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Conserved domains on  [gi|27383034|ref|NP_774563|]
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guanylate cyclase [Bradyrhizobium diazoefficiens USDA 110]

Protein classification: adenylate/guanylate cyclase domain-containing protein with a CHASE2 sensor domain, similar to Myxococcus xanthus CyaA and CyaB adenylate cyclases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
473-661 3.86e-54

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


:

Pssm-ID: 143636  Cd Length: 177  Bit Score: 184.70  E-value: 3.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 473 EMTIMFSDVRGFTTISEsyKHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIMAFWNAPLDDAEHEVNACEAAIQM 552
Cdd:cd07302   1 EVTVLFADIVGFTALSE--RLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 553 LERIDAVNKEREEEAadgghvyiPLNVGIGLNTGIGVVGNMGSDlKKNYSVLGDSVNLASRLEGQSKeyGFPIIVGSRTA 632
Cdd:cd07302  79 QEALAELNAEREGGP--------PLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATY 147
                       170       180       190
                ....*....|....*....|....*....|
gi 27383034 633 LAAKDK-FAILELDFIMVKGKTEPEVIYAV 661
Cdd:cd07302 148 ELLGDAgFEFEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
41-373 4.94e-84

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


:

Pssm-ID: 215016  Cd Length: 303  Bit Score: 270.78  E-value: 4.94e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034     41 QELRLRTFDMFQLIDPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIADLIQNLTSNGAVAIGFDVVFSEADRLNPDlva 120
Cdd:smart01080   1 QRLELRLYDARFRLRPRRAPDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDILFDEPDRDSPD--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    121 sqmrylddatraklrelptNDQILADAIKRSRVVLGetgqraisseidkeLPFTGVATVGEDGAERFLFEFPGLLRNVPV 200
Cdd:smart01080  78 -------------------GDAALAAALARAPNVVL--------------LAKLSREAGGGVLPSPPLPLPELPLPPLPG 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    201 IEKVAAGRGLFSIkTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITGTPTLLVRTDKTGVRGVRLKGVEIPTDRNGQLW 280
Cdd:smart01080 125 LADAAAGLGHVNE-PDADGVVRRVPLLLRYGGKAYPSLALELARVALGTPPLRLRLGGLGGPALTLGDGGYPGDRAGRLL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    281 VHY---ARQDPSIYVSAADVLDNTVP--PAKIAGKLVLVGTSAVGLNDIKTTPVSSTMPGVEIHAQVLESVLSGAVISQ- 354
Cdd:smart01080 204 IPFdgpGRGGTFPTVSAADVLDGEVPalPELLRGKIVLIGATAAGLGDLFPTPFSRVMPGVEIHANAIDNLLDGRFLRPa 283
                          330       340
                   ....*....|....*....|
gi 27383034    355 -PNYALGVELIAALVIGLLV 373
Cdd:smart01080 284 pPWWALLLLLLLWLLLGLLL 303
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
451-665 4.20e-28

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 113.40  E-value: 4.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 451 SPVLVEQLAQSPEKLVLGGEE--REMTIMFSDVRGFTTISESykHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAI 528
Cdd:COG2114  22 DLVLRLYLARVVGRLLARGGAgdRRVTLLFADIVGSTELSES--LGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGF 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 529 MAFWNAPLdDAEHEVnACEAAIQmLERIDAVNKEREEeaadgghvyiPLNVGIGLNTGIGVVGNMGSdlkknYSVLGDSV 608
Cdd:COG2114 100 LAVFGRPS-PLEDAV-ACALDLQ-LALRNPLARLRRE----------SLRVRIGIHTGEVVVGNTGG-----YTVVGSAV 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27383034 609 NLASRLEGQSKeyGFPIIVGSRTA-LAAKDKFAILELDFIMVKGKTEPEVIYAVAGRE 665
Cdd:COG2114 162 NQAARLESLAK--PGQVLLSEATYdLVRDLVDLFSGLGSHRLKGLARPVRVYQLCHRS 217
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
473-661 3.86e-54

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636  Cd Length: 177  Bit Score: 184.70  E-value: 3.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 473 EMTIMFSDVRGFTTISEsyKHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIMAFWNAPLDDAEHEVNACEAAIQM 552
Cdd:cd07302   1 EVTVLFADIVGFTALSE--RLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 553 LERIDAVNKEREEEAadgghvyiPLNVGIGLNTGIGVVGNMGSDlKKNYSVLGDSVNLASRLEGQSKeyGFPIIVGSRTA 632
Cdd:cd07302  79 QEALAELNAEREGGP--------PLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATY 147
                       170       180       190
                ....*....|....*....|....*....|
gi 27383034 633 LAAKDK-FAILELDFIMVKGKTEPEVIYAV 661
Cdd:cd07302 148 ELLGDAgFEFEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
41-373 4.94e-84

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


Pssm-ID: 215016  Cd Length: 303  Bit Score: 270.78  E-value: 4.94e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034     41 QELRLRTFDMFQLIDPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIADLIQNLTSNGAVAIGFDVVFSEADRLNPDlva 120
Cdd:smart01080   1 QRLELRLYDARFRLRPRRAPDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDILFDEPDRDSPD--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    121 sqmrylddatraklrelptNDQILADAIKRSRVVLGetgqraisseidkeLPFTGVATVGEDGAERFLFEFPGLLRNVPV 200
Cdd:smart01080  78 -------------------GDAALAAALARAPNVVL--------------LAKLSREAGGGVLPSPPLPLPELPLPPLPG 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    201 IEKVAAGRGLFSIkTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITGTPTLLVRTDKTGVRGVRLKGVEIPTDRNGQLW 280
Cdd:smart01080 125 LADAAAGLGHVNE-PDADGVVRRVPLLLRYGGKAYPSLALELARVALGTPPLRLRLGGLGGPALTLGDGGYPGDRAGRLL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    281 VHY---ARQDPSIYVSAADVLDNTVP--PAKIAGKLVLVGTSAVGLNDIKTTPVSSTMPGVEIHAQVLESVLSGAVISQ- 354
Cdd:smart01080 204 IPFdgpGRGGTFPTVSAADVLDGEVPalPELLRGKIVLIGATAAGLGDLFPTPFSRVMPGVEIHANAIDNLLDGRFLRPa 283
                          330       340
                   ....*....|....*....|
gi 27383034    355 -PNYALGVELIAALVIGLLV 373
Cdd:smart01080 284 pPWWALLLLLLLWLLLGLLL 303
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
23-373 8.43e-83

CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE2 domains are not known at this time.


Pssm-ID: 253103  Cd Length: 305  Bit Score: 267.65  E-value: 8.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    23 LALLVVFAGARLWDPPPIQELRLRTFDMFQLI----DPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIADLIQNLTSNG 98
Cdd:pfam05226   1 LALLLLLLLALLSLRPLLQRLELALYDLLFRLrgprAPPPEPDPRIVIVAIDEASLAELGRWPWPRALLARLLDRLAAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    99 AVAIGFDVVFSEADRLNPDlvasqmrylddatraklrelptNDQILADAIKRS--RVVLGETGQRAISSEIDKELPftgv 176
Cdd:pfam05226  81 AKAIGLDILFDEPDRDSPA----------------------GDAALAAALARAgnPVVLGVFLEASEDGGGPLAPP---- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   177 atvgedgaerflfefpgllrnvPVIEKVAAGRGLFSIKTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITGTPTLLVRT 256
Cdd:pfam05226 135 ----------------------PALAAAAAGLGFVNVVPDSDGVVRRVPLLLRYGGRLYPSLALALARVALGAPPIRAEA 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   257 DKTGVrgvrlkGVEIPTDrNGQLWVHYARQDPSI-YVSAADVLDNTVPPAKIAGKLVLVGTSAVGLNDIKTTPVSSTMPG 335
Cdd:pfam05226 193 DAGGG------DRRIPTD-GGQLLLNFRGPAGTFpTVSAADVLEGRVPPELLRGKIVLIGATAAGLGDLFPTPFSGRMPG 265
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 27383034   336 VEIHAQVLESVLSGAVISQPN--YALGVELIAALVIGLLV 373
Cdd:pfam05226 266 VEIHANAISNLLSGRLLRPWPdwVELLLILLLALLLGLLL 305
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
10-428 5.55e-42

Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 226703  Cd Length: 400  Bit Score: 157.17  E-value: 5.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034  10 WFARKLGLARLMCLALLVVFAGARLWDPPPIQELRLRTFDMFQLIDPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIAD 89
Cdd:COG4252   8 LLSRVWRLRVILLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLGQWPWPRAALAR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034  90 LIQNLTSNGAVAIGFDVVFSEADRlnpdlvasqmrylddatraklrelpTNDQILADAIKRSRVVLGetgqraisseidk 169
Cdd:COG4252  88 LLDKLAAAQPRAIGLDIYRDLPSS-------------------------PGDRALAAVLQRAPNLIG------------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 170 elpftgVATVGEDgaerflfefPGLLRNVPVIEKVAAGRGLFSIKTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITG- 248
Cdd:COG4252 130 ------VEKLSGD---------PGIAVNPPPELPRQAQIGFSDLILDSDGKVRRLLLAATPGPEPKYSLALKLALQYLAs 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 249 -------TPTLLVRTDKTGVrgVRLKGVEIP---TDRNG-QLWVHY-ARQDPSIYVSAADVLDNTVPPAKIAGKLVLVGT 316
Cdd:COG4252 195 lgispkyPDPERLRLGKTTL--PRLLGNSGGyqgADAGGyQILLNYrSSSSDFRTVSLRDVLNGKVPAELIRGRIVLIGA 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 317 SAVGLNDIKTTPVSST----MPGVEIHAQVLESVLSGAVISQP---NYALGVELIAALVIGLL-VIIFTPNLGPVRLVLA 388
Cdd:COG4252 273 TAPSLNDYFATPYSSSlkelVPGVEIHANIVSQILSALLDGRPllpVWPDGAELLWIFAWSLLgGLLAWRLRSPLRLLLA 352
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 27383034 389 GAMFAAILVGVSWfFYAQYRYLIDFTYPLLSTTAIYLTLI 428
Cdd:COG4252 353 VGLALAGLLLISY-LLFLAGWWIPLIPPLLALVGSGIWST 391
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
472-659 9.90e-28

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 111.19  E-value: 9.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   472 REMTIMFSDVRGFTTISEsyKHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIMAFWNAPLDDAEHEVNACEAAIQ 551
Cdd:pfam00211   7 DNVTILFADIVGFTALSS--AHSPEEVVRLLNDLYTRFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQTIAEMALD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   552 MLERIDAVNKEREEeaadgghvyiPLNVGIGLNTGiGVVGNMGSDLKKNYSVLGDSVNLASRLEGQSKEYGFPIIVGSRT 631
Cdd:pfam00211  85 MLEAIKSVNIPSFE----------GLRVRVGIHTG-PVVAGVIGAKRPRYDVWGDTVNLASRMESTGVPGKIHVSEETYR 153
                         170       180
                  ....*....|....*....|....*...
gi 27383034   632 ALAAKDKFAILELDFIMVKGKTEPEVIY 659
Cdd:pfam00211 154 LLKTREGFEFTERGEVEVKGKGKMETYF 181
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
451-665 4.20e-28

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 113.40  E-value: 4.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 451 SPVLVEQLAQSPEKLVLGGEE--REMTIMFSDVRGFTTISESykHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAI 528
Cdd:COG2114  22 DLVLRLYLARVVGRLLARGGAgdRRVTLLFADIVGSTELSES--LGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGF 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 529 MAFWNAPLdDAEHEVnACEAAIQmLERIDAVNKEREEeaadgghvyiPLNVGIGLNTGIGVVGNMGSdlkknYSVLGDSV 608
Cdd:COG2114 100 LAVFGRPS-PLEDAV-ACALDLQ-LALRNPLARLRRE----------SLRVRIGIHTGEVVVGNTGG-----YTVVGSAV 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27383034 609 NLASRLEGQSKeyGFPIIVGSRTA-LAAKDKFAILELDFIMVKGKTEPEVIYAVAGRE 665
Cdd:COG2114 162 NQAARLESLAK--PGQVLLSEATYdLVRDLVDLFSGLGSHRLKGLARPVRVYQLCHRS 217
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
450-616 6.93e-22

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 94.25  E-value: 6.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    450 MSPVLVEQLAQSPEKLVLGGEEREMTIMFSDVRGFTTISESykHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIM 529
Cdd:smart00044  13 LLPASVAEQLKRGGSPVPAESYDNVTILFSDIVGFTSLCST--STPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    530 AFWNAPLDD-AEHEVNACEAAIQMLERIDAVNKEREEEaadgghvyiPLNVGIGLNTGIGVVGNMGSDLKKnYSVLGDSV 608
Cdd:smart00044  91 VASGLPEEAlVDHAELIADEALDMVEELKTVLVQHREE---------GLRVRIGIHTGPVVAGVVGIRMPR-YCLFGDTV 160

                   ....*...
gi 27383034    609 NLASRLEG 616
Cdd:smart00044 161 NLASRMES 168
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
473-661 3.86e-54

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636  Cd Length: 177  Bit Score: 184.70  E-value: 3.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 473 EMTIMFSDVRGFTTISEsyKHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIMAFWNAPLDDAEHEVNACEAAIQM 552
Cdd:cd07302   1 EVTVLFADIVGFTALSE--RLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 553 LERIDAVNKEREEEAadgghvyiPLNVGIGLNTGIGVVGNMGSDlKKNYSVLGDSVNLASRLEGQSKeyGFPIIVGSRTA 632
Cdd:cd07302  79 QEALAELNAEREGGP--------PLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATY 147
                       170       180       190
                ....*....|....*....|....*....|
gi 27383034 633 LAAKDK-FAILELDFIMVKGKTEPEVIYAV 661
Cdd:cd07302 148 ELLGDAgFEFEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
41-373 4.94e-84

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


Pssm-ID: 215016  Cd Length: 303  Bit Score: 270.78  E-value: 4.94e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034     41 QELRLRTFDMFQLIDPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIADLIQNLTSNGAVAIGFDVVFSEADRLNPDlva 120
Cdd:smart01080   1 QRLELRLYDARFRLRPRRAPDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDILFDEPDRDSPD--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    121 sqmrylddatraklrelptNDQILADAIKRSRVVLGetgqraisseidkeLPFTGVATVGEDGAERFLFEFPGLLRNVPV 200
Cdd:smart01080  78 -------------------GDAALAAALARAPNVVL--------------LAKLSREAGGGVLPSPPLPLPELPLPPLPG 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    201 IEKVAAGRGLFSIkTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITGTPTLLVRTDKTGVRGVRLKGVEIPTDRNGQLW 280
Cdd:smart01080 125 LADAAAGLGHVNE-PDADGVVRRVPLLLRYGGKAYPSLALELARVALGTPPLRLRLGGLGGPALTLGDGGYPGDRAGRLL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    281 VHY---ARQDPSIYVSAADVLDNTVP--PAKIAGKLVLVGTSAVGLNDIKTTPVSSTMPGVEIHAQVLESVLSGAVISQ- 354
Cdd:smart01080 204 IPFdgpGRGGTFPTVSAADVLDGEVPalPELLRGKIVLIGATAAGLGDLFPTPFSRVMPGVEIHANAIDNLLDGRFLRPa 283
                          330       340
                   ....*....|....*....|
gi 27383034    355 -PNYALGVELIAALVIGLLV 373
Cdd:smart01080 284 pPWWALLLLLLLWLLLGLLL 303
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
23-373 8.43e-83

CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE2 domains are not known at this time.


Pssm-ID: 253103  Cd Length: 305  Bit Score: 267.65  E-value: 8.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    23 LALLVVFAGARLWDPPPIQELRLRTFDMFQLI----DPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIADLIQNLTSNG 98
Cdd:pfam05226   1 LALLLLLLLALLSLRPLLQRLELALYDLLFRLrgprAPPPEPDPRIVIVAIDEASLAELGRWPWPRALLARLLDRLAAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    99 AVAIGFDVVFSEADRLNPDlvasqmrylddatraklrelptNDQILADAIKRS--RVVLGETGQRAISSEIDKELPftgv 176
Cdd:pfam05226  81 AKAIGLDILFDEPDRDSPA----------------------GDAALAAALARAgnPVVLGVFLEASEDGGGPLAPP---- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   177 atvgedgaerflfefpgllrnvPVIEKVAAGRGLFSIKTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITGTPTLLVRT 256
Cdd:pfam05226 135 ----------------------PALAAAAAGLGFVNVVPDSDGVVRRVPLLLRYGGRLYPSLALALARVALGAPPIRAEA 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   257 DKTGVrgvrlkGVEIPTDrNGQLWVHYARQDPSI-YVSAADVLDNTVPPAKIAGKLVLVGTSAVGLNDIKTTPVSSTMPG 335
Cdd:pfam05226 193 DAGGG------DRRIPTD-GGQLLLNFRGPAGTFpTVSAADVLEGRVPPELLRGKIVLIGATAAGLGDLFPTPFSGRMPG 265
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 27383034   336 VEIHAQVLESVLSGAVISQPN--YALGVELIAALVIGLLV 373
Cdd:pfam05226 266 VEIHANAISNLLSGRLLRPWPdwVELLLILLLALLLGLLL 305
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
10-428 5.55e-42

Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 226703  Cd Length: 400  Bit Score: 157.17  E-value: 5.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034  10 WFARKLGLARLMCLALLVVFAGARLWDPPPIQELRLRTFDMFQLIDPRHKTARPVTIVDIDDKSLARLGQWPWPRTRIAD 89
Cdd:COG4252   8 LLSRVWRLRVILLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLGQWPWPRAALAR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034  90 LIQNLTSNGAVAIGFDVVFSEADRlnpdlvasqmrylddatraklrelpTNDQILADAIKRSRVVLGetgqraisseidk 169
Cdd:COG4252  88 LLDKLAAAQPRAIGLDIYRDLPSS-------------------------PGDRALAAVLQRAPNLIG------------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 170 elpftgVATVGEDgaerflfefPGLLRNVPVIEKVAAGRGLFSIKTERDGLIRRVPMIMRAQGMVMPSLSLEILRVITG- 248
Cdd:COG4252 130 ------VEKLSGD---------PGIAVNPPPELPRQAQIGFSDLILDSDGKVRRLLLAATPGPEPKYSLALKLALQYLAs 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 249 -------TPTLLVRTDKTGVrgVRLKGVEIP---TDRNG-QLWVHY-ARQDPSIYVSAADVLDNTVPPAKIAGKLVLVGT 316
Cdd:COG4252 195 lgispkyPDPERLRLGKTTL--PRLLGNSGGyqgADAGGyQILLNYrSSSSDFRTVSLRDVLNGKVPAELIRGRIVLIGA 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 317 SAVGLNDIKTTPVSST----MPGVEIHAQVLESVLSGAVISQP---NYALGVELIAALVIGLL-VIIFTPNLGPVRLVLA 388
Cdd:COG4252 273 TAPSLNDYFATPYSSSlkelVPGVEIHANIVSQILSALLDGRPllpVWPDGAELLWIFAWSLLgGLLAWRLRSPLRLLLA 352
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 27383034 389 GAMFAAILVGVSWfFYAQYRYLIDFTYPLLSTTAIYLTLI 428
Cdd:COG4252 353 VGLALAGLLLISY-LLFLAGWWIPLIPPLLALVGSGIWST 391
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
472-659 9.90e-28

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 111.19  E-value: 9.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   472 REMTIMFSDVRGFTTISEsyKHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIMAFWNAPLDDAEHEVNACEAAIQ 551
Cdd:pfam00211   7 DNVTILFADIVGFTALSS--AHSPEEVVRLLNDLYTRFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQTIAEMALD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034   552 MLERIDAVNKEREEeaadgghvyiPLNVGIGLNTGiGVVGNMGSDLKKNYSVLGDSVNLASRLEGQSKEYGFPIIVGSRT 631
Cdd:pfam00211  85 MLEAIKSVNIPSFE----------GLRVRVGIHTG-PVVAGVIGAKRPRYDVWGDTVNLASRMESTGVPGKIHVSEETYR 153
                         170       180
                  ....*....|....*....|....*...
gi 27383034   632 ALAAKDKFAILELDFIMVKGKTEPEVIY 659
Cdd:pfam00211 154 LLKTREGFEFTERGEVEVKGKGKMETYF 181
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
473-619 5.08e-21

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: 90.49  E-value: 5.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 473 EMTIMFSDVRGFTTISESYKHdpQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIMAFWNaplddAEHEVNACEAAIQM 552
Cdd:cd07556   1 PVTILFADIVGFTSLADALGP--DEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDM 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27383034 553 LERIDAVNKEREEeaadgghvyiPLNVGIGLNTGIGVVGNMGSdlKKNYSVLGDSVNLASRLEGQSK 619
Cdd:cd07556  74 REAVSALNQSEGN----------PVRVRIGIHTGPVVVGVIGS--RPQYDVWGALVNLASRMESQAK 128
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
451-665 4.20e-28

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 113.40  E-value: 4.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 451 SPVLVEQLAQSPEKLVLGGEE--REMTIMFSDVRGFTTISESykHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAI 528
Cdd:COG2114  22 DLVLRLYLARVVGRLLARGGAgdRRVTLLFADIVGSTELSES--LGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGF 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034 529 MAFWNAPLdDAEHEVnACEAAIQmLERIDAVNKEREEeaadgghvyiPLNVGIGLNTGIGVVGNMGSdlkknYSVLGDSV 608
Cdd:COG2114 100 LAVFGRPS-PLEDAV-ACALDLQ-LALRNPLARLRRE----------SLRVRIGIHTGEVVVGNTGG-----YTVVGSAV 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27383034 609 NLASRLEGQSKeyGFPIIVGSRTA-LAAKDKFAILELDFIMVKGKTEPEVIYAVAGRE 665
Cdd:COG2114 162 NQAARLESLAK--PGQVLLSEATYdLVRDLVDLFSGLGSHRLKGLARPVRVYQLCHRS 217
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
450-616 6.93e-22

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 94.25  E-value: 6.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    450 MSPVLVEQLAQSPEKLVLGGEEREMTIMFSDVRGFTTISESykHDPQGLITLMNRFLTPLTDVIIDQKGYIDKYMGDAIM 529
Cdd:smart00044  13 LLPASVAEQLKRGGSPVPAESYDNVTILFSDIVGFTSLCST--STPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27383034    530 AFWNAPLDD-AEHEVNACEAAIQMLERIDAVNKEREEEaadgghvyiPLNVGIGLNTGIGVVGNMGSDLKKnYSVLGDSV 608
Cdd:smart00044  91 VASGLPEEAlVDHAELIADEALDMVEELKTVLVQHREE---------GLRVRIGIHTGPVVAGVVGIRMPR-YCLFGDTV 160

                   ....*...
gi 27383034    609 NLASRLEG 616
Cdd:smart00044 161 NLASRMES 168
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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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