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Conserved domains on  [gi|912992351|ref|WP_050339145|]
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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

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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) ...
3-217 8.14e-24

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: 99.09  E-value: 8.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   3 RYFIQPQLNKFNNSLIGYEMLIRYReTDQDRWTLPESFdnIP----------IDVQV---SLLKATASELALKIGSVSIN 69
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRWR-HPDGGLISPAEF--IPaaersgliveLDRWVlerALRQLARWPERGLDLRLSVN 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  70 FNRKQFLNDDIANAVID--AQKKLFPVHVIVEVTEEpgEDTYTLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLl 147
Cdd:COG2200  420 LSARSLLDPDFLERLLEllAEYGLPPERLVLEITES--ALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRL- 496
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351 148 eSAEEIKFAMQNFRAEDRENEIPIQLKFWRDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:COG2200  497 -PPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
3-217 8.14e-24

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: 99.09  E-value: 8.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   3 RYFIQPQLNKFNNSLIGYEMLIRYReTDQDRWTLPESFdnIP----------IDVQV---SLLKATASELALKIGSVSIN 69
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRWR-HPDGGLISPAEF--IPaaersgliveLDRWVlerALRQLARWPERGLDLRLSVN 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  70 FNRKQFLNDDIANAVID--AQKKLFPVHVIVEVTEEpgEDTYTLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLl 147
Cdd:COG2200  420 LSARSLLDPDFLERLLEllAEYGLPPERLVLEITES--ALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRL- 496
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351 148 eSAEEIKFAMQNFRAEDRENEIPIQLKFWRDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:COG2200  497 -PPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
7-217 2.04e-18

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: 80.44  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351    7 QPQLNKFNNSLIGYEMLIRYReTDQDRWTLPESFDNI--------PIDVQV--SLLKATASELALKIGSVSINFNRKQFL 76
Cdd:pfam00563  18 QPIVDLRTGRVVGYEALLRWQ-HPDGGLISPARFLPLaeelgliaELDRWVleQALADLAQLQLGPDIKLSINLSPASLA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   77 NDDIANAVIDAQKKLFPVH--VIVEVTEEpgEDTYTLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLleSAEEIK 154
Cdd:pfam00563  97 DPGFLELLRALLKQAGPPPsrLVLEITES--DLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRL--PPDFVK 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 912992351  155 F---AMQNFRAEDRENEIpiqLKFWRDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:pfam00563 173 IdrsLIADIDKDGEARAI---VRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
7-217 2.65e-18

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: 80.28  E-value: 2.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   7 QPQLNKFNNSLIGYEMLIRYREtDQDRWTLPESFDNI--------PIDVQVslLKATASELA-----LKIGSVSINFNRK 73
Cdd:cd01948   17 QPIVDLRTGRIVGYEALLRWRH-PEGGLISPAEFIPLaeetglivELGRWV--LEEACRQLArwqagGPDLRLSVNLSAR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  74 QFLNDDIANAVIDAQKK--LFPVHVIVEVTE-EPGEDtytLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLleSA 150
Cdd:cd01948   94 QLRDPDFLDRLLELLAEtgLPPRRLVLEITEsALIDD---LEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRL--PV 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912992351 151 EEIKFAMQNFR--AEDRENEIPIQ--LkfwrDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:cd01948  169 DYLKIDRSFVRdiETDPEDRAIVRaiI----ALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
3-217 9.85e-14

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 68.01  E-value: 9.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351     3 RYFIQPQLNKFNNSLIGYEMLIRyRETDQDRWTLPESFDNI--------PIDVQV--SLLKATASELALKIG--SVSINF 70
Cdd:smart00052  14 LLYYQPIVSLRTGRLVGVEALIR-WQHPEGGIISPDEFIPLaeetglivPLGRWVleQACQQLAEWQAQGPPplLISINL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351    71 NRKQFLNDDIANAVID--AQKKLFPVHVIVEVTEEPGEDTytLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLle 148
Cdd:smart00052  93 SARQLISPDLVPRVLEllEETGLPPQRLELEITESVLLDD--DESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRL-- 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912992351   149 SAEEIKFAMQNFRA--EDRENEIPIQLKFwrDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:smart00052 169 PVDLLKIDKSFVRDlqTDPEDEAIVQSII--ELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
5-217 2.59e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 53.56  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   5 FIQPQLNKFNNSLIGYEMLIRYRETDQDrWTLPESF-DNI-PIDVQVSL----LKATASELAL--KIGS---VSINFNRK 73
Cdd:PRK13561 417 WLQPQVEMRSGKLVSAEALLRMQQPDGS-WDLPEGLiDRIeSCGLMVTVghwvLEESCRLLAAwqERGImlpLSVNLSAL 495
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  74 QFLNDDIANAVID--AQKKLFPVHVIVEVTE-----EPGEDTYTLAAMQQqiakykaSGLQFSLDDVGTG---INVYDHI 143
Cdd:PRK13561 496 QLMHPNMVADMLEllTRYRIQPGTLILEVTEsrridDPHAAVAILRPLRN-------AGVRVALDDFGMGyagLRQLQHM 568
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 912992351 144 KPLLESAEEI-KFAMQNFRAEDRENEIPIQlkfwrdIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:PRK13561 569 KSLPIDVLKIdKMFVDGLPEDDSMVAAIIM------LAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
3-217 8.14e-24

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: 99.09  E-value: 8.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   3 RYFIQPQLNKFNNSLIGYEMLIRYReTDQDRWTLPESFdnIP----------IDVQV---SLLKATASELALKIGSVSIN 69
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRWR-HPDGGLISPAEF--IPaaersgliveLDRWVlerALRQLARWPERGLDLRLSVN 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  70 FNRKQFLNDDIANAVID--AQKKLFPVHVIVEVTEEpgEDTYTLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLl 147
Cdd:COG2200  420 LSARSLLDPDFLERLLEllAEYGLPPERLVLEITES--ALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRL- 496
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351 148 eSAEEIKFAMQNFRAEDRENEIPIQLKFWRDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:COG2200  497 -PPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
7-217 2.04e-18

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: 80.44  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351    7 QPQLNKFNNSLIGYEMLIRYReTDQDRWTLPESFDNI--------PIDVQV--SLLKATASELALKIGSVSINFNRKQFL 76
Cdd:pfam00563  18 QPIVDLRTGRVVGYEALLRWQ-HPDGGLISPARFLPLaeelgliaELDRWVleQALADLAQLQLGPDIKLSINLSPASLA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   77 NDDIANAVIDAQKKLFPVH--VIVEVTEEpgEDTYTLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLleSAEEIK 154
Cdd:pfam00563  97 DPGFLELLRALLKQAGPPPsrLVLEITES--DLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRL--PPDFVK 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 912992351  155 F---AMQNFRAEDRENEIpiqLKFWRDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:pfam00563 173 IdrsLIADIDKDGEARAI---VRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
7-217 2.65e-18

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: 80.28  E-value: 2.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   7 QPQLNKFNNSLIGYEMLIRYREtDQDRWTLPESFDNI--------PIDVQVslLKATASELA-----LKIGSVSINFNRK 73
Cdd:cd01948   17 QPIVDLRTGRIVGYEALLRWRH-PEGGLISPAEFIPLaeetglivELGRWV--LEEACRQLArwqagGPDLRLSVNLSAR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  74 QFLNDDIANAVIDAQKK--LFPVHVIVEVTE-EPGEDtytLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLleSA 150
Cdd:cd01948   94 QLRDPDFLDRLLELLAEtgLPPRRLVLEITEsALIDD---LEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRL--PV 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912992351 151 EEIKFAMQNFR--AEDRENEIPIQ--LkfwrDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:cd01948  169 DYLKIDRSFVRdiETDPEDRAIVRaiI----ALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
3-217 9.85e-14

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 68.01  E-value: 9.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351     3 RYFIQPQLNKFNNSLIGYEMLIRyRETDQDRWTLPESFDNI--------PIDVQV--SLLKATASELALKIG--SVSINF 70
Cdd:smart00052  14 LLYYQPIVSLRTGRLVGVEALIR-WQHPEGGIISPDEFIPLaeetglivPLGRWVleQACQQLAEWQAQGPPplLISINL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351    71 NRKQFLNDDIANAVID--AQKKLFPVHVIVEVTEEPGEDTytLAAMQQQIAKYKASGLQFSLDDVGTGINVYDHIKPLle 148
Cdd:smart00052  93 SARQLISPDLVPRVLEllEETGLPPQRLELEITESVLLDD--DESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRL-- 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912992351   149 SAEEIKFAMQNFRA--EDRENEIPIQLKFwrDIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:smart00052 169 PVDLLKIDKSFVRDlqTDPEDEAIVQSII--ELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
7-217 5.03e-09

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: 55.55  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   7 QPQLNKFNNSLIGYEMLIRYRetDQDRWTL-PESFdnIPIdvqvsllkATASELALKIG--------------------- 64
Cdd:COG5001  444 QPQVDLATGRIVGAEALLRWQ--HPERGLVsPAEF--IPL--------AEETGLIVPLGewvlreacrqlaawqdaglpd 511
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  65 -SVSINFNRKQFLNDDIANAVIDA--QKKLFPVHVIVEVTE----EPGEDTytlaamQQQIAKYKASGLQFSLDDVGTGi 137
Cdd:COG5001  512 lRVAVNLSARQLRDPDLVDRVRRAlaETGLPPSRLELEITEsallEDPEEA------LETLRALRALGVRIALDDFGTG- 584
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351 138 nvY-----------DHIK-------PLLESAEEIKFAmqnfRAedreneIpiqlkfwrdIALKH--DIRLILEGVENdvE 197
Cdd:COG5001  585 --YsslsylkrlpvDTLKidrsfvrDLAEDPDDAAIV----RA------I---------IALAHslGLEVVAEGVET--E 641
                        250       260
                 ....*....|....*....|....*..
gi 912992351 198 DQMAddlniALR-------QGYYYGKP 217
Cdd:COG5001  642 EQLE-----FLRelgcdyaQGYLFSRP 663
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
5-217 2.59e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 53.56  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351   5 FIQPQLNKFNNSLIGYEMLIRYRETDQDrWTLPESF-DNI-PIDVQVSL----LKATASELAL--KIGS---VSINFNRK 73
Cdd:PRK13561 417 WLQPQVEMRSGKLVSAEALLRMQQPDGS-WDLPEGLiDRIeSCGLMVTVghwvLEESCRLLAAwqERGImlpLSVNLSAL 495
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  74 QFLNDDIANAVID--AQKKLFPVHVIVEVTE-----EPGEDTYTLAAMQQqiakykaSGLQFSLDDVGTG---INVYDHI 143
Cdd:PRK13561 496 QLMHPNMVADMLEllTRYRIQPGTLILEVTEsrridDPHAAVAILRPLRN-------AGVRVALDDFGMGyagLRQLQHM 568
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 912992351 144 KPLLESAEEI-KFAMQNFRAEDRENEIPIQlkfwrdIALKHDIRLILEGVENDVEDQMADDLNIALRQGYYYGKP 217
Cdd:PRK13561 569 KSLPIDVLKIdKMFVDGLPEDDSMVAAIIM------LAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
66-217 2.76e-05

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 44.29  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351  66 VSINFNRKQFLND----DIANAVIDAQKKLFPVHVivEVTEEP--GEDTYTLAAMQQqiakYKASGLQFSLDDVGTGINV 139
Cdd:PRK10060 495 VAVNVSARQLADQtiftALKQALQELNFEYCPIDV--ELTESCliENEELALSVIQQ----FSQLGAQVHLDDFGTGYSS 568
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912992351 140 YDHIK--PLlesaEEIKFAMQNFRAEDREneiPIQLKFWRDI---ALKHDIRLILEGVENDVEDQMADDLNIALRQGYYY 214
Cdd:PRK10060 569 LSQLArfPI----DAIKLDQSFVRDIHKQ---PVSQSLVRAIvavAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLF 641

                 ...
gi 912992351 215 GKP 217
Cdd:PRK10060 642 AKP 644
 
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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