NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489738504|ref|WP_003642599|]
View 

MULTISPECIES: EAL domain-containing protein [Lactiplantibacillus]

Protein Classification

EAL domain-containing protein( domain architecture ID 10005623)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase; similar to Borreliella burgdorferi cyclic di-GMP phosphodiesterase PdeA that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to pGpG

CATH:  3.20.20.450
EC:  3.1.4.52
Gene Ontology:  GO:0071111
SCOP:  4002400

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EAL super family cl43641
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
40-265 3.42e-17

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2200:

Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 80.98  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWSLP-------------PQLDSLPLQRVIflleDTFKALPDE 105
Cdd:COG2200  337 LEEGELRLYY--QPIVDLRtGRVVGYEALLRWRHPDGGLISPaefipaaersgliVELDRWVLERAL----RQLARWPER 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 A--ITLSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTPQYQPRRINKrlFRRRIREARGYGMQFGIDNVGASLA 181
Cdd:COG2200  411 GldLRLSVNLSARSLLDPDFLERLLELLAeyGLPPERLVLEITESALLEDLEA--AIELLARLRALGVRIALDDFGTGYS 488
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 182 NLKNIQWLlkDIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQGY 255
Cdd:COG2200  489 SLSYLKRL--PPDYLKID-RSFvrdiarDPRDQAI-----VRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
                        250
                 ....*....|
gi 489738504 256 LFGHPINPQQ 265
Cdd:COG2200  561 LFGRPLPLEE 570
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
40-265 3.42e-17

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: 80.98  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWSLP-------------PQLDSLPLQRVIflleDTFKALPDE 105
Cdd:COG2200  337 LEEGELRLYY--QPIVDLRtGRVVGYEALLRWRHPDGGLISPaefipaaersgliVELDRWVLERAL----RQLARWPER 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 A--ITLSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTPQYQPRRINKrlFRRRIREARGYGMQFGIDNVGASLA 181
Cdd:COG2200  411 GldLRLSVNLSARSLLDPDFLERLLELLAeyGLPPERLVLEITESALLEDLEA--AIELLARLRALGVRIALDDFGTGYS 488
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 182 NLKNIQWLlkDIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQGY 255
Cdd:COG2200  489 SLSYLKRL--PPDYLKID-RSFvrdiarDPRDQAI-----VRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
                        250
                 ....*....|
gi 489738504 256 LFGHPINPQQ 265
Cdd:COG2200  561 LFGRPLPLEE 570
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
40-260 6.24e-16

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: 75.05  E-value: 6.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504   40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSwSLPPQ-----LDSLPLQRVI--FLLEDTFKALPDEA----I 107
Cdd:pfam00563   8 LENGEFVLYY--QPIVDLRtGRVVGYEALLRWQHPDGG-LISPArflplAEELGLIAELdrWVLEQALADLAQLQlgpdI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  108 TLSINLEYEQIISPEF-RYFVRWAIANIEPM-HLAIEYTPQYQPRRINKrlFRRRIREARGYGMQFGIDNVGASLANLKN 185
Cdd:pfam00563  85 KLSINLSPASLADPGFlELLRALLKQAGPPPsRLVLEITESDLLARLEA--LREVLKRLRALGIRIALDDFGTGYSSLSY 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489738504  186 IQWLlkDIDTLKCSmRSFRKEDPSvwlDLNLQFWNQ----LSKENNIDLILMGIENEADEQLAEQLQISIRQGYLFGHP 260
Cdd:pfam00563 163 LLRL--PPDFVKID-RSLIADIDK---DGEARAIVRaliaLAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
40-265 1.49e-15

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: 73.73  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWSLP-------------PQLDSLPLQRVIFLLEDTFKALPDe 105
Cdd:cd01948    7 LERGEFELYY--QPIVDLRtGRIVGYEALLRWRHPEGGLISPaefiplaeetgliVELGRWVLEEACRQLARWQAGGPD- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 aITLSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTpQYQPRRINKRLfRRRIREARGYGMQFGIDNVG---ASL 180
Cdd:cd01948   84 -LRLSVNLSARQLRDPDFLDRLLELLAetGLPPRRLVLEIT-ESALIDDLEEA-LATLRRLRALGVRIALDDFGtgySSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 181 ANLKNIQwllkdIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQG 254
Cdd:cd01948  161 SYLKRLP-----VDYLKID-RSFvrdietDPEDRAI-----VRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQG 229
                        250
                 ....*....|.
gi 489738504 255 YLFGHPINPQQ 265
Cdd:cd01948  230 YLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
40-262 9.96e-15

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 71.48  E-value: 9.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504    40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWsLPPQLD---------SLPLQRviFLLEDTFKAL---PDEA 106
Cdd:smart00052   8 LENGQFLLYY--QPIVSLRtGRLVGVEALIRWQHPEGGI-ISPDEFiplaeetglIVPLGR--WVLEQACQQLaewQAQG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504   107 IT---LSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTPQYqpRRINKRLFRRRIREARGYGMQFGIDNVGASLA 181
Cdd:smart00052  83 PPpllISINLSARQLISPDLVPRVLELLEetGLPPQRLELEITESV--LLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504   182 NLKNIQWLlkDIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQGY 255
Cdd:smart00052 161 SLSYLKRL--PVDLLKID-KSFvrdlqtDPEDEAI-----VQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGY 232

                   ....*..
gi 489738504   256 LFGHPIN 262
Cdd:smart00052 233 LFSRPLP 239
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
38-265 1.09e-14

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 73.59  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  38 NYLENDDFNLryFIQKQVDFR-GRTTGYECLLRQQNTDGSWSLPPQL----DSLPLQRVI--FLLEDTFKALPD-----E 105
Cdd:PRK13561 407 NALENHQFAI--WLQPQVEMRsGKLVSAEALLRMQQPDGSWDLPEGLidriESCGLMVTVghWVLEESCRLLAAwqergI 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 AITLSINLEYEQIISPEF---------RYfvrwaiaNIEPMHLAIEYTpqyQPRRINK-RLFRRRIREARGYGMQFGIDN 175
Cdd:PRK13561 485 MLPLSVNLSALQLMHPNMvadmlelltRY-------RIQPGTLILEVT---ESRRIDDpHAAVAILRPLRNAGVRVALDD 554
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 176 VGASLANLKNIQWLLK-DIDTLKCSmRSFRK---EDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISI 251
Cdd:PRK13561 555 FGMGYAGLRQLQHMKSlPIDVLKID-KMFVDglpEDDSM-----VAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI 628
                        250
                 ....*....|....
gi 489738504 252 RQGYLFGHPINPQQ 265
Cdd:PRK13561 629 AQGFLFARALPIEI 642
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
40-265 3.42e-17

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: 80.98  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWSLP-------------PQLDSLPLQRVIflleDTFKALPDE 105
Cdd:COG2200  337 LEEGELRLYY--QPIVDLRtGRVVGYEALLRWRHPDGGLISPaefipaaersgliVELDRWVLERAL----RQLARWPER 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 A--ITLSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTPQYQPRRINKrlFRRRIREARGYGMQFGIDNVGASLA 181
Cdd:COG2200  411 GldLRLSVNLSARSLLDPDFLERLLELLAeyGLPPERLVLEITESALLEDLEA--AIELLARLRALGVRIALDDFGTGYS 488
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 182 NLKNIQWLlkDIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQGY 255
Cdd:COG2200  489 SLSYLKRL--PPDYLKID-RSFvrdiarDPRDQAI-----VRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
                        250
                 ....*....|
gi 489738504 256 LFGHPINPQQ 265
Cdd:COG2200  561 LFGRPLPLEE 570
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
40-260 6.24e-16

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: 75.05  E-value: 6.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504   40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSwSLPPQ-----LDSLPLQRVI--FLLEDTFKALPDEA----I 107
Cdd:pfam00563   8 LENGEFVLYY--QPIVDLRtGRVVGYEALLRWQHPDGG-LISPArflplAEELGLIAELdrWVLEQALADLAQLQlgpdI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  108 TLSINLEYEQIISPEF-RYFVRWAIANIEPM-HLAIEYTPQYQPRRINKrlFRRRIREARGYGMQFGIDNVGASLANLKN 185
Cdd:pfam00563  85 KLSINLSPASLADPGFlELLRALLKQAGPPPsRLVLEITESDLLARLEA--LREVLKRLRALGIRIALDDFGTGYSSLSY 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489738504  186 IQWLlkDIDTLKCSmRSFRKEDPSvwlDLNLQFWNQ----LSKENNIDLILMGIENEADEQLAEQLQISIRQGYLFGHP 260
Cdd:pfam00563 163 LLRL--PPDFVKID-RSLIADIDK---DGEARAIVRaliaLAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
40-265 1.49e-15

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: 73.73  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWSLP-------------PQLDSLPLQRVIFLLEDTFKALPDe 105
Cdd:cd01948    7 LERGEFELYY--QPIVDLRtGRIVGYEALLRWRHPEGGLISPaefiplaeetgliVELGRWVLEEACRQLARWQAGGPD- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 aITLSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTpQYQPRRINKRLfRRRIREARGYGMQFGIDNVG---ASL 180
Cdd:cd01948   84 -LRLSVNLSARQLRDPDFLDRLLELLAetGLPPRRLVLEIT-ESALIDDLEEA-LATLRRLRALGVRIALDDFGtgySSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 181 ANLKNIQwllkdIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQG 254
Cdd:cd01948  161 SYLKRLP-----VDYLKID-RSFvrdietDPEDRAI-----VRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQG 229
                        250
                 ....*....|.
gi 489738504 255 YLFGHPINPQQ 265
Cdd:cd01948  230 YLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
40-262 9.96e-15

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 71.48  E-value: 9.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504    40 LENDDFNLRYfiQKQVDFR-GRTTGYECLLRQQNTDGSWsLPPQLD---------SLPLQRviFLLEDTFKAL---PDEA 106
Cdd:smart00052   8 LENGQFLLYY--QPIVSLRtGRLVGVEALIRWQHPEGGI-ISPDEFiplaeetglIVPLGR--WVLEQACQQLaewQAQG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504   107 IT---LSINLEYEQIISPEFRYFVRWAIA--NIEPMHLAIEYTPQYqpRRINKRLFRRRIREARGYGMQFGIDNVGASLA 181
Cdd:smart00052  83 PPpllISINLSARQLISPDLVPRVLELLEetGLPPQRLELEITESV--LLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504   182 NLKNIQWLlkDIDTLKCSmRSF------RKEDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQGY 255
Cdd:smart00052 161 SLSYLKRL--PVDLLKID-KSFvrdlqtDPEDEAI-----VQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGY 232

                   ....*..
gi 489738504   256 LFGHPIN 262
Cdd:smart00052 233 LFSRPLP 239
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
38-265 1.09e-14

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 73.59  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  38 NYLENDDFNLryFIQKQVDFR-GRTTGYECLLRQQNTDGSWSLPPQL----DSLPLQRVI--FLLEDTFKALPD-----E 105
Cdd:PRK13561 407 NALENHQFAI--WLQPQVEMRsGKLVSAEALLRMQQPDGSWDLPEGLidriESCGLMVTVghWVLEESCRLLAAwqergI 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 106 AITLSINLEYEQIISPEF---------RYfvrwaiaNIEPMHLAIEYTpqyQPRRINK-RLFRRRIREARGYGMQFGIDN 175
Cdd:PRK13561 485 MLPLSVNLSALQLMHPNMvadmlelltRY-------RIQPGTLILEVT---ESRRIDDpHAAVAILRPLRNAGVRVALDD 554
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 176 VGASLANLKNIQWLLK-DIDTLKCSmRSFRK---EDPSVwldlnLQFWNQLSKENNIDLILMGIENEADEQLAEQLQISI 251
Cdd:PRK13561 555 FGMGYAGLRQLQHMKSlPIDVLKID-KMFVDglpEDDSM-----VAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI 628
                        250
                 ....*....|....
gi 489738504 252 RQGYLFGHPINPQQ 265
Cdd:PRK13561 629 AQGFLFARALPIEI 642
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
38-261 2.74e-11

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 63.42  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504  38 NYLENDDFNLryFIQKQVDFRG-RTTGYECLLRQQNTDGSWSLPPQLDSL--------PLQRviFLLEDTFKALPD---- 104
Cdd:PRK11829 412 QAIENHDFTL--FLQPQWDMKRqQVIGAEALLRWCQPDGSYVLPSGFVHFaeeegmmvPLGN--WVLEEACRILADwkar 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 105 -EAITLSINLEYEQIISPEFRYFVRWAIAN--IEPMHLAIEYTPQYQPRRINKRLfrRRIREARGYGMQFGIDNVGASLA 181
Cdd:PRK11829 488 gVSLPLSVNISGLQVQNKQFLPHLKTLISHyhIDPQQLLLEITETAQIQDLDEAL--RLLRELQGLGLLIALDDFGIGYS 565
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738504 182 NLKNIQWLLK-DIDTLKCSmRSFRKEDPsvwLDLNL-QFWNQLSKENNIDLILMGIENEADEQLAEQLQISIRQGYLFGH 259
Cdd:PRK11829 566 SLRYLNHLKSlPIHMIKLD-KSFVKNLP---EDDAIaRIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSP 641

                 ..
gi 489738504 260 PI 261
Cdd:PRK11829 642 PL 643
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH