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Conserved domains on  [gi|1277872826|gb|PIU80234|]
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hypothetical protein COS73_00305 [Nitrospirae bacterium CG06_land_8_20_14_3_00_70_43]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13413304)

sensor domain-containing diguanylate cyclase (GGDEF) with a GAF family sensor domain

CATH:  3.30.450.40|3.30.70.1230
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0005886|GO:0005515|GO:0046872|GO:0052621|GO:0007165
PubMed:  16166544|9433123
SCOP:  4001852|4001316

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 236-396 1.02e-46

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


:

Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 160.03  E-value: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 236 IDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRA 315
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRS------GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 316 YRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASdtGTMVRITASLGVADANVCGR---AVVRCADLALYRAKEEG 392
Cdd:cd01949    76 ARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFID--GQEIRVTASIGIATYPEDGEdaeELLRRADEALYRAKRSG 153


                  ....
gi 1277872826 393 GDRI 396
Cdd:cd01949   154 RNRV 157
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 9-399 4.10e-42

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 159.94  E-value: 4.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   9 ADRSAELAELAHAILADHDLPATAHYLQLFGRVYRHFLEAVPPHQRNRDRLADLFRASIGLPPPHGDARPAPELEREVKR 88
Cdd:COG5001    25 LLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  89 LAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQIEETERTLL 168
Cdd:COG5001   105 LLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLAL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 169 PRMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQIATGDGGSPLVAAIRRLKEEAA-AAGIDALTGLAGRAL 247
Cdd:COG5001   185 LLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRhLAYHDPLTGLPNRRL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 248 FDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAYRLGGDEFLLLL 327
Cdd:COG5001   265 FLDRLEQALARARRS------GRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLL 338

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277872826 328 TD-TDAPGAAHVAEVVRDAIRN-VAVAsdtGTMVRITASLGVA---DANVCGRAVVRCADLALYRAKEEGGDRITTY 399
Cdd:COG5001   339 PDlDDPEDAEAVAERILAALAEpFELD---GHELYVSASIGIAlypDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 236-396 1.02e-46

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 160.03  E-value: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 236 IDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRA 315
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRS------GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 316 YRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASdtGTMVRITASLGVADANVCGR---AVVRCADLALYRAKEEG 392
Cdd:cd01949    76 ARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFID--GQEIRVTASIGIATYPEDGEdaeELLRRADEALYRAKRSG 153


                  ....
gi 1277872826 393 GDRI 396
Cdd:cd01949   154 RNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 118-399 8.05e-45

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 158.99  E-value: 8.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 118 RTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQIEETERTLLPRMTTAARPEMETVLALEGVALRGELMEV 197
Cdd:COG2199     7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 198 TMELTEVVEKLEQIATgdggspLVAAIRRLKEeaaAAGIDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYL 277
Cdd:COG2199    87 LLALLLLLLALEDITE------LRRLEERLRR---LATHDPLTGLPNRRAFEERLERELARARRE------GRPLALLLI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 278 DLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDtGT 357
Cdd:COG2199   152 DLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GK 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1277872826 358 MVRITASLGVADANVCGR---AVVRCADLALYRAKEEGGDRITTY 399
Cdd:COG2199   231 ELRVTVSIGVALYPEDGDsaeELLRRADLALYRAKRAGRNRVVVY 275
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 9-399 4.10e-42

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: 159.94  E-value: 4.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   9 ADRSAELAELAHAILADHDLPATAHYLQLFGRVYRHFLEAVPPHQRNRDRLADLFRASIGLPPPHGDARPAPELEREVKR 88
Cdd:COG5001    25 LLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  89 LAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQIEETERTLL 168
Cdd:COG5001   105 LLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLAL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 169 PRMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQIATGDGGSPLVAAIRRLKEEAA-AAGIDALTGLAGRAL 247
Cdd:COG5001   185 LLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRhLAYHDPLTGLPNRRL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 248 FDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAYRLGGDEFLLLL 327
Cdd:COG5001   265 FLDRLEQALARARRS------GRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLL 338

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277872826 328 TD-TDAPGAAHVAEVVRDAIRN-VAVAsdtGTMVRITASLGVA---DANVCGRAVVRCADLALYRAKEEGGDRITTY 399
Cdd:COG5001   339 PDlDDPEDAEAVAERILAALAEpFELD---GHELYVSASIGIAlypDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 234-395 2.54e-37

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 135.07  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 234 AGIDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALRE------GSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVR-ITASLGVADANVCGR---AVVRCADLALYRAK 389
Cdd:pfam00990  75 LVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGEdpeDLLKRADTALYQAK 154


                  ....*.
gi 1277872826 390 EEGGDR 395
Cdd:pfam00990 155 QAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 234-396 1.14e-36

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 133.53  E-value: 1.14e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  234 AGIDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQ------GSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVAsdTGTMVRITASLGVADANVCGR---AVVRCADLALYRAKE 390
Cdd:smart00267  77 LLARLGGDEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAAYPNPGEdaeDLLKRADTALYQAKK 154


                   ....*.
gi 1277872826  391 EGGDRI 396
Cdd:smart00267 155 AGRNQV 160
PRK09894 PRK09894
diguanylate cyclase; Provisional
 222-396 2.27e-31

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 122.87  E-value: 2.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 222 AAIRRLKEE--AAAAGIDALTGLAGRALFDRDLGHALAanqrtrytRATNQTVVAIYLDLDGFKAVNDTHGHATGDALLR 299
Cdd:PRK09894  115 AALTDYKIYllTIRSNMDVLTGLPGRRVLDESFDHQLR--------NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLR 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 300 AVAAVFGARCRENDRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTmVRITASLGV--ADANVCGRAV 377
Cdd:PRK09894  187 TLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGR-INITATFGVsrAFPEETLDVV 265

                         170
                  ....*....|....*....
gi 1277872826 378 VRCADLALYRAKEEGGDRI 396
Cdd:PRK09894  266 IGRADRAMYEGKQTGRNRV 284
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 234-396 2.72e-30

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 115.90  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 234 AGIDALTGLAGRALFDrdlghALAANQRTRYTRATNQTVVaIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLE-----EMLDSELKRARRFQRSFSV-LMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVRITASLGVADANVCG---RAVVRCADLALYRAKE 390
Cdd:TIGR00254  76 VVGRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGltlEELLKRADEALYQAKK 155


                  ....*.
gi 1277872826 391 EGGDRI 396
Cdd:TIGR00254 156 AGRNRV 161
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
237-350 3.72e-16

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 81.16  E-value: 3.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 237 DALTGLAGRALFDRDLghalaaNQRTRYTRATNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAY 316
Cdd:NF040885  344 DSMTGLYNRKILTPTL------EQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGI 417

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277872826 317 RLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVA 350
Cdd:NF040885  418 RLGGDEFCIILIDYEEAEAQNLIERIRQHLRTID 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-234 7.33e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 7.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   81 ELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVtnlyHELAAQLAAEQRQLAEREVALQRREAELNQRLAQI 160
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL----EQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277872826  161 EETERTLLP----RMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQIATGdggspLVAAIRRLKEEAAAA 234
Cdd:TIGR02168  750 AQLSKELTEleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-----LRAELTLLNEEAANL 822
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 81-238 2.45e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.66  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  81 ELEREVKRLAGMVAELESQARAwsveriALEAGAEQ-GRTVVTNL--YHELAAQLAAEQRQLAEREVALQRREAELNQRL 157
Cdd:pfam04012  54 QLERRLEQQTEQAKKLEEKAQA------ALTKGNEElAREALAEKksLEKQAEALETQLAQQRSAVEQLRKQLAALETKI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 158 AQIEETERTLLPRMTTA-ARPEMETVLALEGValrGELMEVTMELTEVVEKLEQIATGDGGSPLVAAirrLKEEAAAAGI 236
Cdd:pfam04012 128 QQLKAKKNLLKARLKAAkAQEAVQTSLGSLST---SSATDSFERIEEKIEEREARADAAAELASAVD---LDAKLEQAGI 201


                  ..
gi 1277872826 237 DA 238
Cdd:pfam04012 202 QM 203
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 236-396 1.02e-46

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 160.03  E-value: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 236 IDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRA 315
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRS------GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 316 YRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASdtGTMVRITASLGVADANVCGR---AVVRCADLALYRAKEEG 392
Cdd:cd01949    76 ARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFID--GQEIRVTASIGIATYPEDGEdaeELLRRADEALYRAKRSG 153


                  ....
gi 1277872826 393 GDRI 396
Cdd:cd01949   154 RNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 118-399 8.05e-45

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 158.99  E-value: 8.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 118 RTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQIEETERTLLPRMTTAARPEMETVLALEGVALRGELMEV 197
Cdd:COG2199     7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 198 TMELTEVVEKLEQIATgdggspLVAAIRRLKEeaaAAGIDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYL 277
Cdd:COG2199    87 LLALLLLLLALEDITE------LRRLEERLRR---LATHDPLTGLPNRRAFEERLERELARARRE------GRPLALLLI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 278 DLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDtGT 357
Cdd:COG2199   152 DLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GK 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1277872826 358 MVRITASLGVADANVCGR---AVVRCADLALYRAKEEGGDRITTY 399
Cdd:COG2199   231 ELRVTVSIGVALYPEDGDsaeELLRRADLALYRAKRAGRNRVVVY 275
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 9-399 4.10e-42

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: 159.94  E-value: 4.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   9 ADRSAELAELAHAILADHDLPATAHYLQLFGRVYRHFLEAVPPHQRNRDRLADLFRASIGLPPPHGDARPAPELEREVKR 88
Cdd:COG5001    25 LLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  89 LAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQIEETERTLL 168
Cdd:COG5001   105 LLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLAL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 169 PRMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQIATGDGGSPLVAAIRRLKEEAA-AAGIDALTGLAGRAL 247
Cdd:COG5001   185 LLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRhLAYHDPLTGLPNRRL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 248 FDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAYRLGGDEFLLLL 327
Cdd:COG5001   265 FLDRLEQALARARRS------GRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLL 338

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277872826 328 TD-TDAPGAAHVAEVVRDAIRN-VAVAsdtGTMVRITASLGVA---DANVCGRAVVRCADLALYRAKEEGGDRITTY 399
Cdd:COG5001   339 PDlDDPEDAEAVAERILAALAEpFELD---GHELYVSASIGIAlypDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 234-395 2.54e-37

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 135.07  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 234 AGIDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALRE------GSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVR-ITASLGVADANVCGR---AVVRCADLALYRAK 389
Cdd:pfam00990  75 LVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGEdpeDLLKRADTALYQAK 154


                  ....*.
gi 1277872826 390 EEGGDR 395
Cdd:pfam00990 155 QAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 234-396 1.14e-36

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 133.53  E-value: 1.14e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  234 AGIDALTGLAGRALFDRDLGHALAANQRTrytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQ------GSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVAsdTGTMVRITASLGVADANVCGR---AVVRCADLALYRAKE 390
Cdd:smart00267  77 LLARLGGDEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAAYPNPGEdaeDLLKRADTALYQAKK 154


                   ....*.
gi 1277872826  391 EGGDRI 396
Cdd:smart00267 155 AGRNQV 160
PRK09894 PRK09894
diguanylate cyclase; Provisional
 222-396 2.27e-31

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 122.87  E-value: 2.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 222 AAIRRLKEE--AAAAGIDALTGLAGRALFDRDLGHALAanqrtrytRATNQTVVAIYLDLDGFKAVNDTHGHATGDALLR 299
Cdd:PRK09894  115 AALTDYKIYllTIRSNMDVLTGLPGRRVLDESFDHQLR--------NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLR 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 300 AVAAVFGARCRENDRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTmVRITASLGV--ADANVCGRAV 377
Cdd:PRK09894  187 TLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGR-INITATFGVsrAFPEETLDVV 265

                         170
                  ....*....|....*....
gi 1277872826 378 VRCADLALYRAKEEGGDRI 396
Cdd:PRK09894  266 IGRADRAMYEGKQTGRNRV 284
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 234-396 2.72e-30

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 115.90  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 234 AGIDALTGLAGRALFDrdlghALAANQRTRYTRATNQTVVaIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLE-----EMLDSELKRARRFQRSFSV-LMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVRITASLGVADANVCG---RAVVRCADLALYRAKE 390
Cdd:TIGR00254  76 VVGRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGltlEELLKRADEALYQAKK 155


                  ....*.
gi 1277872826 391 EGGDRI 396
Cdd:TIGR00254 156 AGRNRV 161
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 227-399 1.80e-27

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 117.47  E-value: 1.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  227 LKEEAAAAGIDALTGLAGRALFDRDLGHALAANQRTRytratnQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFG 306
Cdd:PRK09776   658 LRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTH------QRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  307 ARCRENDRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDtGTMVRITASLGVA--DANVCGRA-VVRCADL 383
Cdd:PRK09776   732 SMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWE-GRVYRVGASAGITliDANNHQASeVMSQADI 810

                          170
                   ....*....|....*.
gi 1277872826  384 ALYRAKEEGGDRITTY 399
Cdd:PRK09776   811 ACYAAKNAGRGRVTVY 826
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
237-410 2.48e-25

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 109.72  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 237 DALTGLAGR-ALFDRdlghALAANQRTRytrATNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRA 315
Cdd:PRK15426  401 DPLTRLYNRgALFEK----ARALAKRCQ---RDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 316 YRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVRITASLGVADA--NVCG--RAVVRCADLALYRAKEE 391
Cdd:PRK15426  474 GRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAeeDGDYdfEQLQSLADRRLYLAKQA 553

                         170
                  ....*....|....*....
gi 1277872826 392 GGDRITtyCDDAFSAPLPP 410
Cdd:PRK15426  554 GRNRVC--ASDNAHEREVK 570
pleD PRK09581
response regulator PleD; Reviewed
 234-396 6.79e-23

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 101.52  E-value: 6.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 234 AGIDALTGLAGRALFDRDLgHALAANQRTRytratNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREND 313
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHL-KNLIERANER-----GKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTD 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVA-SDTGTMVRITASLGVADANVCG---RAVVRCADLALYRAK 389
Cdd:PRK09581  366 LIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIiSDGKERLNVTVSIGVAELRPSGdtiEALIKRADKALYEAK 445


                  ....*..
gi 1277872826 390 EEGGDRI 396
Cdd:PRK09581  446 NTGRNRV 452
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
223-392 7.67e-21

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 96.29  E-value: 7.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 223 AIRRLKEeaaAAGIDALTGLAGR-ALFDRdLGHALAAnqrtrytrATNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAV 301
Cdd:PRK10060  229 AQERLRI---LANTDSITGLPNRnAIQEL-IDHAINA--------ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 302 AAVFGARCRENDRAYRLGGDEFLLLLTDTDAPG----AAHVAEVVRDAIRNVAVASDTGtmvritASLGVADANVCG--- 374
Cdd:PRK10060  297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQAAleamASRILTRLRLPFRIGLIEVYTG------CSIGIALAPEHGdds 370

                         170
                  ....*....|....*...
gi 1277872826 375 RAVVRCADLALYRAKEEG 392
Cdd:PRK10060  371 ESLIRSADTAMYTAKEGG 388
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
237-350 3.72e-16

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 81.16  E-value: 3.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 237 DALTGLAGRALFDRDLghalaaNQRTRYTRATNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAY 316
Cdd:NF040885  344 DSMTGLYNRKILTPTL------EQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGI 417

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277872826 317 RLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVA 350
Cdd:NF040885  418 RLGGDEFCIILIDYEEAEAQNLIERIRQHLRTID 451
PRK09966 PRK09966
diguanylate cyclase DgcN;
237-395 5.33e-13

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 70.81  E-value: 5.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 237 DALTGLAGRALFdRDLGHALAANQRTRYTRATnqtvvaIYLDLDGFKAVNDTHGHATGDALLRAVA---AVFGArcrEND 313
Cdd:PRK09966  251 DPLTGLANRAAF-RSGINTLMNNSDARKTSAL------LFLDGDNFKYINDTWGHATGDRVLIEIAkrlAEFGG---LRH 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 314 RAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVRITASLGVADA--NVCGRAVVRCADLALYRAKEE 391
Cdd:PRK09966  321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTieHASAEKLQELADHNMYQAKHQ 400


                  ....
gi 1277872826 392 GGDR 395
Cdd:PRK09966  401 RAEK 404
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 313-389 1.46e-10

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 60.31  E-value: 1.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277872826 313 DRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVasdtgtmVRITASLGVADANvcgraVVRCADlALYRAK 389
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPS-------LRVTVSIGVAGDS-----LLKRAD-ALYQAR 179
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 237-395 1.76e-10

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 62.54  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 237 DALTGLagralFDRDLGHALAANQRTRYTRATNQTVVAIyLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAY 316
Cdd:PRK10245  208 DGMTGV-----YNRRHWETLLRNEFDNCRRHHRDATLLI-IDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 317 RLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVAVASDTGTMVRItaSLGVADANV---CGRAVVRCADLALYRAKEEGG 393
Cdd:PRK10245  282 RFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRI--SVGVAPLNPqmsHYREWLKSADLALYKAKNAGR 359


                  ..
gi 1277872826 394 DR 395
Cdd:PRK10245  360 NR 361
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 272-389 5.66e-10

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 [Multi-domain]  Cd Length: 133  Bit Score: 57.37  E-value: 5.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 272 VVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCREN-DRAYRLGGDEFLLLLTDTDAPGAAHVAEVVRDAIRNVA 350
Cdd:cd07556     2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1277872826 351 VASDTGTMVRITASLGVADANVCGR--------AVVRCADLALYRAK 389
Cdd:cd07556    82 QSEGNPVRVRIGIHTGPVVVGVIGSrpqydvwgALVNLASRMESQAK 128
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 237-393 2.47e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 60.17  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 237 DALTGLAGRALFDRDLGHALAanqrtrytraTNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDRAY 316
Cdd:PRK11359  379 DPLTGLPNRNNLHNYLDDLVD----------KAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLC 448

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277872826 317 RLGGDEFLLLLTDTDAPGAAHVAEVVRdAIRNVAVASDtGTMVRITASLGVA-DANVCGRAVVRCADLALYRAKEEGG 393
Cdd:PRK11359  449 RIEGTQFVLVSLENDVSNITQIADELR-NVVSKPIMID-DKPFPLTLSIGISyDVGKNRDYLLSTAHNAMDYIRKNGG 524
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-395 7.14e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  81 ELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREvALQRREAELNQRLAQI 160
Cdd:COG1196   341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-ELEEAEEALLERLERL 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 161 EETERTLLPRMTTAARPEMETVLALEgvALRGELMEVTMELTEVVEKLEQiatgdggsplvaaiRRLKEEAAAAGIDALT 240
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALE--EAAEEEAELEEEEEALLELLAE--------------LLEEAALLEAALAELL 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 241 GLAGRALFDRDLGHALAANQRTRYTRATNQTVVAIYLDLDGFKAVNDTHGHATGDALLRAVAAVFGARCRENDR------ 314
Cdd:COG1196   484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEvaaaai 563

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 315 ----AYRLGGDEFLLLLT--DTDAPGAAHVAEVVRDAIRNVAVASDTGTMVRITASLGVADAnvcgRAVVRCADLALYRA 388
Cdd:COG1196   564 eylkAAKAGRATFLPLDKirARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR----TLVAARLEAALRRA 639


                  ....*..
gi 1277872826 389 KEEGGDR 395
Cdd:COG1196   640 VTLAGRL 646
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-234 7.33e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 7.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   81 ELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVtnlyHELAAQLAAEQRQLAEREVALQRREAELNQRLAQI 160
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL----EQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277872826  161 EETERTLLP----RMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQIATGdggspLVAAIRRLKEEAAAA 234
Cdd:TIGR02168  750 AQLSKELTEleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-----LRAELTLLNEEAANL 822
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-197 1.22e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   81 ELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLA---AEQRQLAEREVALQRREAELNQRL 157
Cdd:COG4913    342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEaleEELEALEEALAEAEAALRDLRREL 421

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1277872826  158 AQIE------ETERTLLPRMTTAARPEMETVLALEGVALR--GELMEV 197
Cdd:COG4913    422 RELEaeiaslERRKSNIPARLLALRDALAEALGLDEAELPfvGELIEV 469
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-261 1.50e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  81 ELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQR------QLAEREVALQRREAELN 154
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 155 QRLAQIEETERTLlpRMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQiatgdggspLVAAIRRLKEEAAAA 234
Cdd:COG1196   316 ERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---------AEAELAEAEEELEEL 384

                         170       180
                  ....*....|....*....|....*..
gi 1277872826 235 GIDALTGLAGRALFDRDLGHALAANQR 261
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEA 411
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 81-238 2.45e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.66  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  81 ELEREVKRLAGMVAELESQARAwsveriALEAGAEQ-GRTVVTNL--YHELAAQLAAEQRQLAEREVALQRREAELNQRL 157
Cdd:pfam04012  54 QLERRLEQQTEQAKKLEEKAQA------ALTKGNEElAREALAEKksLEKQAEALETQLAQQRSAVEQLRKQLAALETKI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 158 AQIEETERTLLPRMTTA-ARPEMETVLALEGValrGELMEVTMELTEVVEKLEQIATGDGGSPLVAAirrLKEEAAAAGI 236
Cdd:pfam04012 128 QQLKAKKNLLKARLKAAkAQEAVQTSLGSLST---SSATDSFERIEEKIEEREARADAAAELASAVD---LDAKLEQAGI 201


                  ..
gi 1277872826 237 DA 238
Cdd:pfam04012 202 QM 203
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-210 3.23e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   2 ASRLPSPADRSAELAELAHAILADHDLPATAHYLQlfgRVYRHFLEAVPPHQRNRDRLADLFRASIGLPPPHGDARPAPE 81
Cdd:COG1196   574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDL---READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  82 LEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQIE 161
Cdd:COG1196   651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1277872826 162 ETErtllpRMTTAARPEMETVLALEGVALRGELMEVTMELTEVVEKLEQ 210
Cdd:COG1196   731 EAE-----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
81-239 4.30e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.65  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  81 ELEREVKRLAGMVAELESQARAwsveriALEAGAEqgrtvvtNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQI 160
Cdd:COG1842    55 RLERQLEELEAEAEKWEEKARL------ALEKGRE-------DLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEAL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826 161 EETERTLlprmtTAARPEMETVLALEGVAlrgelmevtmeltEVVEKLEQIATGDGGSPLVAAIRRLKE-----EAAAAG 235
Cdd:COG1842   122 RQLESKL-----EELKAKKDTLKARAKAA-------------KAQEKVNEALSGIDSDDATSALERMEEkieemEARAEA 183


                  ....
gi 1277872826 236 IDAL 239
Cdd:COG1842   184 AAEL 187
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 81-168 6.26e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   81 ELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVTNlyhelAAQLAAEQRQLAEREVALQRREAELNQRLAQI 160
Cdd:COG3096    582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALAD-----SQEVTAAMQQLLEREREATVERDELAARKQAL 656


                   ....*...
gi 1277872826  161 EETERTLL 168
Cdd:COG3096    657 ESQIERLS 664
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 81-205 6.49e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 6.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   81 ELEREVKRLAGMVAELESQARAWSVERIALEAgaeQGRtVVTNLYHELAAQLAAEQRQLAEREVALQrreaELNQRLAQI 160
Cdd:TIGR02169  865 ELEEELEELEAALRDLESRLGDLKKERDELEA---QLR-ELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEI 936

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1277872826  161 EETERTLLprmttaarPEMETVLALEGVALRGELMEVTMELTEVV 205
Cdd:TIGR02169  937 EDPKGEDE--------EIPEEELSLEDVQAELQRVEEEIRALEPV 973
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-230 6.95e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 6.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826   79 APELEREVKRLAGMVAELEsqarawsveriALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLA 158
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLK-----------RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277872826  159 QIEETERTL--LPRMTTAARPEMETvlalegvaLRGELMEVTMELTEVVEKLEQIATGDGGSP---LVAAIRRLKEE 230
Cdd:TIGR02169  738 RLEELEEDLssLEQEIENVKSELKE--------LEARIEELEEDLHKLEEALNDLEARLSHSRipeIQAELSKLEEE 806
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
80-234 7.67e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277872826  80 PELEREVKRLAGMVAELESQARAWSVERIALEAGAEQGRTVVTNLYHELAAQLAAEQRQLAEREVALQRREAELNQRLAQ 159
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277872826 160 IEETERTLLPRMTTAARPEMETVLALEGVALrgELMEVTMELTEVVEKLEQIATGDGGSPLVAAIRRLKEEAAAA 234
Cdd:COG4717   229 LEQLENELEAAALEERLKEARLLLLIAAALL--ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
 
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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