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Conserved domains on  [gi|512048590|gb|EPD48247|]
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hypothetical protein HMPREF1206_00648 [Corynebacterium sp. HFH0082]

Protein Classification

adenylate/guanylate cyclase domain-containing protein( domain architecture ID 11450023)

adenylate/guanylate cyclase domain-containing protein may function as an adenylate cyclase, catalyzing the synthesis of 3',5'-cyclic AMP, or as a guanylate cyclase, catalyzing the synthesis of 3',5'-cyclic GMP

CATH:  3.30.70.1230
EC:  2.7.7.-|4.6.1.-
Gene Ontology:  GO:0016779|GO:0007165|GO:0046872|GO:0009975|GO:0009190|GO:0035556|GO:0016829|GO:0000166
PubMed:  9914257|16393782
SCOP:  4001316

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
80-488 5.42e-57

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 194.64  E-value: 5.42e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  80 DPRRVRYLVMRVPVYQALLGTVIWSLGVIVFSAVAFTYDSKIGMMVLITSVLGGAMVALLTYLIAERMVRPVAVEALARR 159
Cdd:COG2114    5 ALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 160 APDSSLEPPIGHRLRQTWVLTSGVPVVAILLVLIGQRRGLFTDDAADLLPTITALAILALITGYFGTMLATMSIVDPIRD 239
Cdd:COG2114   85 LAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 240 LTGAINKVRQGQVDTRVPIYdgsemgvlqagfnemmrgLQERQRVRDLFGRYVGSEVARKALE--EKPTLGGENRLVAVL 317
Cdd:COG2114  165 LLLLLLLLLLLALLLLLLLA------------------LRERERLRDLLGRYLPPEVAERLLAggEELRLGGERREVTVL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 318 FVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAARELREELLDL 397
Cdd:COG2114  227 FADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAEL 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 398 ----------QLTAGIGVSAGHVVAGHIGARDRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLAneDEQARWTT 467
Cdd:COG2114  307 naelpaeggpPLRVRIGIHTGEVVVGNIGSEDRLDYTVIGDTVNLAARLESLAK--PGEILVSEATYDLL--RDRFEFRE 382

                        410       420
                 ....*....|....*....|.
gi 512048590 468 LKSVELRGRTHMTQLARPVRP 488
Cdd:COG2114  383 LGEVRLKGKAEPVEVYELLGA 403
 
Name Accession Description Interval E-value
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
80-488 5.42e-57

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 194.64  E-value: 5.42e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  80 DPRRVRYLVMRVPVYQALLGTVIWSLGVIVFSAVAFTYDSKIGMMVLITSVLGGAMVALLTYLIAERMVRPVAVEALARR 159
Cdd:COG2114    5 ALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 160 APDSSLEPPIGHRLRQTWVLTSGVPVVAILLVLIGQRRGLFTDDAADLLPTITALAILALITGYFGTMLATMSIVDPIRD 239
Cdd:COG2114   85 LAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 240 LTGAINKVRQGQVDTRVPIYdgsemgvlqagfnemmrgLQERQRVRDLFGRYVGSEVARKALE--EKPTLGGENRLVAVL 317
Cdd:COG2114  165 LLLLLLLLLLLALLLLLLLA------------------LRERERLRDLLGRYLPPEVAERLLAggEELRLGGERREVTVL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 318 FVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAARELREELLDL 397
Cdd:COG2114  227 FADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAEL 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 398 ----------QLTAGIGVSAGHVVAGHIGARDRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLAneDEQARWTT 467
Cdd:COG2114  307 naelpaeggpPLRVRIGIHTGEVVVGNIGSEDRLDYTVIGDTVNLAARLESLAK--PGEILVSEATYDLL--RDRFEFRE 382

                        410       420
                 ....*....|....*....|.
gi 512048590 468 LKSVELRGRTHMTQLARPVRP 488
Cdd:COG2114  383 LGEVRLKGKAEPVEVYELLGA 403
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
 314-485 8.10e-47

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 [Multi-domain]  Cd Length: 177  Bit Score: 160.44  E-value: 8.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 314 VAVLFVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAARELREE 393
Cdd:cd07302    2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 394 LLDL--------QLTAGIGVSAGHVVAGHIGARdRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLAnEDEQARW 465
Cdd:cd07302   82 LAELnaereggpPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELL-GDAGFEF 157

                        170       180
                 ....*....|....*....|
gi 512048590 466 TTLKSVELRGRTHMTQLARP 485
Cdd:cd07302  158 EELGEVELKGKSGPVRVYRL 177
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
314-481 5.64e-24

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 98.85  E-value: 5.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  314 VAVLFVDVIGSTNFAEKNSPEVVVR---ELNAFFDHVVDcvhRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAAREL 390
Cdd:pfam00211   9 VTILFADIVGFTALSSRHSPEQVVRllnELYTRFDRLLD---KHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMALDM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  391 REEL--------LDLQLtaGIGVSAGHVVAGHIGARdRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLANEdEQ 462
Cdd:pfam00211  86 LEAIgevnvessEGLRV--RVGIHTGPVVAGVIGAR-MPRYDLWGNTVNLASRMESTGV--PGKIHVSEETYRLLKT-EG 159

                         170
                  ....*....|....*....
gi 512048590  463 ARWTTLKSVELRGRTHMTQ 481
Cdd:pfam00211 160 FEFTERGEIEVKGKGKMKT 178
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
 314-465 8.68e-20

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: 87.31  E-value: 8.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590   314 VAVLFVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGapLPLDDTAGHALTAARELRE- 392
Cdd:smart00044  37 VTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASG--LPEEALVDHAELIADEALDm 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590   393 ---------ELLDLQLTAGIGVSAGHVVAGHIGARdRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTI-RLANEDEQ 462
Cdd:smart00044 115 veelktvlvQHREEGLRVRIGIHTGPVVAGVVGIR-MPRYCLFGDTVNLASRMESAGD--PGQIQVSEETYsLLARRGGQ 191


                   ...
gi 512048590   463 ARW 465
Cdd:smart00044 192 FVF 194
 
Name Accession Description Interval E-value
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
80-488 5.42e-57

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 194.64  E-value: 5.42e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  80 DPRRVRYLVMRVPVYQALLGTVIWSLGVIVFSAVAFTYDSKIGMMVLITSVLGGAMVALLTYLIAERMVRPVAVEALARR 159
Cdd:COG2114    5 ALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 160 APDSSLEPPIGHRLRQTWVLTSGVPVVAILLVLIGQRRGLFTDDAADLLPTITALAILALITGYFGTMLATMSIVDPIRD 239
Cdd:COG2114   85 LAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 240 LTGAINKVRQGQVDTRVPIYdgsemgvlqagfnemmrgLQERQRVRDLFGRYVGSEVARKALE--EKPTLGGENRLVAVL 317
Cdd:COG2114  165 LLLLLLLLLLLALLLLLLLA------------------LRERERLRDLLGRYLPPEVAERLLAggEELRLGGERREVTVL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 318 FVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAARELREELLDL 397
Cdd:COG2114  227 FADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAEL 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 398 ----------QLTAGIGVSAGHVVAGHIGARDRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLAneDEQARWTT 467
Cdd:COG2114  307 naelpaeggpPLRVRIGIHTGEVVVGNIGSEDRLDYTVIGDTVNLAARLESLAK--PGEILVSEATYDLL--RDRFEFRE 382

                        410       420
                 ....*....|....*....|.
gi 512048590 468 LKSVELRGRTHMTQLARPVRP 488
Cdd:COG2114  383 LGEVRLKGKAEPVEVYELLGA 403
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
 314-485 8.10e-47

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 [Multi-domain]  Cd Length: 177  Bit Score: 160.44  E-value: 8.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 314 VAVLFVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAARELREE 393
Cdd:cd07302    2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 394 LLDL--------QLTAGIGVSAGHVVAGHIGARdRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLAnEDEQARW 465
Cdd:cd07302   82 LAELnaereggpPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELL-GDAGFEF 157

                        170       180
                 ....*....|....*....|
gi 512048590 466 TTLKSVELRGRTHMTQLARP 485
Cdd:cd07302  158 EELGEVELKGKSGPVRVYRL 177
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
314-481 5.64e-24

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 98.85  E-value: 5.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  314 VAVLFVDVIGSTNFAEKNSPEVVVR---ELNAFFDHVVDcvhRNKGIINKFQGDAALAVFGAPLPLDDTAGHALTAAREL 390
Cdd:pfam00211   9 VTILFADIVGFTALSSRHSPEQVVRllnELYTRFDRLLD---KHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMALDM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  391 REEL--------LDLQLtaGIGVSAGHVVAGHIGARdRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTIRLANEdEQ 462
Cdd:pfam00211  86 LEAIgevnvessEGLRV--RVGIHTGPVVAGVIGAR-MPRYDLWGNTVNLASRMESTGV--PGKIHVSEETYRLLKT-EG 159

                         170
                  ....*....|....*....
gi 512048590  463 ARWTTLKSVELRGRTHMTQ 481
Cdd:pfam00211 160 FEFTERGEIEVKGKGKMKT 178
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
 314-465 8.68e-20

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: 87.31  E-value: 8.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590   314 VAVLFVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGapLPLDDTAGHALTAARELRE- 392
Cdd:smart00044  37 VTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASG--LPEEALVDHAELIADEALDm 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590   393 ---------ELLDLQLTAGIGVSAGHVVAGHIGARdRFEYTVIGDAVNQAARLTELAKdtPGRVLATASTI-RLANEDEQ 462
Cdd:smart00044 115 veelktvlvQHREEGLRVRIGIHTGPVVAGVVGIR-MPRYCLFGDTVNLASRMESAGD--PGQIQVSEETYsLLARRGGQ 191


                   ...
gi 512048590   463 ARW 465
Cdd:smart00044 192 FVF 194
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 313-448 1.98e-17

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 78.55  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 313 LVAVLFVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQGDAALAVFGAplpldDTAGHALTAARELRE 392
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL-----DHPAAAVAFAEDMRE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512048590 393 ELLDLQ------LTAGIGVSAGHVVAGHIGARDRfeYTVIGDAVNQAARLTELAKdtPGRVL 448
Cdd:cd07556   76 AVSALNqsegnpVRVRIGIHTGPVVVGVIGSRPQ--YDVWGALVNLASRMESQAK--AGQVL 133
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
232-283 2.74e-09

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 53.02  E-value: 2.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 512048590   232 SIVDPIRDLTGAINKVRQGQVDTRVPIYDGSEMGVLQAGFNEMMRGLQERQR 283
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 207-291 6.84e-08

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 54.58  E-value: 6.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 207 LLPTITALAILALITGYFGTMLATMSIVDPIRDLTGAINKVRQGQVDTRVPIYDGSEMGVLQAGFNEMMRGLQERQRVRD 286
Cdd:COG5000    7 FLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELE 86


                 ....*
gi 512048590 287 LFGRY 291
Cdd:COG5000   87 ERRRY 91
HAMP pfam00672
HAMP domain;
228-280 9.26e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 48.39  E-value: 9.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 512048590  228 LATMSIVDPIRDLTGAINKVRQGQVDTRVPIYDGSEMGVLQAGFNEMMRGLQE 280
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 236-278 1.22e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 47.82  E-value: 1.22e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 512048590 236 PIRDLTGAINKVRQGQVDTRVPIYDGSEMGVLQAGFNEMMRGL 278
Cdd:cd06225    3 PLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
62-280 4.33e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 52.33  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  62 TWILFKPLLKWQRHPEVHDPRRVRYLVMRVPVYQALLGTVIWSLGVIVFSAVAFTYDSKIGMMVLITSVLGGAMVALLTY 141
Cdd:COG2972   11 VLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLLLLLL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 142 LIAERMVRPVAVEALARRAPDSSLEPPIGHRLRQTWVLTSGVPVVAILLVLIGQRRGLFtDDAADLLPTITALAILALIT 221
Cdd:COG2972   91 LLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELF-RGLFSLRRLILLIILLLLLL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 512048590 222 GYFGTMLATMSIVDPIRDLTGAINKVRQGQVdTRVPIYDGSEMGVLQAGFNEMMRGLQE 280
Cdd:COG2972  170 ALLLSYLLSRSITRPIKRLKKAMKKVEKGDL-VRLEVSGNDEIGILARSFNEMVERIKE 227
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
136-478 1.28e-06

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 50.88  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 136 VALLTYLIAERMVRPVAVEALARRAPDSSLEPPIGHRLRQTWVLTSGVPVVAILLVLIGQRRGLFTDDAADLLPTITALA 215
Cdd:COG2770  139 ALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLA 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 216 ILALITGYFGTMLATMSIVDPIRDLTGAINKVRQGQVDTRVPIYDGSEMGVLQAGFNEMMRGLQER------------QR 283
Cdd:COG2770  219 LLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESieeaeeeeelaeAE 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 284 VRDLFGRYVGSEVARKALEEKPTLGGENRLVAVLFVDVIGSTNFAEKNSPEVVVRELNAFFDHVVDCVHRNKGIINKFQG 363
Cdd:COG2770  299 LARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLA 378

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 364 DAALAVFGAPLPLDDTAGHALTAARELREELLDLQLTAGIGVSAGHVVAGHIGARDRFEYTVIGDAVNQAARLTELAKDT 443
Cdd:COG2770  379 LEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLA 458

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 512048590 444 PGRVLATASTIRLANEDEQARWTTLKSVELRGRTH 478
Cdd:COG2770  459 ELEAEELVAAAEALLLLAALLLLAALGALELLLLE 493
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
38-280 4.14e-05

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 46.17  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  38 RLANGVIYALAGYLILAIIAGIGTTWILFKPLLKWQRHPEVHDPRRVRYLVMRVPVYQALLGTVIWSLGVIVFSAVAFTY 117
Cdd:COG0840   10 LLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 118 DSKIGMMVLITSVLGGAMVALLTYLIAERMVRPVAVEALARRAPDSSLEPPIGHRLRQTWVLTSGVPVVAILL-VLIGQR 196
Cdd:COG0840   90 LLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAAlAALLEA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 197 RGLFTDDAADLLPTITALAILALITGYFGTMLATMSIVDPIRDLTGAINKVRQGQVDTRVPIYDGSEMGVLQAGFNEMMR 276
Cdd:COG0840  170 AALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIE 249


                 ....
gi 512048590 277 GLQE 280
Cdd:COG0840  250 NLRE 253
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 95-283 1.99e-04

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 43.72  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590  95 QALLGTVIWSLGVIVFSAVAFTYDSKIGMMVLITSVLGGAMVALLTYLIAERMVRPVAVEALARRAPDSSLEPPIGHRLR 174
Cdd:COG3850    4 LLLLALALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512048590 175 QTWVLTSGVPVVAILLVLIGQRRGLFTDDAADLLPTITALAILALITGYFGTMLATMSIVDPIRDLTGAINKVRQGQVDT 254
Cdd:COG3850   84 LLLAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDA 163

                        170       180
                 ....*....|....*....|....*....
gi 512048590 255 RVPIYDGSEMGVLQAGFNEMMRGLQERQR 283
Cdd:COG3850  164 RVPVSGRDELGTLARAFNRMADELQELYA 192
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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