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Conserved domains on  [gi|42526444|ref|NP_971542|]
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adenylate/guanylate cyclase catalytic [Treponema denticola ATCC 35405]

Protein Classification

CHASE2 and CHD domain-containing protein (domain architecture ID 10660927)

protein containing domains CHASE2, and CHD

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 ...
675-857 3.98e-57

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: 195.49  E-value: 3.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 675 RITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQ 754
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 755 AEAELNKQLYDVGDIPMpiftRIGINTGEMVVGNMGTeKKMNYTIMGNDVNLAARLEGVNKkyGTWILASESTWNETNDA 834
Cdd:cd07302  81 ALAELNAEREGGPPLRL----RIGIHTGPVVAGVVGS-ERPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDA 153
                       170       180
                ....*....|....*....|....
gi 42526444 835 -FLGRRLDRVRVVGINTPVQLYNV 857
Cdd:cd07302 154 gFEFEELGEVELKGKSGPVRVYRL 177
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
43-395 1.16e-15

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: 78.57  E-value: 1.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444     43 IENQVYDAMLKLKPEIKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGKAAVFDIeylsagragannayve 122
Cdd:smart01080   3 LELRLYDARFRLRPRRAPDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDI---------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    123 helpkeytavrqefgeyikefsdavagkniplsevktigqdmsdYFksriDELSDSikqnvFRDNDAYMGAAVGFFENAF 202
Cdd:smart01080  67 --------------------------------------------LF----DEPDRD-----SPDGDAALAAALARAPNVV 93
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    203 LtinavniniggetkelkdFAYnnfLFTNVEDKTGLFKKETLANRKAANEEygmaptimPILQYARGAGFPNVViDEDGV 282
Cdd:smart01080  94 L------------------LAK---LSREAGGGVLPSPPLPLPELPLPPLP--------GLADAAAGLGHVNEP-DADGV 143
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    283 RRRISLLTEYEGRYIGQLVFTPILHILEpekiirsRRKLILKNAKDPSDLEKRKDLTIPLDEEGNLLINWLKkrfadteN 362
Cdd:smart01080 144 VRRVPLLLRYGGKAYPSLALELARVALG-------TPPLRLRLGGLGGPALTLGDGGYPGDRAGRLLIPFDG-------P 209
                          330       340       350
                   ....*....|....*....|....*....|...
gi 42526444    363 PENGSFKSLSvyaltYADIMEKNLISLLEAIKD 395
Cdd:smart01080 210 GRGGTFPTVS-----AADVLDGEVPALPELLRG 237
CHASE2 super family cl01732
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
522-643 5.31e-05

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.


The actual alignment was detected with superfamily member COG4252:

Pssm-ID: 321636  Cd Length: 400  Bit Score: 46.62  E-value: 5.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 522 VGTSDLGVNPFW---------KSYPNVGTHANIYNTIMNEDFI-RPL----PKWVSIILAFVIAIFTAFMMKKIERGFIK 587
Cdd:COG4252 270 IGATAPSLNDYFatpyssslkELVPGVEIHANIVSQILSALLDgRPLlpvwPDGAELLWIFAWSLLGGLLAWRLRSPLRL 349
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42526444 588 VLLGIVLLSLTLSIGILLFVFGKiylqlFLPVITVVISFIVILLLNFIFSEKEKGF 643
Cdd:COG4252 350 LLAVGLALAGLLLISYLLFLAGW-----WIPLIPPLLALVGSGIWSTLFLKQLRRE 400
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
675-857 3.98e-57

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: 195.49  E-value: 3.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 675 RITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQ 754
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 755 AEAELNKQLYDVGDIPMpiftRIGINTGEMVVGNMGTeKKMNYTIMGNDVNLAARLEGVNKkyGTWILASESTWNETNDA 834
Cdd:cd07302  81 ALAELNAEREGGPPLRL----RIGIHTGPVVAGVVGS-ERPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDA 153
                       170       180
                ....*....|....*....|....
gi 42526444 835 -FLGRRLDRVRVVGINTPVQLYNV 857
Cdd:cd07302 154 gFEFEELGEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
641-867 1.16e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025  Cd Length: 227  Bit Score: 139.98  E-value: 1.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 641 KGFLRKAFGV----YLSDDVVNEIIADPDKLTLGGEQKR---ITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLI 713
Cdd:COG2114   5 LNLLAKEAKVaaagLRSDLVLRLYLARVVGRLLARGGAGdrrVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 714 LQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQAEAELNKQLYDVgdipmpiftRIGINTGEMVVGNMGTek 793
Cdd:COG2114  85 ARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALRNPLARLRRESLRV---------RIGIHTGEVVVGNTGG-- 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42526444 794 kmnYTIMGNDVNLAARLEGVNKKYGtwILASESTWNE-TNDAFLGRRLDRVRVVGINTPVQLYNVMAVKSEAYAE 867
Cdd:COG2114 154 ---YTVVGSAVNQAARLESLAKPGQ--VLLSEATYDLvRDLVDLFSGLGSHRLKGLARPVRVYQLCHRSLRRNLE 223
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
675-847 6.00e-29

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 306677  Cd Length: 183  Bit Score: 116.19  E-value: 6.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   675 RITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQ 754
Cdd:pfam00211   8 NVTILFADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHARKIAEMALDMLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   755 AEAELNKQlyDVGDIPMpiftRIGINTGEMVVGNMGTeKKMNYTIMGNDVNLAARLEGVNKKYGtwILASESTW-NETND 833
Cdd:pfam00211  88 AIGSVNVD--SSEGLRV----RIGIHTGPVVAGVIGA-RRPRYDVWGDTVNVASRMESTGVPGK--IHVSESTYrLLKTE 158
                         170
                  ....*....|....
gi 42526444   834 AFLGRRLDRVRVVG 847
Cdd:pfam00211 159 GFEFTERGEVEVKG 172
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
676-837 2.72e-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  Cd Length: 194  Bit Score: 108.88  E-value: 2.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    676 ITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPM-DLPDHAYRACLAAIRMKQ 754
Cdd:smart00044  37 VTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEeALVDHAELIADEALDMVE 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    755 AEAELNKQlydVGDIPMPIftRIGINTGEMVVGNMGTEKKmNYTIMGNDVNLAARLEGVNKKyGTwILASESTWNETNDA 834
Cdd:smart00044 117 ELKTVLVQ---HREEGLRV--RIGIHTGPVVAGVVGIRMP-RYCLFGDTVNLASRMESAGDP-GQ-IQVSEETYSLLARR 188

                   ...
gi 42526444    835 FLG 837
Cdd:smart00044 189 GGQ 191
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
43-395 1.16e-15

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: 78.57  E-value: 1.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444     43 IENQVYDAMLKLKPEIKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGKAAVFDIeylsagragannayve 122
Cdd:smart01080   3 LELRLYDARFRLRPRRAPDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDI---------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    123 helpkeytavrqefgeyikefsdavagkniplsevktigqdmsdYFksriDELSDSikqnvFRDNDAYMGAAVGFFENAF 202
Cdd:smart01080  67 --------------------------------------------LF----DEPDRD-----SPDGDAALAAALARAPNVV 93
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    203 LtinavniniggetkelkdFAYnnfLFTNVEDKTGLFKKETLANRKAANEEygmaptimPILQYARGAGFPNVViDEDGV 282
Cdd:smart01080  94 L------------------LAK---LSREAGGGVLPSPPLPLPELPLPPLP--------GLADAAAGLGHVNEP-DADGV 143
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    283 RRRISLLTEYEGRYIGQLVFTPILHILEpekiirsRRKLILKNAKDPSDLEKRKDLTIPLDEEGNLLINWLKkrfadteN 362
Cdd:smart01080 144 VRRVPLLLRYGGKAYPSLALELARVALG-------TPPLRLRLGGLGGPALTLGDGGYPGDRAGRLLIPFDG-------P 209
                          330       340       350
                   ....*....|....*....|....*....|...
gi 42526444    363 PENGSFKSLSvyaltYADIMEKNLISLLEAIKD 395
Cdd:smart01080 210 GRGGTFPTVS-----AADVLDGEVPALPELLRG 237
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
21-106 7.32e-15

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


Pssm-ID: 226703  Cd Length: 400  Bit Score: 77.43  E-value: 7.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444  21 FIIAIVVFLIFTAFSFIKFGRNIENQVYDAMLKLKPEIKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGK 100
Cdd:COG4252  19 LLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLGQWPWPRAALARLLDKLAAAQPR 98

                ....*.
gi 42526444 101 AAVFDI 106
Cdd:COG4252  99 AIGLDI 104
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
23-106 2.68e-13

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: 310087  Cd Length: 234  Bit Score: 70.82  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    23 IAIVVFLIFTAFSFikfgRNIENQVYDAMLKLKPEiKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGKAA 102
Cdd:pfam05226   1 VALLALLLLRLLGL----LQLELKAYDLLFRLRRP-PPDEDIVIVAIDEASLQRLGRWPWPRAVLARLLDKLAAAGPRAI 75

                  ....
gi 42526444   103 VFDI 106
Cdd:pfam05226  76 GLDI 79
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
522-643 5.31e-05

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


Pssm-ID: 226703  Cd Length: 400  Bit Score: 46.62  E-value: 5.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 522 VGTSDLGVNPFW---------KSYPNVGTHANIYNTIMNEDFI-RPL----PKWVSIILAFVIAIFTAFMMKKIERGFIK 587
Cdd:COG4252 270 IGATAPSLNDYFatpyssslkELVPGVEIHANIVSQILSALLDgRPLlpvwPDGAELLWIFAWSLLGGLLAWRLRSPLRL 349
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42526444 588 VLLGIVLLSLTLSIGILLFVFGKiylqlFLPVITVVISFIVILLLNFIFSEKEKGF 643
Cdd:COG4252 350 LLAVGLALAGLLLISYLLFLAGW-----WIPLIPPLLALVGSGIWSTLFLKQLRRE 400
DUF2070 pfam09843
Predicted membrane protein (DUF2070); This is a family of Archaeal 7-TM proteins. There are 6 ...
554-653 3.84e-03

Predicted membrane protein (DUF2070); This is a family of Archaeal 7-TM proteins. There are 6 closely assembled TM-regions at the N-terminus followed by a long intracellular, from residues 220-590, highly conserved region, of unknown function, terminating with one more TM-region. The short 25 residue section between TMs 5 and 6 might lie on the outer surface of the membrane and be acting as a receptor (from TMHMM).


Pssm-ID: 313128  Cd Length: 559  Bit Score: 40.73  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   554 FIRPLPKW-VSIILAFVIAIFTAFMMKKIERGFIKVLLGI---VLLSLTLSIGILLFVFGKIYLQ--LFLPVITVVISFI 627
Cdd:pfam09843   7 YIFRLPSWkVSLLAIIVLALLIGVLAFLSLLDALLGILFFglpALISFLLTQPLLRILGGKFTSRrsLFLALLTLLFVVI 86
                          90       100
                  ....*....|....*....|....*.
gi 42526444   628 VILLLNFIFSEKEKGFLRKAFGVYLS 653
Cdd:pfam09843  87 ISLLGILISAFLGPLALVLALAFIFA 112
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
675-857 3.98e-57

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: 195.49  E-value: 3.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 675 RITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQ 754
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 755 AEAELNKQLYDVGDIPMpiftRIGINTGEMVVGNMGTeKKMNYTIMGNDVNLAARLEGVNKkyGTWILASESTWNETNDA 834
Cdd:cd07302  81 ALAELNAEREGGPPLRL----RIGIHTGPVVAGVVGS-ERPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDA 153
                       170       180
                ....*....|....*....|....
gi 42526444 835 -FLGRRLDRVRVVGINTPVQLYNV 857
Cdd:cd07302 154 gFEFEELGEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
641-867 1.16e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025  Cd Length: 227  Bit Score: 139.98  E-value: 1.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 641 KGFLRKAFGV----YLSDDVVNEIIADPDKLTLGGEQKR---ITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLI 713
Cdd:COG2114   5 LNLLAKEAKVaaagLRSDLVLRLYLARVVGRLLARGGAGdrrVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 714 LQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQAEAELNKQLYDVgdipmpiftRIGINTGEMVVGNMGTek 793
Cdd:COG2114  85 ARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALRNPLARLRRESLRV---------RIGIHTGEVVVGNTGG-- 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42526444 794 kmnYTIMGNDVNLAARLEGVNKKYGtwILASESTWNE-TNDAFLGRRLDRVRVVGINTPVQLYNVMAVKSEAYAE 867
Cdd:COG2114 154 ---YTVVGSAVNQAARLESLAKPGQ--VLLSEATYDLvRDLVDLFSGLGSHRLKGLARPVRVYQLCHRSLRRNLE 223
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
675-847 6.00e-29

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 306677  Cd Length: 183  Bit Score: 116.19  E-value: 6.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   675 RITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPMDLPDHAYRACLAAIRMKQ 754
Cdd:pfam00211   8 NVTILFADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHARKIAEMALDMLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   755 AEAELNKQlyDVGDIPMpiftRIGINTGEMVVGNMGTeKKMNYTIMGNDVNLAARLEGVNKKYGtwILASESTW-NETND 833
Cdd:pfam00211  88 AIGSVNVD--SSEGLRV----RIGIHTGPVVAGVIGA-RRPRYDVWGDTVNVASRMESTGVPGK--IHVSESTYrLLKTE 158
                         170
                  ....*....|....
gi 42526444   834 AFLGRRLDRVRVVG 847
Cdd:pfam00211 159 GFEFTERGEVEVKG 172
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
676-837 2.72e-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  Cd Length: 194  Bit Score: 108.88  E-value: 2.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    676 ITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGAPM-DLPDHAYRACLAAIRMKQ 754
Cdd:smart00044  37 VTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEeALVDHAELIADEALDMVE 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    755 AEAELNKQlydVGDIPMPIftRIGINTGEMVVGNMGTEKKmNYTIMGNDVNLAARLEGVNKKyGTwILASESTWNETNDA 834
Cdd:smart00044 117 ELKTVLVQ---HREEGLRV--RIGIHTGPVVAGVVGIRMP-RYCLFGDTVNLASRMESAGDP-GQ-IQVSEETYSLLARR 188

                   ...
gi 42526444    835 FLG 837
Cdd:smart00044 189 GGQ 191
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
676-815 5.42e-22

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: 94.73  E-value: 5.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 676 ITALFTDIKSFSTLSEKITPEHLVSVLNVYLTQMSDLILQEKGTIDKYIGDAIVSFFGapmdlPDHAYRACLAAIRMKQA 755
Cdd:cd07556   2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMREA 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 756 EAELNKQLYDvgdipmPIFTRIGINTGEMVVGNMGTEKKmnYTIMGNDVNLAARLEGVNK 815
Cdd:cd07556  77 VSALNQSEGN------PVRVRIGIHTGPVVVGVIGSRPQ--YDVWGALVNLASRMESQAK 128
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
43-395 1.16e-15

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: 78.57  E-value: 1.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444     43 IENQVYDAMLKLKPEIKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGKAAVFDIeylsagragannayve 122
Cdd:smart01080   3 LELRLYDARFRLRPRRAPDPDIVIVAIDEASLAALGRWPWPRSVLARLLDRLAAAGAKAIGFDI---------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    123 helpkeytavrqefgeyikefsdavagkniplsevktigqdmsdYFksriDELSDSikqnvFRDNDAYMGAAVGFFENAF 202
Cdd:smart01080  67 --------------------------------------------LF----DEPDRD-----SPDGDAALAAALARAPNVV 93
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    203 LtinavniniggetkelkdFAYnnfLFTNVEDKTGLFKKETLANRKAANEEygmaptimPILQYARGAGFPNVViDEDGV 282
Cdd:smart01080  94 L------------------LAK---LSREAGGGVLPSPPLPLPELPLPPLP--------GLADAAAGLGHVNEP-DADGV 143
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    283 RRRISLLTEYEGRYIGQLVFTPILHILEpekiirsRRKLILKNAKDPSDLEKRKDLTIPLDEEGNLLINWLKkrfadteN 362
Cdd:smart01080 144 VRRVPLLLRYGGKAYPSLALELARVALG-------TPPLRLRLGGLGGPALTLGDGGYPGDRAGRLLIPFDG-------P 209
                          330       340       350
                   ....*....|....*....|....*....|...
gi 42526444    363 PENGSFKSLSvyaltYADIMEKNLISLLEAIKD 395
Cdd:smart01080 210 GRGGTFPTVS-----AADVLDGEVPALPELLRG 237
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
21-106 7.32e-15

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


Pssm-ID: 226703  Cd Length: 400  Bit Score: 77.43  E-value: 7.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444  21 FIIAIVVFLIFTAFSFIKFGRNIENQVYDAMLKLKPEIKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGK 100
Cdd:COG4252  19 LLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLGQWPWPRAALARLLDKLAAAQPR 98

                ....*.
gi 42526444 101 AAVFDI 106
Cdd:COG4252  99 AIGLDI 104
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
23-106 2.68e-13

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: 310087  Cd Length: 234  Bit Score: 70.82  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444    23 IAIVVFLIFTAFSFikfgRNIENQVYDAMLKLKPEiKEKSEILLLNVDDFSIEQIGSWPWSRDVLADVLIRLKESGGKAA 102
Cdd:pfam05226   1 VALLALLLLRLLGL----LQLELKAYDLLFRLRRP-PPDEDIVIVAIDEASLQRLGRWPWPRAVLARLLDKLAAAGPRAI 75

                  ....
gi 42526444   103 VFDI 106
Cdd:pfam05226  76 GLDI 79
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
522-643 5.31e-05

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


Pssm-ID: 226703  Cd Length: 400  Bit Score: 46.62  E-value: 5.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 522 VGTSDLGVNPFW---------KSYPNVGTHANIYNTIMNEDFI-RPL----PKWVSIILAFVIAIFTAFMMKKIERGFIK 587
Cdd:COG4252 270 IGATAPSLNDYFatpyssslkELVPGVEIHANIVSQILSALLDgRPLlpvwPDGAELLWIFAWSLLGGLLAWRLRSPLRL 349
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42526444 588 VLLGIVLLSLTLSIGILLFVFGKiylqlFLPVITVVISFIVILLLNFIFSEKEKGF 643
Cdd:COG4252 350 LLAVGLALAGLLLISYLLFLAGW-----WIPLIPPLLALVGSGIWSTLFLKQLRRE 400
GtrA COG2246
Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid ...
558-637 1.61e-03

Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism];


Pssm-ID: 225155  Cd Length: 139  Bit Score: 39.60  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444 558 LPKWVSIILAFVIAIFTAFMM--------KKIERGFIKV-LLGIVLLSLTLSIGILLFVFGKIYLQLFLPVITV--VISF 626
Cdd:COG2246  40 VPYALANAIAYEAAIIFSFVLnrrwtfrdRSTSRLHEFLrRLVKFNVAVLLGLAVLLLVLYILTLGLLLVAYLIanLIGI 119
                        90
                ....*....|.
gi 42526444 627 IVILLLNFIFS 637
Cdd:COG2246 120 VAAFIINFLLS 130
DUF2070 pfam09843
Predicted membrane protein (DUF2070); This is a family of Archaeal 7-TM proteins. There are 6 ...
554-653 3.84e-03

Predicted membrane protein (DUF2070); This is a family of Archaeal 7-TM proteins. There are 6 closely assembled TM-regions at the N-terminus followed by a long intracellular, from residues 220-590, highly conserved region, of unknown function, terminating with one more TM-region. The short 25 residue section between TMs 5 and 6 might lie on the outer surface of the membrane and be acting as a receptor (from TMHMM).


Pssm-ID: 313128  Cd Length: 559  Bit Score: 40.73  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   554 FIRPLPKW-VSIILAFVIAIFTAFMMKKIERGFIKVLLGI---VLLSLTLSIGILLFVFGKIYLQ--LFLPVITVVISFI 627
Cdd:pfam09843   7 YIFRLPSWkVSLLAIIVLALLIGVLAFLSLLDALLGILFFglpALISFLLTQPLLRILGGKFTSRrsLFLALLTLLFVVI 86
                          90       100
                  ....*....|....*....|....*.
gi 42526444   628 VILLLNFIFSEKEKGFLRKAFGVYLS 653
Cdd:pfam09843  87 ISLLGILISAFLGPLALVLALAFIFA 112
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
516-575 5.70e-03

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: 310087  Cd Length: 234  Bit Score: 39.23  E-value: 5.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42526444   516 IIGYSGVGTSDLGVNPFWKSYPNVGTHANIYNTIMNEDF--------IRPLPKWVSIILAFVIAIFTA 575
Cdd:pfam05226 167 LIGATAPGLGDLFPTPFSQVMPGVEIHANALSQILDGSAvgrppwflIWVWPEWGELLWILLWLLLGL 234
DUF5058 pfam16481
Domain of unknown function (DUF5058); This family consists of uncharacterized proteins around ...
561-645 5.76e-03

Domain of unknown function (DUF5058); This family consists of uncharacterized proteins around 250 residues in length and is mainly found in various Firmicutes species. The function of this family is unknown.


Pssm-ID: 318641  Cd Length: 218  Bit Score: 39.06  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42526444   561 WVSIILAFVIAIFTAFMMKKIERGFIKVLLG----IVLLSLTLSIGILLFVFGKIYLQLFLPVITVVISFIVILLLNFIF 636
Cdd:pfam16481 118 WVMTLGGIGWLLFVLLFTKKLDKGREKMSSGdpkwGAIISTAAFLGLFSALIAGEIVKGSPPLAAVLVSALVMVLLLALA 197

                  ....*....
gi 42526444   637 SEKEKGFLR 645
Cdd:pfam16481 198 KKKKIKWLK 206
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
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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