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Conserved domains on  [gi|172039089|ref|YP_001805590|]
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hypothetical protein cce_4176 [Cyanothece sp. ATCC 51142]

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List of domain hits

Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
456-691 4.59e-109

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  Cd Length: 240  Bit Score: 332.97  E-value: 4.59e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 456 ALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLPaI 535
Cdd:cd01948    6 ALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPD-L 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 536 PIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQ 615
Cdd:cd01948   85 RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLK 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172039089 616 KFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPAD 691
Cdd:cd01948  165 RLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
275-433 2.58e-68

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  Cd Length: 158  Bit Score: 222.43  E-value: 2.58e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 275 FYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRWGG 354
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089 355 DEFTLLLPQINtPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKNHYR 433
Cdd:cd01949   81 DEFAILLPGTD-LEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
10-106 9.48e-14

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


:

Pssm-ID: 238017  Cd Length: 102  Bit Score: 68.18  E-value: 9.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  10 HILVIEDQKARRIVALEE-ATYSVGRESSN-DIVIYEQVVSRRHATIVRVkltprldsysyRIIDGDLEGHRSTNGLLIN 87
Cdd:cd00060    3 RLVVLSGDASGRRYYLDPgGTYTIGRDSDNcDIVLDDPSVSRRHAVIRYD-----------GDGGVVLIDLGSTNGTFVN 71
                         90       100
                 ....*....|....*....|..
gi 172039089  88 GQLKDSHN---LNHGDVIIFGP 106
Cdd:cd00060   72 GQRVSPGEpvrLRDGDVIRLGN 93
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
8-137 4.63e-18

FOG: FHA domain [Signal transduction mechanisms]


:

Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 83.08  E-value: 4.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   8 FRHILVIEDQKARRIVAL--------EEATYSVGRESSNDIVIYEQVVSRRHATIVRVKltprldsysyriIDGDLEGHR 79
Cdd:COG1716   61 EPGVLTALDGPLAVTIGLdegsvivlGEPVTTIGRDPDNDIVLDDDVVSRRHAELRREG------------NEVFLEDLG 128
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089  80 STNGLLINGQ-LKDSHNLNHGDVIIFGPQAKVSYYIISTSLDIDLFNPLDPGQLQQEEE 137
Cdd:COG1716  129 STNGTYVNGEkVRQRVLLQDGDVIRLGGTLAERLRIILTELEIDGVDPVATSAKELEEE 187
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
456-691 4.59e-109

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  Cd Length: 240  Bit Score: 332.97  E-value: 4.59e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 456 ALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLPaI 535
Cdd:cd01948    6 ALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPD-L 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 536 PIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQ 615
Cdd:cd01948   85 RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLK 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172039089 616 KFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPAD 691
Cdd:cd01948  165 RLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
275-433 2.58e-68

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  Cd Length: 158  Bit Score: 222.43  E-value: 2.58e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 275 FYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRWGG 354
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089 355 DEFTLLLPQINtPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKNHYR 433
Cdd:cd01949   81 DEFAILLPGTD-LEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
10-106 9.48e-14

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 68.18  E-value: 9.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  10 HILVIEDQKARRIVALEE-ATYSVGRESSN-DIVIYEQVVSRRHATIVRVkltprldsysyRIIDGDLEGHRSTNGLLIN 87
Cdd:cd00060    3 RLVVLSGDASGRRYYLDPgGTYTIGRDSDNcDIVLDDPSVSRRHAVIRYD-----------GDGGVVLIDLGSTNGTFVN 71
                         90       100
                 ....*....|....*....|..
gi 172039089  88 GQLKDSHN---LNHGDVIIFGP 106
Cdd:cd00060   72 GQRVSPGEpvrLRDGDVIRLGN 93
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
455-692 6.77e-101

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


Pssm-ID: 214491  Cd Length: 242  Bit Score: 311.84  E-value: 6.77e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLPA 534
Cdd:smart00052   6 QALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGPPP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   535 IPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:smart00052  86 LLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYL 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172039089   615 QKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLkPADA 692
Cdd:smart00052 166 KRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL-PLDD 242
Rtn COG2200
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]
455-698 2.55e-98

c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]


Pssm-ID: 225110  Cd Length: 256  Bit Score: 305.37  E-value: 2.55e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLpa 534
Cdd:COG2200   10 QALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRTWPRAGP-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 535 IPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:COG2200   88 LRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGTGYSSLSYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 615 QKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPADATT 694
Cdd:COG2200  168 KRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPLPADALDA 247

                 ....
gi 172039089 695 FLSQ 698
Cdd:COG2200  248 LLSS 251
GGDEF pfam00990
GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a ...
274-430 9.66e-67

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.


Pssm-ID: 250276  Cd Length: 159  Bit Score: 218.26  E-value: 9.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  274 AFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRWG 353
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEELEQELQRARRQQSPLALLLIDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089  354 GDEFTLLLPQINTPE--DTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKN 430
Cdd:pfam00990  81 GEEFAILLPDTSLEGaqELAERIRRLLAALAIPHTLSGLPLYVTISIGIAAYPNDGEDPEDLLKRADQALYQAKQQGRN 159
COG2199 COG2199
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]
256-435 1.49e-64

c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]


Pssm-ID: 225109  Cd Length: 181  Bit Score: 213.47  E-value: 1.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 256 YLFDITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSF 335
Cdd:COG2199    2 LLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 336 ARRLSSCVRNNDVVSRWGGDEFTLLLPQInTPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDT-ETLL 414
Cdd:COG2199   82 ARRLRSNLREGDLVARLGGDEFAVLLPGT-SLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDDaELLL 160
                        170       180
                 ....*....|....*....|.
gi 172039089 415 KNADAALYRAKERGKNHYRFY 435
Cdd:COG2199  161 RRADLALYRAKRAGRNRVVVF 181
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
272-435 4.91e-64

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563  Cd Length: 163  Bit Score: 211.34  E-value: 4.91e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   272 YRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSR 351
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   352 WGGDEFTLLLPQINtPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKNH 431
Cdd:smart00267  81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ....
gi 172039089   432 YRFY 435
Cdd:smart00267 160 VAVY 163
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
455-686 9.45e-62

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: 249961  Cd Length: 231  Bit Score: 207.62  E-value: 9.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKqglPA 534
Cdd:pfam00563   6 EALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLISPDEFLPLAERLGLIAELDRWVLEKALAQLAEWLN---PD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  535 IPIAVNLSTKQFQQPNLVNIVTQvLEETELDPHLLDLEITETAMMENIDFsQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:pfam00563  83 LPLSVNLSPASLLDPSFLEALLA-LKQGGLPPSRLVLEITESALDEDLRL-LEALARLRSLGFRLALDDFGTGYSSLSLL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 172039089  615 QKFPITTLKIDQSFIQTLQnNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRP 686
Cdd:pfam00563 161 SRLPPDYIKIDRSFIKDLS-DPESRALLRALIALARSLGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 231
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
273-433 5.86e-51

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: 232895  Cd Length: 165  Bit Score: 174.83  E-value: 5.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  273 RAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRW 352
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  353 GGDEFTLLLPQINTpEDTINLAQRILDDLKQ-PFEVSGH-QLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKN 430
Cdd:TIGR00254  81 GGEEFVVILPGTPL-EDALSKAERLRDAINSkPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159

                  ...
gi 172039089  431 HYR 433
Cdd:TIGR00254 160 RVV 162
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
30-105 1.28e-15

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 249907  Cd Length: 67  Bit Score: 72.62  E-value: 1.28e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172039089   30 YSVGRESSNDIVIYEQVVSRRHATIVrvkltpRLDSYSYRIIDgdlegHRSTNGLLINGQL--KDSHNLNHGDVIIFG 105
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIR------YDGGGRFYLED-----LGSTNGTFVNGQRlgPGPVRLRDGDVIRLG 67
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
466-687 5.87e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222  Cd Length: 255  Bit Score: 53.08  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 466 YQPQLRlTNNKISGMEALLRWYHPELGQvspLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQglpaipiavnlstkq 545
Cdd:PRK11596  34 FQPIYR-TSGRLMAIELLTAVTHPSNPS---QRLSPERYFAEITVSHRLDVVKEQLDLLAQWADF--------------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 546 FQQPNL---VNIVTQVLEETELDPHLLDLeITETA-----MMENIDFSQE-TLQKLRDIGvQISLDDFGTGYCSLAYLQK 616
Cdd:PRK11596  95 FVRHGLlasVNIDGPTLIALRQQPAILRL-IERLPwlrfeLVEHIRLPKDsPFASMCEFG-PLWLDDFGTGMANFSALSE 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 172039089 617 FPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPL 687
Cdd:PRK11596 173 VRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
30-89 1.63e-07

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578  Cd Length: 52  Bit Score: 49.10  E-value: 1.63e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 172039089    30 YSVGRES-SNDIVIYEQVVSRRHATIVRvkltprlDSYS-YRIIDgdlegHRSTNGLLINGQ 89
Cdd:smart00240   1 VTIGRSSeDCDIQLDGPSISRRHAVIVY-------DGGGrFYLID-----LGSTNGTFVNGK 50
PRK10060 PRK10060
RNase II stability modulator; Provisional
259-692 1.98e-127

RNase II stability modulator; Provisional


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 395.59  E-value: 1.98e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 259 DITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAkqNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARR 338
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 339 LSSCVRNNDVVSRWGGDEFTLLLPQINTP--EDTinlAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKN 416
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAalEAM---ASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRS 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 417 ADAALYRAKERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNnKISGMEALLRWYHPELGQVSP 496
Cdd:PRK10060 377 ADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPP 455
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 497 LRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLpAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITET 576
Cdd:PRK10060 456 LEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTES 534
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 577 AMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRV 656
Cdd:PRK10060 535 CLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQV 614
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 172039089 657 IAEGVETLQQLEFLQRLHCQEIQGFWFSRPLkPADA 692
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKPM-PAVA 649
COG5001 COG5001
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain ...
258-692 2.29e-104

Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms]


Pssm-ID: 227334 [Multi-domain]  Cd Length: 663  Bit Score: 334.94  E-value: 2.29e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 258 FDITARKQAEKNLEYR----AFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLK 333
Cdd:COG5001  208 VTLTQRAEETRRLSDEndrlANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLI 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 334 SFARRLSSCVRNNDVVSRWGGDEFTLLLPQINTPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETL 413
Cdd:COG5001  288 EVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQL 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 414 LKNADAALYRAKERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQ 493
Cdd:COG5001  368 FERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIGP 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 494 VSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQkqglPAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEI 573
Cdd:COG5001  448 VPPDVFIGIAERSGQIVELTRLLLAKALREARAWP----MDVRVSINLSARDLASMENVRRLLAIVSESCIAPHRLDFEI 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 574 TETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFD 653
Cdd:COG5001  524 TETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLR 603
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 172039089 654 LRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLkPADA 692
Cdd:COG5001  604 MECVVEGVETEAQRDRVAALGATVMQGYHYARPM-PAEE 641
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
8-137 4.63e-18

FOG: FHA domain [Signal transduction mechanisms]


Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 83.08  E-value: 4.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   8 FRHILVIEDQKARRIVAL--------EEATYSVGRESSNDIVIYEQVVSRRHATIVRVKltprldsysyriIDGDLEGHR 79
Cdd:COG1716   61 EPGVLTALDGPLAVTIGLdegsvivlGEPVTTIGRDPDNDIVLDDDVVSRRHAELRREG------------NEVFLEDLG 128
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089  80 STNGLLINGQ-LKDSHNLNHGDVIIFGPQAKVSYYIISTSLDIDLFNPLDPGQLQQEEE 137
Cdd:COG1716  129 STNGTYVNGEkVRQRVLLQDGDVIRLGGTLAERLRIILTELEIDGVDPVATSAKELEEE 187
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
31-183 2.32e-05

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis].


Pssm-ID: 234178 [Multi-domain]  Cd Length: 396  Bit Score: 45.82  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   31 SVGRESSNDIVIY--EQVVSRRHATIVrvkltpRLDSYsYRIIDgdleghRSTNGLLINGQLK-----DSHNLNHGDVII 103
Cdd:TIGR03354  27 TIGRSEDCDWVLPdpERHVSGRHARIR------YRDGA-YLLTD------LSTNGVFLNGSGSplgrgNPVRLEQGDRLR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  104 FGP-QAKVSYYIISTSLDIDLF--------------------NPLDPGQLQQEEEAMIETMMADDNNkstliSDESLQER 162
Cdd:TIGR03354  94 LGDyEIRVSLGDPLVSRQASESradtslptaggpptpdpaplAQLDPLKALDQEPLSAADLDDLSAP-----LFPPLDAR 168
                         170       180
                  ....*....|....*....|....*
gi 172039089  163 DHDDLIRLAS----FPELSPNPIIE 183
Cdd:TIGR03354 169 LPAFAAPIDAeptmVPPFVPLPAPE 193
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
456-691 4.59e-109

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  Cd Length: 240  Bit Score: 332.97  E-value: 4.59e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 456 ALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLPaI 535
Cdd:cd01948    6 ALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPD-L 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 536 PIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQ 615
Cdd:cd01948   85 RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLK 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172039089 616 KFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPAD 691
Cdd:cd01948  165 RLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
275-433 2.58e-68

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  Cd Length: 158  Bit Score: 222.43  E-value: 2.58e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 275 FYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRWGG 354
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089 355 DEFTLLLPQINtPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKNHYR 433
Cdd:cd01949   81 DEFAILLPGTD-LEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
10-106 9.48e-14

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 68.18  E-value: 9.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  10 HILVIEDQKARRIVALEE-ATYSVGRESSN-DIVIYEQVVSRRHATIVRVkltprldsysyRIIDGDLEGHRSTNGLLIN 87
Cdd:cd00060    3 RLVVLSGDASGRRYYLDPgGTYTIGRDSDNcDIVLDDPSVSRRHAVIRYD-----------GDGGVVLIDLGSTNGTFVN 71
                         90       100
                 ....*....|....*....|..
gi 172039089  88 GQLKDSHN---LNHGDVIIFGP 106
Cdd:cd00060   72 GQRVSPGEpvrLRDGDVIRLGN 93
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
455-692 6.77e-101

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


Pssm-ID: 214491  Cd Length: 242  Bit Score: 311.84  E-value: 6.77e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLPA 534
Cdd:smart00052   6 QALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGPPP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   535 IPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:smart00052  86 LLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYL 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172039089   615 QKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLkPADA 692
Cdd:smart00052 166 KRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL-PLDD 242
Rtn COG2200
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]
455-698 2.55e-98

c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]


Pssm-ID: 225110  Cd Length: 256  Bit Score: 305.37  E-value: 2.55e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLpa 534
Cdd:COG2200   10 QALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRTWPRAGP-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 535 IPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:COG2200   88 LRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGTGYSSLSYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 615 QKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPADATT 694
Cdd:COG2200  168 KRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPLPADALDA 247

                 ....
gi 172039089 695 FLSQ 698
Cdd:COG2200  248 LLSS 251
GGDEF pfam00990
GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a ...
274-430 9.66e-67

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.


Pssm-ID: 250276  Cd Length: 159  Bit Score: 218.26  E-value: 9.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  274 AFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRWG 353
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEELEQELQRARRQQSPLALLLIDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089  354 GDEFTLLLPQINTPE--DTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKN 430
Cdd:pfam00990  81 GEEFAILLPDTSLEGaqELAERIRRLLAALAIPHTLSGLPLYVTISIGIAAYPNDGEDPEDLLKRADQALYQAKQQGRN 159
COG2199 COG2199
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]
256-435 1.49e-64

c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]


Pssm-ID: 225109  Cd Length: 181  Bit Score: 213.47  E-value: 1.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 256 YLFDITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSF 335
Cdd:COG2199    2 LLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 336 ARRLSSCVRNNDVVSRWGGDEFTLLLPQInTPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDT-ETLL 414
Cdd:COG2199   82 ARRLRSNLREGDLVARLGGDEFAVLLPGT-SLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDDaELLL 160
                        170       180
                 ....*....|....*....|.
gi 172039089 415 KNADAALYRAKERGKNHYRFY 435
Cdd:COG2199  161 RRADLALYRAKRAGRNRVVVF 181
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
272-435 4.91e-64

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563  Cd Length: 163  Bit Score: 211.34  E-value: 4.91e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   272 YRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSR 351
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   352 WGGDEFTLLLPQINtPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKNH 431
Cdd:smart00267  81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ....
gi 172039089   432 YRFY 435
Cdd:smart00267 160 VAVY 163
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
455-686 9.45e-62

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: 249961  Cd Length: 231  Bit Score: 207.62  E-value: 9.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKqglPA 534
Cdd:pfam00563   6 EALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLISPDEFLPLAERLGLIAELDRWVLEKALAQLAEWLN---PD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  535 IPIAVNLSTKQFQQPNLVNIVTQvLEETELDPHLLDLEITETAMMENIDFsQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:pfam00563  83 LPLSVNLSPASLLDPSFLEALLA-LKQGGLPPSRLVLEITESALDEDLRL-LEALARLRSLGFRLALDDFGTGYSSLSLL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 172039089  615 QKFPITTLKIDQSFIQTLQnNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRP 686
Cdd:pfam00563 161 SRLPPDYIKIDRSFIKDLS-DPESRALLRALIALARSLGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 231
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
273-433 5.86e-51

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: 232895  Cd Length: 165  Bit Score: 174.83  E-value: 5.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  273 RAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRW 352
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  353 GGDEFTLLLPQINTpEDTINLAQRILDDLKQ-PFEVSGH-QLYIKTSIGIAIYPQDGEDTETLLKNADAALYRAKERGKN 430
Cdd:TIGR00254  81 GGEEFVVILPGTPL-EDALSKAERLRDAINSkPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159

                  ...
gi 172039089  431 HYR 433
Cdd:TIGR00254 160 RVV 162
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
30-105 1.28e-15

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 249907  Cd Length: 67  Bit Score: 72.62  E-value: 1.28e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172039089   30 YSVGRESSNDIVIYEQVVSRRHATIVrvkltpRLDSYSYRIIDgdlegHRSTNGLLINGQL--KDSHNLNHGDVIIFG 105
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIR------YDGGGRFYLED-----LGSTNGTFVNGQRlgPGPVRLRDGDVIRLG 67
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
308-401 2.70e-08

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637  Cd Length: 133  Bit Score: 52.74  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 308 LLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSS-CVRNNDVVSRWGGDEFTLLLPqINTPEDTINLAQRILDDLKQPFE 386
Cdd:cd07556    4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSlIRRSGDLKIKTIGDEFMVVSG-LDHPAAAVAFAEDMREAVSALNQ 82
                         90
                 ....*....|....*
gi 172039089 387 VSGhqLYIKTSIGIA 401
Cdd:cd07556   83 SEG--NPVRVRIGIH 95
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
466-687 5.87e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222  Cd Length: 255  Bit Score: 53.08  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 466 YQPQLRlTNNKISGMEALLRWYHPELGQvspLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQglpaipiavnlstkq 545
Cdd:PRK11596  34 FQPIYR-TSGRLMAIELLTAVTHPSNPS---QRLSPERYFAEITVSHRLDVVKEQLDLLAQWADF--------------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 546 FQQPNL---VNIVTQVLEETELDPHLLDLeITETA-----MMENIDFSQE-TLQKLRDIGvQISLDDFGTGYCSLAYLQK 616
Cdd:PRK11596  95 FVRHGLlasVNIDGPTLIALRQQPAILRL-IERLPwlrfeLVEHIRLPKDsPFASMCEFG-PLWLDDFGTGMANFSALSE 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 172039089 617 FPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPL 687
Cdd:PRK11596 173 VRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
30-89 1.63e-07

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578  Cd Length: 52  Bit Score: 49.10  E-value: 1.63e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 172039089    30 YSVGRES-SNDIVIYEQVVSRRHATIVRvkltprlDSYS-YRIIDgdlegHRSTNGLLINGQ 89
Cdd:smart00240   1 VTIGRSSeDCDIQLDGPSISRRHAVIVY-------DGGGrFYLID-----LGSTNGTFVNGK 50
COG1550 COG1550
Uncharacterized protein conserved in bacteria [Function unknown]
356-417 7.22e-03

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 224467  Cd Length: 95  Bit Score: 35.43  E-value: 7.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 172039089 356 EFTLLLPQINTPEDTINLAQRILDDLKQPF-----EVSGHQLYIKTSIGIAIYPQDGEDTETLLKNA 417
Cdd:COG1550    7 ECELRLYDVRSLKEKRAVLRPIVTRLKNKFnvsvaETGYQDLWQRAEIGIATVSSDRAVAERVLDRA 73
PRK10060 PRK10060
RNase II stability modulator; Provisional
259-692 1.98e-127

RNase II stability modulator; Provisional


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 395.59  E-value: 1.98e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 259 DITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAkqNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARR 338
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 339 LSSCVRNNDVVSRWGGDEFTLLLPQINTP--EDTinlAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKN 416
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAalEAM---ASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRS 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 417 ADAALYRAKERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNnKISGMEALLRWYHPELGQVSP 496
Cdd:PRK10060 377 ADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPP 455
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 497 LRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLpAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITET 576
Cdd:PRK10060 456 LEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTES 534
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 577 AMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRV 656
Cdd:PRK10060 535 CLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQV 614
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 172039089 657 IAEGVETLQQLEFLQRLHCQEIQGFWFSRPLkPADA 692
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKPM-PAVA 649
COG5001 COG5001
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain ...
258-692 2.29e-104

Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms]


Pssm-ID: 227334 [Multi-domain]  Cd Length: 663  Bit Score: 334.94  E-value: 2.29e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 258 FDITARKQAEKNLEYR----AFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLK 333
Cdd:COG5001  208 VTLTQRAEETRRLSDEndrlANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLI 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 334 SFARRLSSCVRNNDVVSRWGGDEFTLLLPQINTPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTETL 413
Cdd:COG5001  288 EVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQL 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 414 LKNADAALYRAKERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQ 493
Cdd:COG5001  368 FERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIGP 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 494 VSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQkqglPAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEI 573
Cdd:COG5001  448 VPPDVFIGIAERSGQIVELTRLLLAKALREARAWP----MDVRVSINLSARDLASMENVRRLLAIVSESCIAPHRLDFEI 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 574 TETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFD 653
Cdd:COG5001  524 TETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLR 603
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 172039089 654 LRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLkPADA 692
Cdd:COG5001  604 MECVVEGVETEAQRDRVAALGATVMQGYHYARPM-PAEE 641
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
276-699 2.16e-99

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 325.57  E-value: 2.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 276 YDTLTDLPNRNYFDEKLEIALvkakQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVVSRWGGD 355
Cdd:PRK11359 378 FDPLTGLPNRNNLHNYLDDLV----DKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGT 453
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 356 EFTLLlpqinTPEDTINLAQRILDDLK----QPFEVSGHQLYIKTSIGIAIypQDGEDTETLLKNADAALYRAKERGKNH 431
Cdd:PRK11359 454 QFVLV-----SLENDVSNITQIADELRnvvsKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNG 526
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 432 YRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIP 511
Cdd:PRK11359 527 WQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIEN 606
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 512 ISLWVLKTACQQNKAWQKQGLPAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDFSQETLQK 591
Cdd:PRK11359 607 IGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQI 686
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 592 LRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQ 671
Cdd:PRK11359 687 LRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLR 766
                        410       420
                 ....*....|....*....|....*...
gi 172039089 672 RLHCQEIQGFWFSRPLKPADATTFLSQV 699
Cdd:PRK11359 767 KIHCRVIQGYFFSRPLPAEEIPGWMSSV 794
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
252-690 1.14e-82

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 276.98  E-value: 1.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 252 LIRSYLFDITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALvkAKQNNhlMALLFLDLDSFKNVNDTLGHKIGDQL 331
Cdd:PRK13561 209 LVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVV--ARKQT--TALMIITCETLRDTAGVLKEAQREIL 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 332 LKSFARRLSSCVRNNDVVSRWGGDEFTLLLPQINTPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYpQDGEDTE 411
Cdd:PRK13561 285 LLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAE 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 412 TLLKNADAALYRAKERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPEL 491
Cdd:PRK13561 364 QLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDG 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 492 GQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLpAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDL 571
Cdd:PRK13561 444 SWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGI-MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLIL 522
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 572 EITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKF---PITTLKIDQSFIQTLqnnPANTAIISAIIGL 648
Cdd:PRK13561 523 EVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGL---PEDDSMVAAIIML 599
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 172039089 649 GKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPA 690
Cdd:PRK13561 600 AQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE 641
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
252-698 1.24e-72

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 249.86  E-value: 1.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 252 LIRSYLFDITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHlMALLFLDLDSFKNVNDTLGHKIGDQL 331
Cdd:PRK11829 210 LVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETLQEVSGAMSEAQHQQL 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 332 LKSFARRLSSCVRNNDVVSRWGGDEFTLLLPQINTPEDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIAIYPQDGEDTE 411
Cdd:PRK11829 289 LLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAE 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 412 TLLKNADAALYRAKERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPEL 491
Cdd:PRK11829 369 SMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDG 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 492 GQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGLpAIPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDL 571
Cdd:PRK11829 449 SYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGV-SLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLL 527
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 572 EITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYL---QKFPITTLKIDQSFIQTLqnnPANTAIISAIIGL 648
Cdd:PRK11829 528 EITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARIISCV 604
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 172039089 649 GKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPADattFLSQ 698
Cdd:PRK11829 605 SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE---FEAQ 651
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
259-686 2.90e-69

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 244.97  E-value: 2.90e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  259 DITARKQAEKNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARR 338
Cdd:PRK09776  650 DVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASL 729
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  339 LSSCVRNNDVVSRWGGDEFTLLLPQINTPE-DTInlAQRILDDLKQ-PFEVSGHQLYIKTSIGIAIYPQDGEDTETLLKN 416
Cdd:PRK09776  730 MLSMLRSSDVLARLGGDEFGLLLPDCNVESaRFI--ATRIISAINDyHFPWEGRVYRVGASAGITLIDANNHQASEVMSQ 807
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  417 ADAALYRAKERGKNHYRFYRS---------TMTSKASLLLKlenllykALEEEAFSLDYQ---PQLRLTNNKIsgmEALL 484
Cdd:PRK09776  808 ADIACYAAKNAGRGRVTVYEPqqaaahsehRALSLAEQWRM-------IKENQLMMLAHGvasPRIPEARNHW---LISL 877
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  485 RWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQglPAIPIAVNLSTKQFQQPNLVNIVTQVLEETEL 564
Cdd:PRK09776  878 RLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS--KGLSIALPLSVAGLSSPTLLPFLLEQLENSPL 955
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  565 DPHLLDLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQNNPANTAIISA 644
Cdd:PRK09776  956 PPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISI 1035
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 172039089  645 IIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRP 686
Cdd:PRK09776 1036 IQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
COG4943 COG4943
Predicted signal transduction protein containing sensor and EAL domains [Signal transduction ...
455-698 2.06e-56

Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms]


Pssm-ID: 227279 [Multi-domain]  Cd Length: 524  Bit Score: 201.50  E-value: 2.06e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 455 KALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQGlPA 534
Cdd:COG4943  275 RAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDLLRQH-RD 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 535 IPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMEnIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:COG4943  354 LHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFAD-PKKMTPIILRLREAGHEIYIDDFGTGYSNLHYL 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 615 QKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPADATT 694
Cdd:COG4943  433 QSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKALPAQAFLD 512

                 ....
gi 172039089 695 FLSQ 698
Cdd:COG4943  513 WAEQ 516
PRK10551 PRK10551
phage resistance protein; Provisional
456-698 1.84e-43

phage resistance protein; Provisional


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 163.24  E-value: 1.84e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 456 ALEEEAFSLDYQPQLRLTNNKISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQgLPA- 534
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKV-LPVg 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 535 IPIAVNLSTKQFQQPNLVNIVTQVLEETELDPHLLDLEITETAMMENIDfSQETLQKLRDIGVQISLDDFGTGYCSLAYL 614
Cdd:PRK10551 350 AKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEE-ATKLFAWLHSQGIEIAIDDFGTGHSALIYL 428
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 615 QKFPITTLKIDQSFIQTLQNNPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRPLKPADATT 694
Cdd:PRK10551 429 ERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVR 508

                 ....
gi 172039089 695 FLSQ 698
Cdd:PRK10551 509 WLKE 512
PleD COG3706
Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal ...
263-436 2.54e-40

Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal transduction mechanisms]


Pssm-ID: 226229 [Multi-domain]  Cd Length: 435  Bit Score: 152.86  E-value: 2.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 263 RKQAEKNLE-------YRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSF 335
Cdd:COG3706  252 RKRYERQLReslerlqELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQV 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 336 ARRLSSCVRNNDVVSRWGGDEFTLLLPQINtPEDTINLAQRILDDLKQ---PFEVSGHQLYIKTSIGIAIYPQDGEDTET 412
Cdd:COG3706  332 ARRLRQTVRGLDLVARYGGEEFAVVLPDTD-LEAAIAIAERIRQKINElpfVHELSREPLEVTISIGVAEGKPGEDSIEE 410
                        170       180
                 ....*....|....*....|....
gi 172039089 413 LLKNADAALYRAKERGKNHYRFYR 436
Cdd:COG3706  411 LLKRADKALYKAKASGRNRVVVKR 434
pleD PRK09581
response regulator PleD; Reviewed
263-430 4.05e-39

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 149.67  E-value: 4.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 263 RKQAEKNLEYrAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSC 342
Cdd:PRK09581 282 RNNLEQSIEM-AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNN 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 343 VRNNDVVSRWGGDEFTLLLPQINtPEDTINLAQRILDDL-KQPFEVSG--HQLYIKTSIGIAIYPQDGEDTETLLKNADA 419
Cdd:PRK09581 361 IRGTDLIARYGGEEFVVVMPDTD-IEDAIAVAERIRRKIaEEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADK 439
                        170
                 ....*....|.
gi 172039089 420 ALYRAKERGKN 430
Cdd:PRK09581 440 ALYEAKNTGRN 450
PRK09894 PRK09894
diguanylate cyclase; Provisional
270-430 5.94e-30

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 120.17  E-value: 5.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 270 LEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNhlMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSSCVRNNDVV 349
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQN--LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 350 SRWGGDEFTLLLPQiNTPEDTINLAQRILDDL-KQPFEVSGHQLYIKTSIGIAIYPQdGEDTETLLKNADAALYRAKERG 428
Cdd:PRK09894 203 YRYGGEEFIICLKA-ATDEEACRAGERIRQLIaNHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTG 280

                 ..
gi 172039089 429 KN 430
Cdd:PRK09894 281 RN 282
PRK15426 PRK15426
putative diguanylate cyclase YedQ; Provisional
250-430 3.50e-26

putative diguanylate cyclase YedQ; Provisional


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 112.42  E-value: 3.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 250 HQLIRSYLfditARKQAeknLEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGD 329
Cdd:PRK15426 381 RRMVSNMF----VLQSS---LQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGD 453
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 330 QLLKSFARRLSSCVRNNDVVSRWGGDEFTLLLPQInTPEDTINLAQRI---LDDlKQPFEVSGHQLYIKTSIGIAIYPQD 406
Cdd:PRK15426 454 RVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGA-SLAEAAQVAERIrlrINE-KEILVAKSTTIRISASLGVSSAEED 531
                        170       180
                 ....*....|....*....|....*
gi 172039089 407 GE-DTETLLKNADAALYRAKERGKN 430
Cdd:PRK15426 532 GDyDFEQLQSLADRRLYLAKQAGRN 556
adrA PRK10245
diguanylate cyclase AdrA; Provisional
261-430 2.53e-22

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 97.98  E-value: 2.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 261 TARKQAE--KNLEYRAFYDTLTDLPNRNYFDEKLEIALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARR 338
Cdd:PRK10245 190 TATKLAEhkRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 339 LSSCVRNNDVVSRWGGDEFTLLLpqINTP-EDTINLAQRILDDLKQPFEVSGHQLYIKTSIGIA-IYPQDGEDTEtLLKN 416
Cdd:PRK10245 270 LQITLRGSDVIGRFGGDEFAVIM--SGTPaESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVApLNPQMSHYRE-WLKS 346
                        170
                 ....*....|....
gi 172039089 417 ADAALYRAKERGKN 430
Cdd:PRK10245 347 ADLALYKAKNAGRN 360
PRK09966 PRK09966
putative inner membrane diguanylate cyclase; Provisional
263-427 1.95e-19

putative inner membrane diguanylate cyclase; Provisional


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 90.07  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 263 RKQAEKNLEYR-AFYDTLTDLPNRNYFDEKLEiALVKAKQNNHLMALLFLDLDSFKNVNDTLGHKIGDQLLKSFARRLSS 341
Cdd:PRK09966 236 RLQAKNAQLLRtALHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAE 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 342 CVRNNDVVSRWGGDEFTLLLPQINTPEDTinlaQRILDDLKQ----PFEV-SGHQLYIKTSIGIAIYPQDGEdTETLLKN 416
Cdd:PRK09966 315 FGGLRHKAYRLGGDEFAMVLYDVQSESEV----QQICSALTQifnlPFDLhNGHQTTMTLSIGYAMTIEHAS-AEKLQEL 389
                        170
                 ....*....|.
gi 172039089 417 ADAALYRAKER 427
Cdd:PRK09966 390 ADHNMYQAKHQ 400
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
8-137 4.63e-18

FOG: FHA domain [Signal transduction mechanisms]


Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 83.08  E-value: 4.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   8 FRHILVIEDQKARRIVAL--------EEATYSVGRESSNDIVIYEQVVSRRHATIVRVKltprldsysyriIDGDLEGHR 79
Cdd:COG1716   61 EPGVLTALDGPLAVTIGLdegsvivlGEPVTTIGRDPDNDIVLDDDVVSRRHAELRREG------------NEVFLEDLG 128
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 172039089  80 STNGLLINGQ-LKDSHNLNHGDVIIFGPQAKVSYYIISTSLDIDLFNPLDPGQLQQEEE 137
Cdd:COG1716  129 STNGTYVNGEkVRQRVLLQDGDVIRLGGTLAERLRIILTELEIDGVDPVATSAKELEEE 187
PRK11059 PRK11059
regulatory protein CsrD; Provisional
251-686 1.62e-17

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 85.30  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 251 QLIRSYlfditarkqaeknleyrAFYDTLTDLPNRNYFDEKLEIALvkakQNNHLMA----LLFLDLDSFKNVNDTLGHK 326
Cdd:PRK11059 222 TFIRSN-----------------AFQDAKTGLGNRLFFDNQLATLL----EDQEMVGahgvVMLIRLPDFDLLQEEWGES 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 327 IGDQLLKSFARRLSSCVR--NNDVVSRWGGDEFTLLLPQInTPEDTINLAQRILDDL-KQPFEVSG------Hqlyikts 397
Cdd:PRK11059 281 QVEELLFELINLLSTFVMryPGALLARYSRSDFAVLLPHR-SLKEADSLASQLLKAVdALPPPKMLdrddflH------- 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 398 IGIAIYpQDGEDTETLLKNADAALYRAK-ERGKNHYRFYRSTMTSKASLLLKLENLLYKALEEEAFSLDYQPQLrLTNNK 476
Cdd:PRK11059 353 IGICAY-RSGQSTEQVMEEAEMALRSAQlQGGNGWFVYDKAQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQPAV-TRDGK 430
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 477 ISGMEALLRWYHPELGQVSPLRLIPLAEKTDLIIPISLWVLKTACQQNKAWQKQglpaiPIAVNLSTKQFQQPNLVNIVT 556
Cdd:PRK11059 431 VHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE-----NLSINLSVDSLLSRAFQRWLR 505
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089 557 QVLEETE--LDPHLLdLEITETAMMENIDFSQETLQKLRDIGVQISLDDFGTGYCSLAYLQKFPITTLKIDQSFIQTLQN 634
Cdd:PRK11059 506 DTLLQCPrsQRKRLI-FELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHK 584
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 172039089 635 NPANTAIISAIIGLGKSFDLRVIAEGVETLQQLEFLQRLHCQEIQGFWFSRP 686
Cdd:PRK11059 585 RTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
31-183 2.32e-05

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis].


Pssm-ID: 234178 [Multi-domain]  Cd Length: 396  Bit Score: 45.82  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089   31 SVGRESSNDIVIY--EQVVSRRHATIVrvkltpRLDSYsYRIIDgdleghRSTNGLLINGQLK-----DSHNLNHGDVII 103
Cdd:TIGR03354  27 TIGRSEDCDWVLPdpERHVSGRHARIR------YRDGA-YLLTD------LSTNGVFLNGSGSplgrgNPVRLEQGDRLR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172039089  104 FGP-QAKVSYYIISTSLDIDLF--------------------NPLDPGQLQQEEEAMIETMMADDNNkstliSDESLQER 162
Cdd:TIGR03354  94 LGDyEIRVSLGDPLVSRQASESradtslptaggpptpdpaplAQLDPLKALDQEPLSAADLDDLSAP-----LFPPLDAR 168
                         170       180
                  ....*....|....*....|....*
gi 172039089  163 DHDDLIRLAS----FPELSPNPIIE 183
Cdd:TIGR03354 169 LPAFAAPIDAeptmVPPFVPLPAPE 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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