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Conserved domains on  [gi|1958649988|ref|XP_038947972|]
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adenylate cyclase type 2 isoform X4 [Rattus norvegicus]

Protein Classification

CHD and DUF1053 domain-containing protein( domain architecture ID 11069821)

protein containing domains AC_N, CHD, and DUF1053

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
285-469 6.64e-65

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 214.80  E-value: 6.64e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 285 LYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK 364
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 365 MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLN--GA 442
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKteGF 160
                         170       180
                  ....*....|....*....|....*..
gi 1958649988 443 YKVEEGDGEIRDPylkqHLVKTYFVIN 469
Cdd:pfam00211 161 EFTERGEIEVKGK----GKMKTYFLNG 183
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
54-474 2.71e-42

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 159.58  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  54 LLLIVMGACLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRVFSLVIWICLVAMGYLFMCFGG 133
Cdd:COG2114     1 AALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 134 TVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHTIVLSVYLSATPGAKEHLFWQILANVIIFICGNLAGAYHK 213
Cdd:COG2114    81 LGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 214 HLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPkagqmentnnfhnlyvkRHTNV 293
Cdd:COG2114   161 LLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGG-----------------ERREV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 294 SILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAI 373
Cdd:COG2114   224 TVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEAL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 374 KKV----RDATGVDINMRVGVHSGNVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEG 448
Cdd:COG2114   304 AELnaelPAEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFREL 383
                         410       420
                  ....*....|....*....|....*...
gi 1958649988 449 dGEIRdpyLK--QHLVKTYFVINPKGER 474
Cdd:COG2114   384 -GEVR---LKgkAEPVEVYELLGAKEAA 407
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
499-604 5.32e-42

Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity.


:

Pssm-ID: 461877  Cd Length: 98  Bit Score: 148.05  E-value: 5.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 499 TRYLESWGAAKPFAHLHHRDSMTTENGKIsttDVPMGQHNFQnrtLRTKSQKKRFEEELNERMIQAIDGINAQKQwlKSE 578
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRI---GLPLADHILQ---DRSASPVARLEEEIDEFIEQAIDGRSSDKL--RSE 72
                          90       100
                  ....*....|....*....|....*.
gi 1958649988 579 DIQRISLLFYNKNIEKEYRATALPAF 604
Cdd:pfam06327  73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
285-469 6.64e-65

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 214.80  E-value: 6.64e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 285 LYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK 364
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 365 MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLN--GA 442
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKteGF 160
                         170       180
                  ....*....|....*....|....*..
gi 1958649988 443 YKVEEGDGEIRDPylkqHLVKTYFVIN 469
Cdd:pfam00211 161 EFTERGEIEVKGK----GKMKTYFLNG 183
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
240-443 1.16e-59

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: 200.95  E-value: 1.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  240 EKRQQERLLLSLLPAHIAMEMKaeiiqrlqgpkagqmentNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHML 319
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  320 NELFGKFDQIAKENECMRIKILGDCYYCVSGLPIS-LPNHAKNCVKMGLDMCEAIKKVRD-ATGVDINMRVGVHSGNVLC 397
Cdd:smart00044  64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVqHREEGLRVRIGIHTGPVVA 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958649988  398 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAY 443
Cdd:smart00044 144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
292-467 3.04e-52

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: 179.70  E-value: 3.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 292 NVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCE 371
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 372 AIKKVRD--ATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGA-YKVEE- 447
Cdd:cd07302    81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEFEEl 160
                         170       180
                  ....*....|....*....|
gi 1958649988 448 GDGEIRDpylKQHLVKTYFV 467
Cdd:cd07302   161 GEVELKG---KSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
54-474 2.71e-42

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 159.58  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  54 LLLIVMGACLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRVFSLVIWICLVAMGYLFMCFGG 133
Cdd:COG2114     1 AALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 134 TVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHTIVLSVYLSATPGAKEHLFWQILANVIIFICGNLAGAYHK 213
Cdd:COG2114    81 LGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 214 HLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPkagqmentnnfhnlyvkRHTNV 293
Cdd:COG2114   161 LLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGG-----------------ERREV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 294 SILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAI 373
Cdd:COG2114   224 TVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEAL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 374 KKV----RDATGVDINMRVGVHSGNVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEG 448
Cdd:COG2114   304 AELnaelPAEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFREL 383
                         410       420
                  ....*....|....*....|....*...
gi 1958649988 449 dGEIRdpyLK--QHLVKTYFVINPKGER 474
Cdd:COG2114   384 -GEVR---LKgkAEPVEVYELLGAKEAA 407
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
499-604 5.32e-42

Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity.


Pssm-ID: 461877  Cd Length: 98  Bit Score: 148.05  E-value: 5.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 499 TRYLESWGAAKPFAHLHHRDSMTTENGKIsttDVPMGQHNFQnrtLRTKSQKKRFEEELNERMIQAIDGINAQKQwlKSE 578
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRI---GLPLADHILQ---DRSASPVARLEEEIDEFIEQAIDGRSSDKL--RSE 72
                          90       100
                  ....*....|....*....|....*.
gi 1958649988 579 DIQRISLLFYNKNIEKEYRATALPAF 604
Cdd:pfam06327  73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
37-264 3.70e-29

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


Pssm-ID: 318454  Cd Length: 415  Bit Score: 120.88  E-value: 3.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  37 LYESYYCMSQQHPLIVFLLLIVMgACLALLAvFFALGLEVEdhVAFLITVptALAIFFA-IFILVCIESVFKK---LLRV 112
Cdd:pfam16214 186 LYQRYFFRLNQSSLTMLMAVLVL-VCLVMLA-FHAARGPLQ--VPYVVVL--SLAIGLIlVLAVLCNRNAFHQdhmWLAC 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 113 FSLVIWICLV-AMGYLFMcfgGTVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHtivLSVYLSaTPGAKEHL 191
Cdd:pfam16214 260 YAVILVVLAVqVVGVLLV---QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIH---LAVSLR-TNAQDQFL 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958649988 192 FWQILANVIIFICGNLAGAYHKHLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEI 264
Cdd:pfam16214 333 LKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADI 405
MFS_YajR_like cd17472
Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux ...
50-169 9.99e-04

Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli inner membrane transport protein YajR and some uncharacterized multidrug-efflux transporters. YajR is a putative proton-driven major facilitator superfamily (MFS) transporter found in many gram-negative bacteria. Unlike most MFS transporters, YajR contains a C-terminal, cytosolic YAM domain, which may play an essential role for the proper functioning of the transporter. YajR-like transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341025 [Multi-domain]  Cd Length: 371  Bit Score: 42.20  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  50 LIVFLLLIVMgaclalLAVFFALGLEVEDHVA-----FLITVPTALAIFFAIFILVCIESVFKKLLRVFslVIWICLVAM 124
Cdd:cd17472   201 FSIFILHFVL------MAFFYILPLLLTQLGGgkgqlWKVYLPAILIGFILMVPFVIYAEKKGKMKQVF--VSSILLIAV 272
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958649988 125 GYLFMCFGGTvsawdqvSFFLFIIFVVYTMLPFNMRDAIIASILT 169
Cdd:cd17472   273 GFLLLLFAAT-------SLWLLIIGLIIFFIGFNLLEALLPSLVS 310
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
285-469 6.64e-65

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 214.80  E-value: 6.64e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 285 LYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK 364
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 365 MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLN--GA 442
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKteGF 160
                         170       180
                  ....*....|....*....|....*..
gi 1958649988 443 YKVEEGDGEIRDPylkqHLVKTYFVIN 469
Cdd:pfam00211 161 EFTERGEIEVKGK----GKMKTYFLNG 183
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
240-443 1.16e-59

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: 200.95  E-value: 1.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  240 EKRQQERLLLSLLPAHIAMEMKaeiiqrlqgpkagqmentNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHML 319
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  320 NELFGKFDQIAKENECMRIKILGDCYYCVSGLPIS-LPNHAKNCVKMGLDMCEAIKKVRD-ATGVDINMRVGVHSGNVLC 397
Cdd:smart00044  64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVqHREEGLRVRIGIHTGPVVA 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958649988  398 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAY 443
Cdd:smart00044 144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
292-467 3.04e-52

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: 179.70  E-value: 3.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 292 NVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCE 371
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 372 AIKKVRD--ATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGA-YKVEE- 447
Cdd:cd07302    81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEFEEl 160
                         170       180
                  ....*....|....*....|
gi 1958649988 448 GDGEIRDpylKQHLVKTYFV 467
Cdd:cd07302   161 GEVELKG---KSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
54-474 2.71e-42

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 159.58  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  54 LLLIVMGACLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRVFSLVIWICLVAMGYLFMCFGG 133
Cdd:COG2114     1 AALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 134 TVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHTIVLSVYLSATPGAKEHLFWQILANVIIFICGNLAGAYHK 213
Cdd:COG2114    81 LGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 214 HLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPkagqmentnnfhnlyvkRHTNV 293
Cdd:COG2114   161 LLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGG-----------------ERREV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 294 SILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAI 373
Cdd:COG2114   224 TVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEAL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 374 KKV----RDATGVDINMRVGVHSGNVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEG 448
Cdd:COG2114   304 AELnaelPAEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFREL 383
                         410       420
                  ....*....|....*....|....*...
gi 1958649988 449 dGEIRdpyLK--QHLVKTYFVINPKGER 474
Cdd:COG2114   384 -GEVR---LKgkAEPVEVYELLGAKEAA 407
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
499-604 5.32e-42

Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity.


Pssm-ID: 461877  Cd Length: 98  Bit Score: 148.05  E-value: 5.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 499 TRYLESWGAAKPFAHLHHRDSMTTENGKIsttDVPMGQHNFQnrtLRTKSQKKRFEEELNERMIQAIDGINAQKQwlKSE 578
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRI---GLPLADHILQ---DRSASPVARLEEEIDEFIEQAIDGRSSDKL--RSE 72
                          90       100
                  ....*....|....*....|....*.
gi 1958649988 579 DIQRISLLFYNKNIEKEYRATALPAF 604
Cdd:pfam06327  73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
292-430 1.20e-40

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: 145.58  E-value: 1.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 292 NVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGlpislPNHAKNCVKMGLDMCE 371
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649988 372 AIKKVRDATGVDINMRVGVHSGNVLCGVIGLqKWQYDVWSHDVTLANHMEAGGVPGRVH 430
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGS-RPQYDVWGALVNLASRMESQAKAGQVL 133
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
37-264 3.70e-29

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


Pssm-ID: 318454  Cd Length: 415  Bit Score: 120.88  E-value: 3.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  37 LYESYYCMSQQHPLIVFLLLIVMgACLALLAvFFALGLEVEdhVAFLITVptALAIFFA-IFILVCIESVFKK---LLRV 112
Cdd:pfam16214 186 LYQRYFFRLNQSSLTMLMAVLVL-VCLVMLA-FHAARGPLQ--VPYVVVL--SLAIGLIlVLAVLCNRNAFHQdhmWLAC 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988 113 FSLVIWICLV-AMGYLFMcfgGTVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHtivLSVYLSaTPGAKEHL 191
Cdd:pfam16214 260 YAVILVVLAVqVVGVLLV---QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIH---LAVSLR-TNAQDQFL 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958649988 192 FWQILANVIIFICGNLAGAYHKHLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEI 264
Cdd:pfam16214 333 LKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADI 405
MFS_YajR_like cd17472
Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux ...
50-169 9.99e-04

Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli inner membrane transport protein YajR and some uncharacterized multidrug-efflux transporters. YajR is a putative proton-driven major facilitator superfamily (MFS) transporter found in many gram-negative bacteria. Unlike most MFS transporters, YajR contains a C-terminal, cytosolic YAM domain, which may play an essential role for the proper functioning of the transporter. YajR-like transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341025 [Multi-domain]  Cd Length: 371  Bit Score: 42.20  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649988  50 LIVFLLLIVMgaclalLAVFFALGLEVEDHVA-----FLITVPTALAIFFAIFILVCIESVFKKLLRVFslVIWICLVAM 124
Cdd:cd17472   201 FSIFILHFVL------MAFFYILPLLLTQLGGgkgqlWKVYLPAILIGFILMVPFVIYAEKKGKMKQVF--VSSILLIAV 272
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958649988 125 GYLFMCFGGTvsawdqvSFFLFIIFVVYTMLPFNMRDAIIASILT 169
Cdd:cd17472   273 GFLLLLFAAT-------SLWLLIIGLIIFFIGFNLLEALLPSLVS 310
 
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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