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Conserved domains on  [gi|15964012|ref|NP_384365|]
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adenylate cyclase [Sinorhizobium meliloti 1021]

Protein Classification

HAMP and CHD domain-containing protein (domain architecture ID 11058936)

protein containing domains CTC1, Cache_1, HAMP, 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 ...
469-649 1.42e-58

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: 196.26  E-value: 1.42e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 469 EVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADTRHAEHACRCALAVEE 548
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 549 RLEAFNsaQRASGLPEFRTRFGIHTGTAVVGSVGAKeRLQYTAMGDTVNVASRLEGMNKdyGTSVLASGAVVAQCKDM-V 627
Cdd:cd07302  81 ALAELN--AEREGGPPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDAgF 155
                       170       180
                ....*....|....*....|..
gi 15964012 628 KFRPLGTAKAKGRSTALDIYEV 649
Cdd:cd07302 156 EFEELGEVELKGKSGPVRVYRL 177
Cache_1 super family cl24147
Cache domain;
221-287 5.48e-05

Cache domain;


The actual alignment was detected with superfamily member pfam02743:

Pssm-ID: 280839  Cd Length: 79  Bit Score: 41.90  E-value: 5.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15964012   221 PYEMATTGNLGMTISQAHRGNPQI--VIGADVVLDTITDFLSRERLTDDSVSFVLDAVGRPIIHSDSTM 287
Cdd:pfam02743   4 PYVDASTGDMVVTIAQPVKDDGDGlgVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLAHPNHKP 72
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
391-439 4.03e-04

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


:

Pssm-ID: 197640  Cd Length: 53  Bit Score: 38.77  E-value: 4.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 15964012    391 HLITKSLNQLTDSANRLQDLDFATPIDVSSHvAEISTLNGAMNRARDAI 439
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGR-DEIGELARAFNEMADRL 48
CTC1 super family cl24054
CST, telomere maintenance, complex subunit CTC1; CTC1 is one of the three components of the ...
76-150 6.98e-03

CST, telomere maintenance, complex subunit CTC1; CTC1 is one of the three components of the CST complex that assists Shelterin to protect the ends of telomeres from attack by DNA-repair mechanisms. Mutations in human CTC1 have been recognized as contributing to cerebroretinal microangiopathy.


The actual alignment was detected with superfamily member pfam15491:

Pssm-ID: 305211  Cd Length: 286  Bit Score: 37.39  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    76 RLVDRLGALSGDTSALVS--------LVASVANSFLVPPPERMndKVAVLREGIARSPHIDGVYVGYPSGAFFH--VVDL 145
Cdd:pfam15491 186 KLVGRLVSLSGLKKKLVSvgkkdsylMLVTTENTVVHWCPSYS--GRPPLDRSVVRGPGKCGSYTGVVTGIYMQgmLVEL 263

                  ....*
gi 15964012   146 DSAAW 150
Cdd:pfam15491 264 DETVW 268
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
460-663 1.41e-34

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 131.12  E-value: 1.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 460 FGGRAAWRQEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPvadtRHAEHA 539
Cdd:COG2114  37 LARGGAGDRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRP----SPLEDA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 540 CRCALAV-EERLEAFNSAQRasglPEFRTRFGIHTGTAVVGSVGAkerlqYTAMGDTVNVASRLEGMNKdyGTSVLASGA 618
Cdd:COG2114 113 VACALDLqLALRNPLARLRR----ESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAK--PGQVLLSEA 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15964012 619 VVAQCKD-MVKFRPLGTAKAKGRSTALDIYEVVGVVRAVNTTEAGT 663
Cdd:COG2114 182 TYDLVRDlVDLFSGLGSHRLKGLARPVRVYQLCHRSLRRNLELRTR 227
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
469-649 1.42e-58

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: 196.26  E-value: 1.42e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 469 EVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADTRHAEHACRCALAVEE 548
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 549 RLEAFNsaQRASGLPEFRTRFGIHTGTAVVGSVGAKeRLQYTAMGDTVNVASRLEGMNKdyGTSVLASGAVVAQCKDM-V 627
Cdd:cd07302  81 ALAELN--AEREGGPPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDAgF 155
                       170       180
                ....*....|....*....|..
gi 15964012 628 KFRPLGTAKAKGRSTALDIYEV 649
Cdd:cd07302 156 EFEELGEVELKGKSGPVRVYRL 177
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
468-647 4.16e-32

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 278633  Cd Length: 183  Bit Score: 123.12  E-value: 4.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012   468 QEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADTRHAEHACRCALAVE 547
Cdd:pfam00211   7 DNVTILFADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQKIAEMALDML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012   548 ERLEAFNsaqrASGLPEFRTRFGIHTGTAVVGSVGAKeRLQYTAMGDTVNVASRLEGMNKDYGtsVLASGAVVAQCKDM- 626
Cdd:pfam00211  87 EAIGSVN----VDSSEGLRVRIGIHTGPVVAGVIGAR-RPRYDVWGDTVNVASRMESTGVPGK--IHVSEETYRLLKREg 159
                         170       180
                  ....*....|....*....|.
gi 15964012   627 VKFRPLGTAKAKGRSTALDIY 647
Cdd:pfam00211 160 FEFTERGEVEVKGKGKMKTYF 180
Cache_1 pfam02743
Cache domain;
221-287 5.48e-05

Cache domain;


Pssm-ID: 280839  Cd Length: 79  Bit Score: 41.90  E-value: 5.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15964012   221 PYEMATTGNLGMTISQAHRGNPQI--VIGADVVLDTITDFLSRERLTDDSVSFVLDAVGRPIIHSDSTM 287
Cdd:pfam02743   4 PYVDASTGDMVVTIAQPVKDDGDGlgVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLAHPNHKP 72
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
391-439 4.03e-04

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 38.77  E-value: 4.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 15964012    391 HLITKSLNQLTDSANRLQDLDFATPIDVSSHvAEISTLNGAMNRARDAI 439
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGR-DEIGELARAFNEMADRL 48
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
393-439 2.50e-03

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 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: 100122  Cd Length: 48  Bit Score: 36.46  E-value: 2.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15964012 393 ITKSLNQLTDSANRLQDLDFATPIDVSSHvAEISTLNGAMNRARDAI 439
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGR-DEIGELARAFNQMAERL 46
CTC1_2 pfam15491
CST, telomere maintenance, complex subunit CTC1; CTC1 is one of the three components of the ...
76-150 6.98e-03

CST, telomere maintenance, complex subunit CTC1; CTC1 is one of the three components of the CST complex that assists Shelterin to protect the ends of telomeres from attack by DNA-repair mechanisms. This family largely represents sequences from plants species.


Pssm-ID: 292130  Cd Length: 286  Bit Score: 37.39  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    76 RLVDRLGALSGDTSALVS--------LVASVANSFLVPPPERMndKVAVLREGIARSPHIDGVYVGYPSGAFFH--VVDL 145
Cdd:pfam15491 186 KLVGRLVSLSGLKKKLVSvgkkdsylMLVTTENTVVHWCPSYS--GRPPLDRSVVRGPGKCGSYTGVVTGIYMQgmLVEL 263

                  ....*
gi 15964012   146 DSAAW 150
Cdd:pfam15491 264 DETVW 268
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
460-663 1.41e-34

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 131.12  E-value: 1.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 460 FGGRAAWRQEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPvadtRHAEHA 539
Cdd:COG2114  37 LARGGAGDRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRP----SPLEDA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 540 CRCALAV-EERLEAFNSAQRasglPEFRTRFGIHTGTAVVGSVGAkerlqYTAMGDTVNVASRLEGMNKdyGTSVLASGA 618
Cdd:COG2114 113 VACALDLqLALRNPLARLRR----ESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAK--PGQVLLSEA 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15964012 619 VVAQCKD-MVKFRPLGTAKAKGRSTALDIYEVVGVVRAVNTTEAGT 663
Cdd:COG2114 182 TYDLVRDlVDLFSGLGSHRLKGLARPVRVYQLCHRSLRRNLELRTR 227
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
461-607 1.10e-26

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 108.11  E-value: 1.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    461 GGRAAW---RQEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADT-RHA 536
Cdd:smart00044  25 GGSPVPaesYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEALvDHA 104
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15964012    537 EHACRCALAVeerLEAFNSAQRASGLPEFRTRFGIHTGTAVVGSVGAKERlQYTAMGDTVNVASRLEGMNK 607
Cdd:smart00044 105 ELIADEALDM---VEELKTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP-RYCLFGDTVNLASRMESAGD 171
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
447-651 2.80e-03

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 39.44  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    447 PKELVRKGIESGHFGGRAAWRQEVTAMFTDIYdftTISEGRSPEEVVAMlSEYFDLF--------SEVVAAHDGTIIQFH 518
Cdd:TIGR03903  264 REAIAAPLVASGTLDGETGERRQLTALCCHVG---LSTPPEPAEGVEED-DEELDLLlrswltrcADIAVRYGAHVGGVL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    519 GDSVFAMWNAPVADTRHAEHACRCALavEERLEAFNSAQRASGLPEFRTRF--GIHTGTAVVGSVGAkerlqytAMGDTV 596
Cdd:TIGR03903  340 GDTLLFYFGYPSAAERDARRAARAAL--EMVRQAGRKGEAAAGEGKWRVEIaaGIHTGLVLAQAPHA-------SGGTTP 410
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15964012    597 NVASRLEGMNKDYGtsVLASGAVVAQCKDMVKFRPLGTAKAKGRSTALDIYEVVG 651
Cdd:TIGR03903  411 NAAVRMQAQAEPGQ--ILVSEAARKLLRRHADFDPTALEEAAAGAESQPVFELLG 463
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
469-649 1.42e-58

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: 196.26  E-value: 1.42e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 469 EVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADTRHAEHACRCALAVEE 548
Cdd:cd07302   1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 549 RLEAFNsaQRASGLPEFRTRFGIHTGTAVVGSVGAKeRLQYTAMGDTVNVASRLEGMNKdyGTSVLASGAVVAQCKDM-V 627
Cdd:cd07302  81 ALAELN--AEREGGPPLRLRIGIHTGPVVAGVVGSE-RPEYTVIGDTVNLAARLESLAK--PGQILVSEATYELLGDAgF 155
                       170       180
                ....*....|....*....|..
gi 15964012 628 KFRPLGTAKAKGRSTALDIYEV 649
Cdd:cd07302 156 EFEELGEVELKGKSGPVRVYRL 177
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
468-647 4.16e-32

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 278633  Cd Length: 183  Bit Score: 123.12  E-value: 4.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012   468 QEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADTRHAEHACRCALAVE 547
Cdd:pfam00211   7 DNVTILFADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQKIAEMALDML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012   548 ERLEAFNsaqrASGLPEFRTRFGIHTGTAVVGSVGAKeRLQYTAMGDTVNVASRLEGMNKDYGtsVLASGAVVAQCKDM- 626
Cdd:pfam00211  87 EAIGSVN----VDSSEGLRVRIGIHTGPVVAGVIGAR-RPRYDVWGDTVNVASRMESTGVPGK--IHVSEETYRLLKREg 159
                         170       180
                  ....*....|....*....|.
gi 15964012   627 VKFRPLGTAKAKGRSTALDIY 647
Cdd:pfam00211 160 FEFTERGEVEVKGKGKMKTYF 180
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
469-604 2.54e-19

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: 85.10  E-value: 2.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 469 EVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPvadtrHAEHACRCALAVEE 548
Cdd:cd07556   1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLD-----HPAAAVAFAEDMRE 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15964012 549 RLEAFNsaqrASGLPEFRTRFGIHTGTAVVGSVGAkeRLQYTAMGDTVNVASRLEG 604
Cdd:cd07556  76 AVSALN----QSEGNPVRVRIGIHTGPVVVGVIGS--RPQYDVWGALVNLASRMES 125
Cache_1 pfam02743
Cache domain;
221-287 5.48e-05

Cache domain;


Pssm-ID: 280839  Cd Length: 79  Bit Score: 41.90  E-value: 5.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15964012   221 PYEMATTGNLGMTISQAHRGNPQI--VIGADVVLDTITDFLSRERLTDDSVSFVLDAVGRPIIHSDSTM 287
Cdd:pfam02743   4 PYVDASTGDMVVTIAQPVKDDGDGlgVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLAHPNHKP 72
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
391-439 4.03e-04

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 38.77  E-value: 4.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 15964012    391 HLITKSLNQLTDSANRLQDLDFATPIDVSSHvAEISTLNGAMNRARDAI 439
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGR-DEIGELARAFNEMADRL 48
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
393-439 2.50e-03

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 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: 100122  Cd Length: 48  Bit Score: 36.46  E-value: 2.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15964012 393 ITKSLNQLTDSANRLQDLDFATPIDVSSHvAEISTLNGAMNRARDAI 439
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGR-DEIGELARAFNQMAERL 46
CTC1_2 pfam15491
CST, telomere maintenance, complex subunit CTC1; CTC1 is one of the three components of the ...
76-150 6.98e-03

CST, telomere maintenance, complex subunit CTC1; CTC1 is one of the three components of the CST complex that assists Shelterin to protect the ends of telomeres from attack by DNA-repair mechanisms. This family largely represents sequences from plants species.


Pssm-ID: 292130  Cd Length: 286  Bit Score: 37.39  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    76 RLVDRLGALSGDTSALVS--------LVASVANSFLVPPPERMndKVAVLREGIARSPHIDGVYVGYPSGAFFH--VVDL 145
Cdd:pfam15491 186 KLVGRLVSLSGLKKKLVSvgkkdsylMLVTTENTVVHWCPSYS--GRPPLDRSVVRGPGKCGSYTGVVTGIYMQgmLVEL 263

                  ....*
gi 15964012   146 DSAAW 150
Cdd:pfam15491 264 DETVW 268
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
460-663 1.41e-34

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 131.12  E-value: 1.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 460 FGGRAAWRQEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPvadtRHAEHA 539
Cdd:COG2114  37 LARGGAGDRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRP----SPLEDA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012 540 CRCALAV-EERLEAFNSAQRasglPEFRTRFGIHTGTAVVGSVGAkerlqYTAMGDTVNVASRLEGMNKdyGTSVLASGA 618
Cdd:COG2114 113 VACALDLqLALRNPLARLRR----ESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAK--PGQVLLSEA 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15964012 619 VVAQCKD-MVKFRPLGTAKAKGRSTALDIYEVVGVVRAVNTTEAGT 663
Cdd:COG2114 182 TYDLVRDlVDLFSGLGSHRLKGLARPVRVYQLCHRSLRRNLELRTR 227
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
461-607 1.10e-26

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 108.11  E-value: 1.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    461 GGRAAW---RQEVTAMFTDIYDFTTISEGRSPEEVVAMLSEYFDLFSEVVAAHDGTIIQFHGDSVFAMWNAPVADT-RHA 536
Cdd:smart00044  25 GGSPVPaesYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEALvDHA 104
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15964012    537 EHACRCALAVeerLEAFNSAQRASGLPEFRTRFGIHTGTAVVGSVGAKERlQYTAMGDTVNVASRLEGMNK 607
Cdd:smart00044 105 ELIADEALDM---VEELKTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP-RYCLFGDTVNLASRMESAGD 171
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
447-651 2.80e-03

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 39.44  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    447 PKELVRKGIESGHFGGRAAWRQEVTAMFTDIYdftTISEGRSPEEVVAMlSEYFDLF--------SEVVAAHDGTIIQFH 518
Cdd:TIGR03903  264 REAIAAPLVASGTLDGETGERRQLTALCCHVG---LSTPPEPAEGVEED-DEELDLLlrswltrcADIAVRYGAHVGGVL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15964012    519 GDSVFAMWNAPVADTRHAEHACRCALavEERLEAFNSAQRASGLPEFRTRF--GIHTGTAVVGSVGAkerlqytAMGDTV 596
Cdd:TIGR03903  340 GDTLLFYFGYPSAAERDARRAARAAL--EMVRQAGRKGEAAAGEGKWRVEIaaGIHTGLVLAQAPHA-------SGGTTP 410
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15964012    597 NVASRLEGMNKDYGtsVLASGAVVAQCKDMVKFRPLGTAKAKGRSTALDIYEVVG 651
Cdd:TIGR03903  411 NAAVRMQAQAEPGQ--ILVSEAARKLLRRHADFDPTALEEAAAGAESQPVFELLG 463
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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