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Conserved domains on  [gi|33864410|ref|NP_895970|]
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adenylate cyclase [Prochlorococcus marinus str. MIT 9313]

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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 ...
454-638 1.10e-44

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: 157.36  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 454 VSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRGESteAQSAICCA 533
Cdd:cd07302   2 VTVLFADIVGFTALSERLGPEELVEL----LNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDH--AERAVRAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 534 MAMRERLVHMNRLWQseGVEPLVNGIGIASGIVLAGGIGGRKLGGlSVIGDTVNLASRLEGLTRslDQSILFDQRTSELA 613
Cdd:cd07302  76 LEMQEALAELNAERE--GGPPLRLRIGIHTGPVVAGVVGSERPEY-TVIGDTVNLAARLESLAK--PGQILVSEATYELL 150
                       170       180
                ....*....|....*....|....*..
gi 33864410 614 GE-GFAIRSLGMQELKGI-GRLEVYSL 638
Cdd:cd07302 151 GDaGFEFEELGEVELKGKsGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
37-336 2.18e-23

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: 100.52  E-value: 2.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410     37 LERNLEGQLVRIRGPRLASPEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVVVLNV 116
Cdd:smart01080   3 LELRLYDARFRLRPRRAPDPDIVIVAIDEASLAA----------------LGRWPWPRSVLARLLDRLAAAGAKAIGFDI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    117 VFAGESVFGPADDKAFIAALEPHQQHLVLAAEMVEAEDQLGA---GAISLLRPDAVDAAELDKLSLGLSNLfPPEHGARF 193
Cdd:smart01080  67 LFDEPDRDSPDGDAALAAALARAPNVVLLAKLSREAGGGVLPsppLPLPELPLPPLPGLADAAAGLGHVNE-PDADGVVR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    194 LQPEFY----------ATTLEQPLGHEALHSLPVAALE------QAGRSLELDLDGQTLNFYGPEPepigmdgscstlGH 257
Cdd:smart01080 146 RVPLLLryggkaypslALELARVALGTPPLRLRLGGLGgpaltlGDGGYPGDRAGRLLIPFDGPGR------------GG 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    258 GFLRMSAKNVINPRQWAVhpcrervdgavvlvgvvvsggGSALSD---------------LPSPFGD-LSGMELLATSTG 321
Cdd:smart01080 214 TFPTVSAADVLDGEVPAL---------------------PELLRGkivligataaglgdlFPTPFSRvMPGVEIHANAID 272
                          330
                   ....*....|....*
gi 33864410    322 NALTGDGLRAWPQSL 336
Cdd:smart01080 273 NLLDGRFLRPAPPWW 287
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
396-641 4.20e-28

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


:

Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 112.63  E-value: 4.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 396 VALVVGALLYGGEAYRRMSIKRRLTRRWLERCVDPSVVGPMLsdpsdmealfdgQLKSVSVLFADLQGFTALTRQRSEqg 475
Cdd:COG2114   1 IAAVLNLLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGA------------GDRRVTLLFADIVGSTELSESLGD-- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 476 rvRVHLEQLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRGEsteaqsAICCAMAMRERLVhmnRLWQSEGVEPL 555
Cdd:COG2114  67 --EALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLED------AVACALDLQLALR---NPLARLRRESL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 556 VNGIGIASGIVLAggiggRKLGGLSVIGDTVNLASRLEGLTRslDQSILFDQRTSELAGEG-FAIRSLGMQELKGIGR-L 633
Cdd:COG2114 136 RVRIGIHTGEVVV-----GNTGGYTVVGSAVNQAARLESLAK--PGQVLLSEATYDLVRDLvDLFSGLGSHRLKGLARpV 208

                ....*...
gi 33864410 634 EVYSLSER 641
Cdd:COG2114 209 RVYQLCHR 216
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
454-638 1.10e-44

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: 157.36  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 454 VSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRGESteAQSAICCA 533
Cdd:cd07302   2 VTVLFADIVGFTALSERLGPEELVEL----LNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDH--AERAVRAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 534 MAMRERLVHMNRLWQseGVEPLVNGIGIASGIVLAGGIGGRKLGGlSVIGDTVNLASRLEGLTRslDQSILFDQRTSELA 613
Cdd:cd07302  76 LEMQEALAELNAERE--GGPPLRLRIGIHTGPVVAGVVGSERPEY-TVIGDTVNLAARLESLAK--PGQILVSEATYELL 150
                       170       180
                ....*....|....*....|....*..
gi 33864410 614 GE-GFAIRSLGMQELKGI-GRLEVYSL 638
Cdd:cd07302 151 GDaGFEFEELGEVELKGKsGPVRVYRL 177
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
453-638 1.03e-26

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 107.72  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   453 SVSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRgeSTEAQSAICC 532
Cdd:pfam00211   8 NVTILFADIVGFTALSSAHSPEEVVRL----LNDLYTRFDELLDEHGVYKVKTIGDAYMAASGLPEPS--PAHAQTIAEM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   533 AMAMRERLVHMNrlwqSEGVEPLVNGIGIASGIVLAGGIGGRKLGGlSVIGDTVNLASRLEGLTRSLDqsILFDQRTSEL 612
Cdd:pfam00211  82 ALDMLEAIKSVN----IPSFEGLRVRVGIHTGPVVAGVIGAKRPRY-DVWGDTVNLASRMESTGVPGK--IHVSEETYRL 154
                         170       180
                  ....*....|....*....|....*...
gi 33864410   613 --AGEGFAIRSLGMQELKGIGRLEVYSL 638
Cdd:pfam00211 155 lkTREGFEFTERGEVEVKGKGKMETYFL 182
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
37-336 2.18e-23

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: 100.52  E-value: 2.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410     37 LERNLEGQLVRIRGPRLASPEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVVVLNV 116
Cdd:smart01080   3 LELRLYDARFRLRPRRAPDPDIVIVAIDEASLAA----------------LGRWPWPRSVLARLLDRLAAAGAKAIGFDI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    117 VFAGESVFGPADDKAFIAALEPHQQHLVLAAEMVEAEDQLGA---GAISLLRPDAVDAAELDKLSLGLSNLfPPEHGARF 193
Cdd:smart01080  67 LFDEPDRDSPDGDAALAAALARAPNVVLLAKLSREAGGGVLPsppLPLPELPLPPLPGLADAAAGLGHVNE-PDADGVVR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    194 LQPEFY----------ATTLEQPLGHEALHSLPVAALE------QAGRSLELDLDGQTLNFYGPEPepigmdgscstlGH 257
Cdd:smart01080 146 RVPLLLryggkaypslALELARVALGTPPLRLRLGGLGgpaltlGDGGYPGDRAGRLLIPFDGPGR------------GG 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    258 GFLRMSAKNVINPRQWAVhpcrervdgavvlvgvvvsggGSALSD---------------LPSPFGD-LSGMELLATSTG 321
Cdd:smart01080 214 TFPTVSAADVLDGEVPAL---------------------PELLRGkivligataaglgdlFPTPFSRvMPGVEIHANAID 272
                          330
                   ....*....|....*
gi 33864410    322 NALTGDGLRAWPQSL 336
Cdd:smart01080 273 NLLDGRFLRPAPPWW 287
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
37-336 2.24e-22

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: 97.39  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    37 LERNLEGQLVRIRGPRLAS----PEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVV 112
Cdd:pfam05226  21 LELALYDLLFRLRGPRAPPpepdPRIVIVAIDEASLAE----------------LGRWPWPRALLARLLDRLAAAGAKAI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   113 VLNVVFAGESVFGPADDKAFIAALEPHQQHLVLAAEMVEAEDQLGAGAISLLRPDAvdaaeldKLSLGLSNLFPPEHGAR 192
Cdd:pfam05226  85 GLDILFDEPDRDSPAGDAALAAALARAGNPVVLGVFLEASEDGGGPLAPPPALAAA-------AAGLGFVNVVPDSDGVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   193 FLQPefyattLEQPLGHEALHSLPVAALEQAGRSLELDLDGQT---------------LNFYGPEpepigmdgscstlgH 257
Cdd:pfam05226 158 RRVP------LLLRYGGRLYPSLALALARVALGAPPIRAEADAgggdrriptdggqllLNFRGPA--------------G 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   258 GFLRMSAKNVIN---PRQW-----------AvhpcrervdgavvlvgvvvsgggSALSDL-PSPFG-DLSGMELLATSTG 321
Cdd:pfam05226 218 TFPTVSAADVLEgrvPPELlrgkivligatA-----------------------AGLGDLfPTPFSgRMPGVEIHANAIS 274
                         330
                  ....*....|....*
gi 33864410   322 NALTGDGLRAWPQSL 336
Cdd:pfam05226 275 NLLSGRLLRPWPDWV 289
COG4252 COG4252
Predicted transmembrane sensor domain [Signal transduction mechanisms]
37-229 1.24e-08

Predicted transmembrane sensor domain [Signal transduction mechanisms]


Pssm-ID: 226703  Cd Length: 400  Bit Score: 56.25  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410  37 LERNLEGQLVRIRGPRLASPEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVVVLNV 116
Cdd:COG4252  41 LELAAFDQLLRLRPSEPPDDRILIVAIDEQDLES----------------LGQWPWPRAALARLLDKLAAAQPRAIGLDI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 117 VFageSVFGPADDKAFIAALEphQQHLVLAAEMVeaedqLGAGAISLLRPDAVDAAEldklSLGLSNlFPPEHGARFLQP 196
Cdd:COG4252 105 YR---DLPSSPGDRALAAVLQ--RAPNLIGVEKL-----SGDPGIAVNPPPELPRQA----QIGFSD-LILDSDGKVRRL 169
                       170       180       190
                ....*....|....*....|....*....|...
gi 33864410 197 EFYATTLEQPLGHEALHsLPVAALEQAGRSLEL 229
Cdd:COG4252 170 LLAATPGPEPKYSLALK-LALQYLASLGISPKY 201
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
396-641 4.20e-28

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 112.63  E-value: 4.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 396 VALVVGALLYGGEAYRRMSIKRRLTRRWLERCVDPSVVGPMLsdpsdmealfdgQLKSVSVLFADLQGFTALTRQRSEqg 475
Cdd:COG2114   1 IAAVLNLLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGA------------GDRRVTLLFADIVGSTELSESLGD-- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 476 rvRVHLEQLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRGEsteaqsAICCAMAMRERLVhmnRLWQSEGVEPL 555
Cdd:COG2114  67 --EALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLED------AVACALDLQLALR---NPLARLRRESL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 556 VNGIGIASGIVLAggiggRKLGGLSVIGDTVNLASRLEGLTRslDQSILFDQRTSELAGEG-FAIRSLGMQELKGIGR-L 633
Cdd:COG2114 136 RVRIGIHTGEVVV-----GNTGGYTVVGSAVNQAARLESLAK--PGQVLLSEATYDLVRDLvDLFSGLGSHRLKGLARpV 208

                ....*...
gi 33864410 634 EVYSLSER 641
Cdd:COG2114 209 RVYQLCHR 216
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
453-596 1.37e-18

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: 84.23  E-value: 1.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    453 SVSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPdgrgESTEAQSAICC 532
Cdd:smart00044  36 NVTILFSDIVGFTSLCSTSTPEQVVNL----LNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLP----EEALVDHAELI 107
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33864410    533 AMAMRERLVHMNRLWQSEGVEPLVNGIGIASGIVLAgGIGGRKLGGLSVIGDTVNLASRLEGLT 596
Cdd:smart00044 108 ADEALDMVEELKTVLVQHREEGLRVRIGIHTGPVVA-GVVGIRMPRYCLFGDTVNLASRMESAG 170
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
454-638 1.10e-44

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: 157.36  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 454 VSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRGESteAQSAICCA 533
Cdd:cd07302   2 VTVLFADIVGFTALSERLGPEELVEL----LNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDH--AERAVRAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 534 MAMRERLVHMNRLWQseGVEPLVNGIGIASGIVLAGGIGGRKLGGlSVIGDTVNLASRLEGLTRslDQSILFDQRTSELA 613
Cdd:cd07302  76 LEMQEALAELNAERE--GGPPLRLRIGIHTGPVVAGVVGSERPEY-TVIGDTVNLAARLESLAK--PGQILVSEATYELL 150
                       170       180
                ....*....|....*....|....*..
gi 33864410 614 GE-GFAIRSLGMQELKGI-GRLEVYSL 638
Cdd:cd07302 151 GDaGFEFEELGEVELKGKsGPVRVYRL 177
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
453-638 1.03e-26

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 107.72  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   453 SVSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRgeSTEAQSAICC 532
Cdd:pfam00211   8 NVTILFADIVGFTALSSAHSPEEVVRL----LNDLYTRFDELLDEHGVYKVKTIGDAYMAASGLPEPS--PAHAQTIAEM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   533 AMAMRERLVHMNrlwqSEGVEPLVNGIGIASGIVLAGGIGGRKLGGlSVIGDTVNLASRLEGLTRSLDqsILFDQRTSEL 612
Cdd:pfam00211  82 ALDMLEAIKSVN----IPSFEGLRVRVGIHTGPVVAGVIGAKRPRY-DVWGDTVNLASRMESTGVPGK--IHVSEETYRL 154
                         170       180
                  ....*....|....*....|....*...
gi 33864410   613 --AGEGFAIRSLGMQELKGIGRLEVYSL 638
Cdd:pfam00211 155 lkTREGFEFTERGEVEVKGKGKMETYFL 182
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
37-336 2.18e-23

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: 100.52  E-value: 2.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410     37 LERNLEGQLVRIRGPRLASPEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVVVLNV 116
Cdd:smart01080   3 LELRLYDARFRLRPRRAPDPDIVIVAIDEASLAA----------------LGRWPWPRSVLARLLDRLAAAGAKAIGFDI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    117 VFAGESVFGPADDKAFIAALEPHQQHLVLAAEMVEAEDQLGA---GAISLLRPDAVDAAELDKLSLGLSNLfPPEHGARF 193
Cdd:smart01080  67 LFDEPDRDSPDGDAALAAALARAPNVVLLAKLSREAGGGVLPsppLPLPELPLPPLPGLADAAAGLGHVNE-PDADGVVR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    194 LQPEFY----------ATTLEQPLGHEALHSLPVAALE------QAGRSLELDLDGQTLNFYGPEPepigmdgscstlGH 257
Cdd:smart01080 146 RVPLLLryggkaypslALELARVALGTPPLRLRLGGLGgpaltlGDGGYPGDRAGRLLIPFDGPGR------------GG 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    258 GFLRMSAKNVINPRQWAVhpcrervdgavvlvgvvvsggGSALSD---------------LPSPFGD-LSGMELLATSTG 321
Cdd:smart01080 214 TFPTVSAADVLDGEVPAL---------------------PELLRGkivligataaglgdlFPTPFSRvMPGVEIHANAID 272
                          330
                   ....*....|....*
gi 33864410    322 NALTGDGLRAWPQSL 336
Cdd:smart01080 273 NLLDGRFLRPAPPWW 287
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
37-336 2.24e-22

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: 97.39  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    37 LERNLEGQLVRIRGPRLAS----PEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVV 112
Cdd:pfam05226  21 LELALYDLLFRLRGPRAPPpepdPRIVIVAIDEASLAE----------------LGRWPWPRALLARLLDRLAAAGAKAI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   113 VLNVVFAGESVFGPADDKAFIAALEPHQQHLVLAAEMVEAEDQLGAGAISLLRPDAvdaaeldKLSLGLSNLFPPEHGAR 192
Cdd:pfam05226  85 GLDILFDEPDRDSPAGDAALAAALARAGNPVVLGVFLEASEDGGGPLAPPPALAAA-------AAGLGFVNVVPDSDGVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   193 FLQPefyattLEQPLGHEALHSLPVAALEQAGRSLELDLDGQT---------------LNFYGPEpepigmdgscstlgH 257
Cdd:pfam05226 158 RRVP------LLLRYGGRLYPSLALALARVALGAPPIRAEADAgggdrriptdggqllLNFRGPA--------------G 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410   258 GFLRMSAKNVIN---PRQW-----------AvhpcrervdgavvlvgvvvsgggSALSDL-PSPFG-DLSGMELLATSTG 321
Cdd:pfam05226 218 TFPTVSAADVLEgrvPPELlrgkivligatA-----------------------AGLGDLfPTPFSgRMPGVEIHANAIS 274
                         330
                  ....*....|....*
gi 33864410   322 NALTGDGLRAWPQSL 336
Cdd:pfam05226 275 NLLSGRLLRPWPDWV 289
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
454-597 1.52e-18

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: 82.79  E-value: 1.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 454 VSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLpdgrgesTEAQSAICCA 533
Cdd:cd07556   2 VTILFADIVGFTSLADALGPDEGDEL----LNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL-------DHPAAAVAFA 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33864410 534 MAMRErlvHMNRLWQSEGVePLVNGIGIASGIVLAGGIGGRKLGGlsVIGDTVNLASRLEGLTR 597
Cdd:cd07556  71 EDMRE---AVSALNQSEGN-PVRVRIGIHTGPVVVGVIGSRPQYD--VWGALVNLASRMESQAK 128
COG4252 COG4252
Predicted transmembrane sensor domain [Signal transduction mechanisms]
37-229 1.24e-08

Predicted transmembrane sensor domain [Signal transduction mechanisms]


Pssm-ID: 226703  Cd Length: 400  Bit Score: 56.25  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410  37 LERNLEGQLVRIRGPRLASPEIVQVVIDDATLAEglwfeqqeqipfwavgMGSLPWPRARYGDLLEPLIAAGADVVVLNV 116
Cdd:COG4252  41 LELAAFDQLLRLRPSEPPDDRILIVAIDEQDLES----------------LGQWPWPRAALARLLDKLAAAQPRAIGLDI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 117 VFageSVFGPADDKAFIAALEphQQHLVLAAEMVeaedqLGAGAISLLRPDAVDAAEldklSLGLSNlFPPEHGARFLQP 196
Cdd:COG4252 105 YR---DLPSSPGDRALAAVLQ--RAPNLIGVEKL-----SGDPGIAVNPPPELPRQA----QIGFSD-LILDSDGKVRRL 169
                       170       180       190
                ....*....|....*....|....*....|...
gi 33864410 197 EFYATTLEQPLGHEALHsLPVAALEQAGRSLEL 229
Cdd:COG4252 170 LLAATPGPEPKYSLALK-LALQYLASLGISPKY 201
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
396-641 4.20e-28

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 112.63  E-value: 4.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 396 VALVVGALLYGGEAYRRMSIKRRLTRRWLERCVDPSVVGPMLsdpsdmealfdgQLKSVSVLFADLQGFTALTRQRSEqg 475
Cdd:COG2114   1 IAAVLNLLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGA------------GDRRVTLLFADIVGSTELSESLGD-- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 476 rvRVHLEQLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPDGRGEsteaqsAICCAMAMRERLVhmnRLWQSEGVEPL 555
Cdd:COG2114  67 --EALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLED------AVACALDLQLALR---NPLARLRRESL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410 556 VNGIGIASGIVLAggiggRKLGGLSVIGDTVNLASRLEGLTRslDQSILFDQRTSELAGEG-FAIRSLGMQELKGIGR-L 633
Cdd:COG2114 136 RVRIGIHTGEVVV-----GNTGGYTVVGSAVNQAARLESLAK--PGQVLLSEATYDLVRDLvDLFSGLGSHRLKGLARpV 208

                ....*...
gi 33864410 634 EVYSLSER 641
Cdd:COG2114 209 RVYQLCHR 216
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
453-596 1.37e-18

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: 84.23  E-value: 1.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33864410    453 SVSVLFADLQGFTALTRQRSEQGRVRVhleqLNHYLDEMRSVVWDHHGFLDKFIGDAVMAVFGLPdgrgESTEAQSAICC 532
Cdd:smart00044  36 NVTILFSDIVGFTSLCSTSTPEQVVNL----LNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLP----EEALVDHAELI 107
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33864410    533 AMAMRERLVHMNRLWQSEGVEPLVNGIGIASGIVLAgGIGGRKLGGLSVIGDTVNLASRLEGLT 596
Cdd:smart00044 108 ADEALDMVEELKTVLVQHREEGLRVRIGIHTGPVVA-GVVGIRMPRYCLFGDTVNLASRMESAG 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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