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Conserved domains on  [gi|82946175|dbj|BAE51039|]
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Adenylate cyclase [Magnetospirillum magneticum AMB-1]

Protein Classification

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 ...
426-605 1.06e-59

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: 199.73  E-value: 1.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 426 EMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALGMVK 505
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 506 KMEELKDDFvaRGWKPIKVGIGLNTGIMNVGNMGSDfRMAYTVLGDAVNLGSRVESLTKqyGVNMMVTEYTQAAVPGLIS 585
Cdd:cd07302  81 ALAELNAER--EGGPPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDAGF 155
                       170       180
                ....*....|....*....|..
gi 82946175 586 --REIDLVRVKGKDTPVRLYEP 605
Cdd:cd07302 156 efEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
27-312 3.35e-44

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: 160.23  E-value: 3.35e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175     27 ALLEDQTLSFRHQLRLAYgdakklAVSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNLKALGAKVIAVDMLMDFPSSY 106
Cdd:smart01080   1 QRLELRLYDARFRLRPRR------APDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDILFDEPDRD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    107 NE--DPALAKALSDAGNTVLVAQGEFRDGK----FAKINYPTTLL-------DQASASAYTNIQSNSKLITslsrlRVFP 173
Cdd:smart01080  75 SPdgDAALAAALARAPNVVLLAKLSREAGGgvlpSPPLPLPELPLpplpglaDAAAGLGHVNEPDADGVVR-----RVPL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    174 EMTAEKGGWP-FAVKAAAMYLGVEPR------LDGTTLVLGELRVPLNHEHKLYIDFPPLPTGTRFLSqsagLSALEFLD 246
Cdd:smart01080 150 LLRYGGKAYPsLALELARVALGTPPLrlrlggLGGPALTLGDGGYPGDRAGRLLIPFDGPGRGGTFPT----VSAADVLD 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82946175    247 ISGLDERElaeleyWVKDKIVVLGDTSEVSHDWFDTPVGMVY-GVEIIADSISSILKGAPLRGAGPV 312
Cdd:smart01080 226 GEVPALPE------LLRGKIVLIGATAAGLGDLFPTPFSRVMpGVEIHANAIDNLLDGRFLRPAPPW 286
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
425-619 8.20e-35

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 131.89  E-value: 8.20e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 425 REMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALGMV 504
Cdd:COG2114  45 RRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 505 KKMEELKDdfvargwKPIKVGIGLNTGIMNVGNMGSdfrmaYTVLGDAVNLGSRVESLTKQYGVnmMVTEYTQAAVPGLI 584
Cdd:COG2114 125 NPLARLRR-------ESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAKPGQV--LLSEATYDLVRDLV 190
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 82946175 585 SREIDL--VRVKGKDTPVRLYEPLGFEGEVDAETVAR 619
Cdd:COG2114 191 DLFSGLgsHRLKGLARPVRVYQLCHRSLRRNLELRTR 227
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
426-605 1.06e-59

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: 199.73  E-value: 1.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 426 EMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALGMVK 505
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 506 KMEELKDDFvaRGWKPIKVGIGLNTGIMNVGNMGSDfRMAYTVLGDAVNLGSRVESLTKqyGVNMMVTEYTQAAVPGLIS 585
Cdd:cd07302  81 ALAELNAER--EGGPPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDAGF 155
                       170       180
                ....*....|....*....|..
gi 82946175 586 --REIDLVRVKGKDTPVRLYEP 605
Cdd:cd07302 156 efEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
27-312 3.35e-44

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: 160.23  E-value: 3.35e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175     27 ALLEDQTLSFRHQLRLAYgdakklAVSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNLKALGAKVIAVDMLMDFPSSY 106
Cdd:smart01080   1 QRLELRLYDARFRLRPRR------APDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDILFDEPDRD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    107 NE--DPALAKALSDAGNTVLVAQGEFRDGK----FAKINYPTTLL-------DQASASAYTNIQSNSKLITslsrlRVFP 173
Cdd:smart01080  75 SPdgDAALAAALARAPNVVLLAKLSREAGGgvlpSPPLPLPELPLpplpglaDAAAGLGHVNEPDADGVVR-----RVPL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    174 EMTAEKGGWP-FAVKAAAMYLGVEPR------LDGTTLVLGELRVPLNHEHKLYIDFPPLPTGTRFLSqsagLSALEFLD 246
Cdd:smart01080 150 LLRYGGKAYPsLALELARVALGTPPLrlrlggLGGPALTLGDGGYPGDRAGRLLIPFDGPGRGGTFPT----VSAADVLD 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82946175    247 ISGLDERElaeleyWVKDKIVVLGDTSEVSHDWFDTPVGMVY-GVEIIADSISSILKGAPLRGAGPV 312
Cdd:smart01080 226 GEVPALPE------LLRGKIVLIGATAAGLGDLFPTPFSRVMpGVEIHANAIDNLLDGRFLRPAPPW 286
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
423-600 1.78e-31

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 278633  Cd Length: 183  Bit Score: 121.20  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175   423 ESREMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALG 502
Cdd:pfam00211   5 PYDNVTILFADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQKIAEMALD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175   503 MVKKMEElkddFVARGWKPIKVGIGLNTGIMNVGNMGSdfRMA-YTVLGDAVNLGSRVESLTKQYGVNMMVTEYTQAAVP 581
Cdd:pfam00211  85 MLEAIGS----VNVDSSEGLRVRIGIHTGPVVAGVIGA--RRPrYDVWGDTVNVASRMESTGVPGKIHVSEETYRLLKRE 158
                         170
                  ....*....|....*....
gi 82946175   582 GLISREIDLVRVKGKDTPV 600
Cdd:pfam00211 159 GFEFTERGEVEVKGKGKMK 177
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
7-318 6.30e-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: 283008  Cd Length: 234  Bit Score: 95.08  E-value: 6.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175     7 ILFTLILFLVAIPAQHFEWFALleDQTLSFRHQLRlaygdakklavSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNL 86
Cdd:pfam05226   1 VALLALLLLRLLGLLQLELKAY--DLLFRLRRPPP-----------DEDIVIVAIDEASLQRLGRWPWPRAVLARLLDKL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    87 KALGAKVIAVDMLMDFPSSYNE--DPALAKAlsdagntvlvaqgefrdgkfakinypttlldqasasaytniqsnsklit 164
Cdd:pfam05226  68 AAAGPRAIGLDILFDEPDRDVPpgDEALAQS------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175   165 slsrlrvfpemtaekggwpFAVKAAAMYLGVEPRLDGTTLVLgeLRVPLNHEHKLYIDFPPLPTGTRFLSqsaglsaleF 244
Cdd:pfam05226  99 -------------------LALALALLYLKAEISPELGKTVF--LRIPTDNDGGILLNYRGPPGTFPTVS---------A 148
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82946175   245 LDIsgLDERELAEleyWVKDKIVVLGDTSEVSHDWFDTPVG-MVYGVEIIADSISSILKGAPLRGAGPVMDSVAP 318
Cdd:pfam05226 149 ADV--LEGKVPPE---LFKDKIVLIGATAPGLGDLFPTPFSqVMPGVEIHANALSQILDGSAVGRPPWALIWVWP 218
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
10-385 1.81e-17

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


Pssm-ID: 226703  Cd Length: 400  Bit Score: 83.60  E-value: 1.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175  10 TLILFLVAIPaqhfeWFALLEDQTLSFRHQLRlaygdaKKLAVSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNLKAL 89
Cdd:COG4252  27 LLVLLLRLLG-----LLQLLELAAFDQLLRLR------PSEPPDDRILIVAIDEQDLESLGQWPWPRAALARLLDKLAAA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175  90 GAKVIAVDMLMDFPSSyNEDPALAKALSDAGNTVLVAQGEfrDGKFAKINYPTTLLDQAS-ASAYTNIQSNSKLitslsr 168
Cdd:COG4252  96 QPRAIGLDIYRDLPSS-PGDRALAAVLQRAPNLIGVEKLS--GDPGIAVNPPPELPRQAQiGFSDLILDSDGKV------ 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 169 LRVFPEMTAEKG-GWPFAVKAAAMYLGVE------PRLDGTTLVLGELRVPLNHEHK-LYIDFPPLPTGTRFLSQSAGLS 240
Cdd:COG4252 167 RRLLLAATPGPEpKYSLALKLALQYLASLgispkyPDPERLRLGKTTLPRLLGNSGGyQGADAGGYQILLNYRSSSSDFR 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 241 ALEFLDIsgLDERELAEleyWVKDKIVVLGDTSEVSHDWFDTPV-----GMVYGVEIIADSISSILKGA----PLRGAGP 311
Cdd:COG4252 247 TVSLRDV--LNGKVPAE---LIRGRIVLIGATAPSLNDYFATPYssslkELVPGVEIHANIVSQILSALldgrPLLPVWP 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82946175 312 VMDSVAPVVLLLAMLLLSLYLTRPLLRGMFVVALGVGFIVSASALYVHLGVVISMSYGVLALVLS-----YLLVEFRQY 385
Cdd:COG4252 322 DGAELLWIFAWSLLGGLLAWRLRSPLRLLLAVGLALAGLLLISYLLFLAGWWIPLIPPLLALVGSgiwstLFLKQLRRE 400
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
425-619 8.20e-35

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 131.89  E-value: 8.20e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 425 REMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALGMV 504
Cdd:COG2114  45 RRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 505 KKMEELKDdfvargwKPIKVGIGLNTGIMNVGNMGSdfrmaYTVLGDAVNLGSRVESLTKQYGVnmMVTEYTQAAVPGLI 584
Cdd:COG2114 125 NPLARLRR-------ESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAKPGQV--LLSEATYDLVRDLV 190
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 82946175 585 SREIDL--VRVKGKDTPVRLYEPLGFEGEVDAETVAR 619
Cdd:COG2114 191 DLFSGLgsHRLKGLARPVRVYQLCHRSLRRNLELRTR 227
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
405-579 1.64e-26

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: 107.73  E-value: 1.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    405 PELVAEMNKTGQQVTVGGESREMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWG 484
Cdd:smart00044  15 PASVAEQLKRGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    485 APLHD-PDHARHAVQAALGMVKKMEELKddfVARGWKPIKVGIGLNTGIMNVGNMGSDFRMaYTVLGDAVNLGSRVESLT 563
Cdd:smart00044  95 LPEEAlVDHAELIADEALDMVEELKTVL---VQHREEGLRVRIGIHTGPVVAGVVGIRMPR-YCLFGDTVNLASRMESAG 170
                          170
                   ....*....|....*.
gi 82946175    564 KQYGVNmmVTEYTQAA 579
Cdd:smart00044 171 DPGQIQ--VSEETYSL 184
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
422-531 4.83e-03

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 38.67  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    422 GESREMTVLFSDVrgftTISEGLAP--------QQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHA 493
Cdd:TIGR03903  282 GERRQLTALCCHV----GLSTPPEPaegveeddEELDLLLRSWLTRCADIAVRYGAHVGGVLGDTLLFYFGYPSAAERDA 357
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 82946175    494 RHAVQAALGMVKKMEELKDDFVARGWKPIKVGIGLNTG 531
Cdd:TIGR03903  358 RRAARAALEMVRQAGRKGEAAAGEGKWRVEIAAGIHTG 395
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
426-605 1.06e-59

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: 199.73  E-value: 1.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 426 EMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALGMVK 505
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 506 KMEELKDDFvaRGWKPIKVGIGLNTGIMNVGNMGSDfRMAYTVLGDAVNLGSRVESLTKqyGVNMMVTEYTQAAVPGLIS 585
Cdd:cd07302  81 ALAELNAER--EGGPPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDAGF 155
                       170       180
                ....*....|....*....|..
gi 82946175 586 --REIDLVRVKGKDTPVRLYEP 605
Cdd:cd07302 156 efEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
27-312 3.35e-44

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: 160.23  E-value: 3.35e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175     27 ALLEDQTLSFRHQLRLAYgdakklAVSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNLKALGAKVIAVDMLMDFPSSY 106
Cdd:smart01080   1 QRLELRLYDARFRLRPRR------APDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDILFDEPDRD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    107 NE--DPALAKALSDAGNTVLVAQGEFRDGK----FAKINYPTTLL-------DQASASAYTNIQSNSKLITslsrlRVFP 173
Cdd:smart01080  75 SPdgDAALAAALARAPNVVLLAKLSREAGGgvlpSPPLPLPELPLpplpglaDAAAGLGHVNEPDADGVVR-----RVPL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    174 EMTAEKGGWP-FAVKAAAMYLGVEPR------LDGTTLVLGELRVPLNHEHKLYIDFPPLPTGTRFLSqsagLSALEFLD 246
Cdd:smart01080 150 LLRYGGKAYPsLALELARVALGTPPLrlrlggLGGPALTLGDGGYPGDRAGRLLIPFDGPGRGGTFPT----VSAADVLD 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82946175    247 ISGLDERElaeleyWVKDKIVVLGDTSEVSHDWFDTPVGMVY-GVEIIADSISSILKGAPLRGAGPV 312
Cdd:smart01080 226 GEVPALPE------LLRGKIVLIGATAAGLGDLFPTPFSRVMpGVEIHANAIDNLLDGRFLRPAPPW 286
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
423-600 1.78e-31

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 278633  Cd Length: 183  Bit Score: 121.20  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175   423 ESREMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALG 502
Cdd:pfam00211   5 PYDNVTILFADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQKIAEMALD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175   503 MVKKMEElkddFVARGWKPIKVGIGLNTGIMNVGNMGSdfRMA-YTVLGDAVNLGSRVESLTKQYGVNMMVTEYTQAAVP 581
Cdd:pfam00211  85 MLEAIGS----VNVDSSEGLRVRIGIHTGPVVAGVIGA--RRPrYDVWGDTVNVASRMESTGVPGKIHVSEETYRLLKRE 158
                         170
                  ....*....|....*....
gi 82946175   582 GLISREIDLVRVKGKDTPV 600
Cdd:pfam00211 159 GFEFTERGEVEVKGKGKMK 177
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
426-564 2.49e-24

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: 99.35  E-value: 2.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 426 EMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGaplhdPDHARHAVQAALGMVK 505
Cdd:cd07556   1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 82946175 506 KMEELKDDfvarGWKPIKVGIGLNTGIMNVGNMGSDFRmaYTVLGDAVNLGSRVESLTK 564
Cdd:cd07556  76 AVSALNQS----EGNPVRVRIGIHTGPVVVGVIGSRPQ--YDVWGALVNLASRMESQAK 128
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
7-318 6.30e-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: 283008  Cd Length: 234  Bit Score: 95.08  E-value: 6.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175     7 ILFTLILFLVAIPAQHFEWFALleDQTLSFRHQLRlaygdakklavSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNL 86
Cdd:pfam05226   1 VALLALLLLRLLGLLQLELKAY--DLLFRLRRPPP-----------DEDIVIVAIDEASLQRLGRWPWPRAVLARLLDKL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    87 KALGAKVIAVDMLMDFPSSYNE--DPALAKAlsdagntvlvaqgefrdgkfakinypttlldqasasaytniqsnsklit 164
Cdd:pfam05226  68 AAAGPRAIGLDILFDEPDRDVPpgDEALAQS------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175   165 slsrlrvfpemtaekggwpFAVKAAAMYLGVEPRLDGTTLVLgeLRVPLNHEHKLYIDFPPLPTGTRFLSqsaglsaleF 244
Cdd:pfam05226  99 -------------------LALALALLYLKAEISPELGKTVF--LRIPTDNDGGILLNYRGPPGTFPTVS---------A 148
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82946175   245 LDIsgLDERELAEleyWVKDKIVVLGDTSEVSHDWFDTPVG-MVYGVEIIADSISSILKGAPLRGAGPVMDSVAP 318
Cdd:pfam05226 149 ADV--LEGKVPPE---LFKDKIVLIGATAPGLGDLFPTPFSqVMPGVEIHANALSQILDGSAVGRPPWALIWVWP 218
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
10-385 1.81e-17

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


Pssm-ID: 226703  Cd Length: 400  Bit Score: 83.60  E-value: 1.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175  10 TLILFLVAIPaqhfeWFALLEDQTLSFRHQLRlaygdaKKLAVSPEVVVVNTDEAFFKAYKSFPLRRTDIGTMVTNLKAL 89
Cdd:COG4252  27 LLVLLLRLLG-----LLQLLELAAFDQLLRLR------PSEPPDDRILIVAIDEQDLESLGQWPWPRAALARLLDKLAAA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175  90 GAKVIAVDMLMDFPSSyNEDPALAKALSDAGNTVLVAQGEfrDGKFAKINYPTTLLDQAS-ASAYTNIQSNSKLitslsr 168
Cdd:COG4252  96 QPRAIGLDIYRDLPSS-PGDRALAAVLQRAPNLIGVEKLS--GDPGIAVNPPPELPRQAQiGFSDLILDSDGKV------ 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 169 LRVFPEMTAEKG-GWPFAVKAAAMYLGVE------PRLDGTTLVLGELRVPLNHEHK-LYIDFPPLPTGTRFLSQSAGLS 240
Cdd:COG4252 167 RRLLLAATPGPEpKYSLALKLALQYLASLgispkyPDPERLRLGKTTLPRLLGNSGGyQGADAGGYQILLNYRSSSSDFR 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 241 ALEFLDIsgLDERELAEleyWVKDKIVVLGDTSEVSHDWFDTPV-----GMVYGVEIIADSISSILKGA----PLRGAGP 311
Cdd:COG4252 247 TVSLRDV--LNGKVPAE---LIRGRIVLIGATAPSLNDYFATPYssslkELVPGVEIHANIVSQILSALldgrPLLPVWP 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82946175 312 VMDSVAPVVLLLAMLLLSLYLTRPLLRGMFVVALGVGFIVSASALYVHLGVVISMSYGVLALVLS-----YLLVEFRQY 385
Cdd:COG4252 322 DGAELLWIFAWSLLGGLLAWRLRSPLRLLLAVGLALAGLLLISYLLFLAGWWIPLIPPLLALVGSgiwstLFLKQLRRE 400
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
425-619 8.20e-35

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 131.89  E-value: 8.20e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 425 REMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHARHAVQAALGMV 504
Cdd:COG2114  45 RRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175 505 KKMEELKDdfvargwKPIKVGIGLNTGIMNVGNMGSdfrmaYTVLGDAVNLGSRVESLTKQYGVnmMVTEYTQAAVPGLI 584
Cdd:COG2114 125 NPLARLRR-------ESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAKPGQV--LLSEATYDLVRDLV 190
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 82946175 585 SREIDL--VRVKGKDTPVRLYEPLGFEGEVDAETVAR 619
Cdd:COG2114 191 DLFSGLgsHRLKGLARPVRVYQLCHRSLRRNLELRTR 227
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
405-579 1.64e-26

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: 107.73  E-value: 1.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    405 PELVAEMNKTGQQVTVGGESREMTVLFSDVRGFTTISEGLAPQQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWG 484
Cdd:smart00044  15 PASVAEQLKRGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    485 APLHD-PDHARHAVQAALGMVKKMEELKddfVARGWKPIKVGIGLNTGIMNVGNMGSDFRMaYTVLGDAVNLGSRVESLT 563
Cdd:smart00044  95 LPEEAlVDHAELIADEALDMVEELKTVL---VQHREEGLRVRIGIHTGPVVAGVVGIRMPR-YCLFGDTVNLASRMESAG 170
                          170
                   ....*....|....*.
gi 82946175    564 KQYGVNmmVTEYTQAA 579
Cdd:smart00044 171 DPGQIQ--VSEETYSL 184
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
422-531 4.83e-03

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 38.67  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946175    422 GESREMTVLFSDVrgftTISEGLAP--------QQLTVLMNAFLSPMTHVIHDFRGTIDKYMGDAIMAFWGAPLHDPDHA 493
Cdd:TIGR03903  282 GERRQLTALCCHV----GLSTPPEPaegveeddEELDLLLRSWLTRCADIAVRYGAHVGGVLGDTLLFYFGYPSAAERDA 357
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 82946175    494 RHAVQAALGMVKKMEELKDDFVARGWKPIKVGIGLNTG 531
Cdd:TIGR03903  358 RRAARAALEMVRQAGRKGEAAAGEGKWRVEIAAGIHTG 395
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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