FISMAE--QLNV--YHDLSQLVMEKAtSELKTILLADACftLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITE 378
Cdd:PRK10551 314 FINYAEaqKLIVplTQHLFELIARDA-AELQKVLPVGAK--LGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITE 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 379 RSG-EYYKKIAAFS-LQamNRGLRIALDDFGTGSSNLQWLTEVFYDEIKLDKFFVNGLKNEykrAILTSLLDVVC----R 452
Cdd:PRK10551 391 RDMvQEEEATKLFAwLH--SQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTE---TVTSPVLDAVLtlakR 465
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 505396784 453 LNKQIVFEGVESKADFEFVKSFDENALiQGWYFYRSMPIEKLTA 496
Cdd:PRK10551 466 LNMLTVAEGVETPEQARWLRERGVNFL-QGYWISRPLPLEDFVR 508
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
253-498 3.22e-31

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 127.88  E-value: 3.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 253 LEFRLKKAIINQRIYMEYQPLVCAKNErIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSEL---- 328
Cdd:PRK10060 409 LDTNLRKALENDQLVIHYQPKITWRGE-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVakwr 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 329 -KTILLadacfTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITErSGEYYKKIAAFSL--QAMNRGLRIALDD 405
Cdd:PRK10060 488 dKGINL-----RVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE-SCLIENEELALSViqQFSQLGAQVHLDD 561
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 406 FGTGSSNLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENAlIQGWY 484
Cdd:PRK10060 562 FGTGYSSLSQLARFPIDAIKLDQSFVRDIhKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE-RQGFL 640
                        250
                 ....*....|....
gi 505396784 485 FYRSMPIEKLTALL 498
Cdd:PRK10060 641 FAKPMPAVAFERWY 654
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
250-505 4.30e-24

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 106.18  E-value: 4.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 250 RRSLEFRLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELK 329
Cdd:PRK11829 403 RLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILA 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 330 TILLADACFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSgeYYKKI--AAFSLQAM-NRGLRIALDDF 406
Cdd:PRK11829 483 DWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETA--QIQDLdeALRLLRELqGLGLLIALDDF 560
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 407 GTGSSNLQWLTEVFY---DEIKLDKFFVNGLKNEYKRA-ILTSLLDVvcrLNKQIVFEGVESKADFEFVKsfdENAL--I 480
Cdd:PRK11829 561 GIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLPEDDAIArIISCVSDV---LKVRVMAEGVETEEQRQWLL---EHGIqcG 634
                        250       260
                 ....*....|....*....|....*
gi 505396784 481 QGWYFYRSMPIEKLTAlLLPVSPSH 505
Cdd:PRK11829 635 QGFLFSPPLPRAEFEA-QYFSSAHH 658
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
260-500 1.56e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 98.25  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 260 AIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKATSELKTILLADACFT 339
Cdd:PRK13561 408 ALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLP 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 340 LAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITE--RSGEYYKKIAAFS-LQamNRGLRIALDDFGTGSSNLQWL 416
Cdd:PRK13561 488 LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTEsrRIDDPHAAVAILRpLR--NAGVRVALDDFGMGYAGLRQL 565
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 417 TE---VFYDEIKLDKFFVNGLKNEykRAILTSLLDVVCRLNKQIVFEGVESKADFEFVksfdENALI---QGWYFYRSMP 490
Cdd:PRK13561 566 QHmksLPIDVLKIDKMFVDGLPED--DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWL----LKAGVgiaQGFLFARALP 639
                        250
                 ....*....|
gi 505396784 491 IEKLTALLLP 500
Cdd:PRK13561 640 IEIFEERYLE 649
CSS-motif pfam12792
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ...
34-174 6.13e-17

CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS sequence motif is found N-terminal to the EAL, pfam00563, domain in many cyclic diguanylate phosphodiesterases.


Pssm-ID: 463709  Cd Length: 209  Bit Score: 79.49  E-value: 6.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784   34 RAQLDMLSHELLAHAEDVTTQIISSIDHAQKRHLDGCNKQAIAALREVIWKYASVEDIGIVENGKLACTANWGRLDKPLP 113
Cdd:pfam12792   2 QEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPLP 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  114 LPAEKYVVPNGYRIYPGVKN---------YLPYGVVLDMTQQGNIISFTSSFAFSTFSRQHHGFNFSLTS 174
Cdd:pfam12792  82 LLPPDLTTPPGVRLWLLRGTplvpgrpalVLRRGGYGVVIDPGVFIDVQYLPGLLAAVSQPDGRLLALVV 151
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
247-496 3.54e-16

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 82.03  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  247 LSERRSLEF--RLKKAIINQRIYMEYQPLVCAKNERIVGVEALVRWHDPRYGHISPELFISMAEQLNVYHDLSQLVMEKA 324
Cdd:PRK09776  834 HSEHRALSLaeQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF 913
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  325 TSELKTILLADAcFTLAINIGKYEINDPLYLDNLLRVLQHKGIRPQQIKIEITERSGEYYKKIAAFSLQAMNR-GLRIAL 403
Cdd:PRK09776  914 FRQAAKAVASKG-LSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLaGCRVVL 992
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784  404 DDFGTGSSNLQWLTEVFYDEIKLDKFFVNGL-KNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENaLIQG 482
Cdd:PRK09776  993 SDFGRGLSSFNYLKAFMADYLKLDGELVANLhGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVD-LAYG 1071
                         250
                  ....*....|....
gi 505396784  483 WYFYRSMPIEKLTA 496
Cdd:PRK09776 1072 YAIARPQPLDLLLN 1085
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
264-499 5.53e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 68.87  E-value: 5.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 264 QRIYmEYQPL--VCAkneRIVGVEAL-VRWH--DPRYgHISPELF---ISMAEQLNVYHDLSQLVMEKATSELKTILLAd 335
Cdd:PRK11596  29 ERAY-TFQPIyrTSG---RLMAIELLtAVTHpsNPSQ-RLSPERYfaeITVSHRLDVVKEQLDLLAQWADFFVRHGLLA- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 336 acftlAINIgkyeinDPLyldNLLRVLQHKGIRPQ-----QIKIEITERSGEYYKKIAAfslqAMNRGLRIALDDFGTGS 410
Cdd:PRK11596 103 -----SVNI------DGP---TLIALRQQPAILRLierlpWLRFELVEHIRLPKDSPFA----SMCEFGPLWLDDFGTGM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 411 SNLQWLTEVFYDEIKLDK-FFVNGLKNEYKRAILTSLLDVVCRLNKQIVFEGVESKADFEFVKSFDENAlIQGWYFYRSM 489
Cdd:PRK11596 165 ANFSALSEVRYDYIKVAReLFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFA-AQGYFLSRPA 243
                        250
                 ....*....|
gi 505396784 490 PIEKLTALLL 499
Cdd:PRK11596 244 PFETLETLPL 253
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
397-499 2.24e-04

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 43.64  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505396784 397 RGLRIALDDFGTGSSNLQWLTEVfyDEIKLDkffVNGLKNEYKRAILTSLLdvvcRLNKQIVFEGVESKADFEFVKS--F 474
Cdd:COG3434  110 KGYRIALDDFVLDPEWDPLLPLA--DIIKID---VLALDLEELAELVARLK----RYGIKLLAEKVETREEFELCKElgF 180
                         90       100       110
                 ....*....|....*....|....*....|...
gi 505396784 475 DenaLIQGwYFY--------RSMPIEKLTALLL 499
Cdd:COG3434  181 D---LFQG-YFFskpeilkgKKLPPSQLTLLQL 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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