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Conserved domains on  [gi|1840721581|ref|WP_170399886|]
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adenylate/guanylate cyclase domain-containing protein [Ruegeria arenilitoris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
 7-168 7.19e-38

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: 137.71  E-value: 7.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   7 SILAADIVGFSRLVEAAEEATLARQ-KELRvSVFDPGVAQAGGKIIKSTGDGFLAEF-------SSVVEAVRFAIAAQEA 78
Cdd:cd07302     3 TVLFADIVGFTALSERLGPEELVELlNEYF-SAFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  79 VRAEEESVPQDRQISYRMGLHIGDVVVD-------DGDIYGDGVNLAARLEGAAPTGGICISAAVRDQiVGVMDELFGDV 151
Cdd:cd07302    82 LAELNAEREGGPPLRLRIGIHTGPVVAGvvgserpEYTVIGDTVNLAARLESLAKPGQILVSEATYEL-LGDAGFEFEEL 160

                         170
                  ....*....|....*..
gi 1840721581 152 GELTLKNISRPIRAFVW 168
Cdd:cd07302   161 GEVELKGKSGPVRVYRL 177
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-533 1.87e-13

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 70.91  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 304 ERAAETETNDPEAMLNLAGHYMmgsQPEEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAADAG 383
Cdd:COG2956    32 EEALELDPETVEAHLALGNLYR---RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKA----------GLLDRAEEL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 384 LSKAVSLNDQSDYVHLIRGIFhYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgsfSLAKN 463
Cdd:COG2956    99 LEKLLELDPDDAEALRLLAEI-YEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK---ALKLD 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 464 RIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG2956   175 PDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
FlgO super family cl41967
FlgO protein; This entry represents the FlgO protein. Mutation of this protein in Vibrio ...
 182-295 1.68e-07

FlgO protein; This entry represents the FlgO protein. Mutation of this protein in Vibrio cholerae has been shown to reduce motility. FlgO is an outer membrane protein that localizes throughout the membrane and not at the flagellar pole. Although FlgO and FlgP do not specifically localize to the flagellum, they are required for flagellar stability. Proteins in this family mostly contain an N-terminal lipoprotein attachment motif.


The actual alignment was detected with superfamily member COG5616:

Pssm-ID: 477887  Cd Length: 135  Bit Score: 50.27  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 182 PPIGGTSRKPTIAIAAFEALGNNDDAKMLAEACNHTVEAALANLTGVDLIA---------LDADPDHIA---------TA 243
Cdd:COG5616     2 SPAPAAPDRPSIAVLPFENLSGDPEQEYFADGLTEELITALSRLRGLRVIArtssfafkgRAVDLREIArelgvryvlEG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1840721581 244 VFQASGNQVRATLKLRETSTSATYLTQRMNGDISNPFVAEDLLSGEIATTIR 295
Cdd:COG5616    82 SVRRSGDRVRVTAQLIDAATGRHLWSERYDRDLDDLFALQDEIARAIAAALA 133
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
 7-168 7.19e-38

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: 137.71  E-value: 7.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   7 SILAADIVGFSRLVEAAEEATLARQ-KELRvSVFDPGVAQAGGKIIKSTGDGFLAEF-------SSVVEAVRFAIAAQEA 78
Cdd:cd07302     3 TVLFADIVGFTALSERLGPEELVELlNEYF-SAFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  79 VRAEEESVPQDRQISYRMGLHIGDVVVD-------DGDIYGDGVNLAARLEGAAPTGGICISAAVRDQiVGVMDELFGDV 151
Cdd:cd07302    82 LAELNAEREGGPPLRLRIGIHTGPVVAGvvgserpEYTVIGDTVNLAARLESLAKPGQILVSEATYEL-LGDAGFEFEEL 160

                         170
                  ....*....|....*..
gi 1840721581 152 GELTLKNISRPIRAFVW 168
Cdd:cd07302   161 GEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
1-175 7.17e-33

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 130.31  E-value: 7.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   1 MKRKLTSILAADIVGFSRLVEAAEEATLARQKELRVSVFDPGVAQAGGKIIKSTGDGFLAEFSSVVE-------AVRFAI 73
Cdd:COG2114   218 GERREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAredhaerAVRAAL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  74 AAQEAVRAEEESVPQ--DRQISYRMGLHIGDVVVD--------DGDIYGDGVNLAARLEGAAPTGGICISAAVRDQIVGv 143
Cdd:COG2114   298 AMQEALAELNAELPAegGPPLRVRIGIHTGEVVVGnigsedrlDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD- 376

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840721581 144 mDELFGDVGELTLKNISRPIRAFVWPPDQDGA 175
Cdd:COG2114   377 -RFEFRELGEVRLKGKAEPVEVYELLGAKEAA 407
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-533 1.87e-13

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 70.91  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 304 ERAAETETNDPEAMLNLAGHYMmgsQPEEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAADAG 383
Cdd:COG2956    32 EEALELDPETVEAHLALGNLYR---RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKA----------GLLDRAEEL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 384 LSKAVSLNDQSDYVHLIRGIFhYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgsfSLAKN 463
Cdd:COG2956    99 LEKLLELDPDDAEALRLLAEI-YEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK---ALKLD 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 464 RIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG2956   175 PDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
 7-138 1.19e-11

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: 63.82  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581    7 SILAADIVGFSRLVEAAE-EATLARQKELrVSVFDPGVAQAGGKIIKSTGDGFLAEFSSVVEAVrfaiaAQEAVRAEEES 85
Cdd:smart00044  38 TILFSDIVGFTSLCSTSTpEQVVNLLNDL-YSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAL-----VDHAELIADEA 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840721581   86 -----------VP-QDRQISYRMGLHIGDVVVD-DG------DIYGDGVNLAARLEGAAPTGGICISAAVRD 138
Cdd:smart00044 112 ldmveelktvlVQhREEGLRVRIGIHTGPVVAGvVGirmpryCLFGDTVNLASRMESAGDPGQIQVSEETYS 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
7-157 6.22e-11

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 61.49  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   7 SILAADIVGFSRLVEAAE-EATLARQKELrVSVFDPGVAQAGGKIIKSTGDGFLA-------EFSSVVEAVRFAIAAQEA 78
Cdd:pfam00211  10 TILFADIVGFTALSSRHSpEQVVRLLNEL-YTRFDRLLDKHKVYKVKTIGDAYMVvsglpepSPAHARKIAEMALDMLEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  79 vrAEEESVPQDRQISYRMGLHIGDVVVD-DG------DIYGDGVNLAARLEGAAPTGGICISAAVRDqIVGVMDELFGDV 151
Cdd:pfam00211  89 --IGEVNVESSEGLRVRVGIHTGPVVAGvIGarmpryDLWGNTVNLASRMESTGVPGKIHVSEETYR-LLKTEGFEFTER 165


                  ....*.
gi 1840721581 152 GELTLK 157
Cdd:pfam00211 166 GEIEVK 171
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 303-534 3.95e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 56.25  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 303 AERAAETETNDPEAMLnLAG--HYMMGSqpeeWEAAGRLLDRILTVQPRNFMAVGMKANTLIgelvwgyrpiRPEDIEAA 380
Cdd:TIGR02917 284 LQDALKSAPEYLPALL-LAGasEYQLGN----LEQAYQYLNQILKYAPNSHQARRLLASIQL----------RLGRVDEA 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 381 DAGLSKAVSLNDQSDYVHLIRGIFHYGiTGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGSfSL 460
Cdd:TIGR02917 349 IATLSPALGLDPDDPAALSLLGEAYLA-LGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAA-QL 426

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840721581 461 AKNRIyhRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:TIGR02917 427 DPELG--RADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDF 498
TolBN COG5616
TolB amino-terminal domain (function unknown) [Signal transduction mechanisms];
182-295 1.68e-07

TolB amino-terminal domain (function unknown) [Signal transduction mechanisms];


Pssm-ID: 444347  Cd Length: 135  Bit Score: 50.27  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 182 PPIGGTSRKPTIAIAAFEALGNNDDAKMLAEACNHTVEAALANLTGVDLIA---------LDADPDHIA---------TA 243
Cdd:COG5616     2 SPAPAAPDRPSIAVLPFENLSGDPEQEYFADGLTEELITALSRLRGLRVIArtssfafkgRAVDLREIArelgvryvlEG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1840721581 244 VFQASGNQVRATLKLRETSTSATYLTQRMNGDISNPFVAEDLLSGEIATTIR 295
Cdd:COG5616    82 SVRRSGDRVRVTAQLIDAATGRHLWSERYDRDLDDLFALQDEIARAIAAALA 133
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
 7-168 7.19e-38

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: 137.71  E-value: 7.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   7 SILAADIVGFSRLVEAAEEATLARQ-KELRvSVFDPGVAQAGGKIIKSTGDGFLAEF-------SSVVEAVRFAIAAQEA 78
Cdd:cd07302     3 TVLFADIVGFTALSERLGPEELVELlNEYF-SAFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  79 VRAEEESVPQDRQISYRMGLHIGDVVVD-------DGDIYGDGVNLAARLEGAAPTGGICISAAVRDQiVGVMDELFGDV 151
Cdd:cd07302    82 LAELNAEREGGPPLRLRIGIHTGPVVAGvvgserpEYTVIGDTVNLAARLESLAKPGQILVSEATYEL-LGDAGFEFEEL 160

                         170
                  ....*....|....*..
gi 1840721581 152 GELTLKNISRPIRAFVW 168
Cdd:cd07302   161 GEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
1-175 7.17e-33

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 130.31  E-value: 7.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   1 MKRKLTSILAADIVGFSRLVEAAEEATLARQKELRVSVFDPGVAQAGGKIIKSTGDGFLAEFSSVVE-------AVRFAI 73
Cdd:COG2114   218 GERREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAredhaerAVRAAL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  74 AAQEAVRAEEESVPQ--DRQISYRMGLHIGDVVVD--------DGDIYGDGVNLAARLEGAAPTGGICISAAVRDQIVGv 143
Cdd:COG2114   298 AMQEALAELNAELPAegGPPLRVRIGIHTGEVVVGnigsedrlDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD- 376

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840721581 144 mDELFGDVGELTLKNISRPIRAFVWPPDQDGA 175
Cdd:COG2114   377 -RFEFRELGEVRLKGKAEPVEVYELLGAKEAA 407
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-533 1.87e-13

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 70.91  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 304 ERAAETETNDPEAMLNLAGHYMmgsQPEEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAADAG 383
Cdd:COG2956    32 EEALELDPETVEAHLALGNLYR---RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKA----------GLLDRAEEL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 384 LSKAVSLNDQSDYVHLIRGIFhYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgsfSLAKN 463
Cdd:COG2956    99 LEKLLELDPDDAEALRLLAEI-YEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK---ALKLD 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 464 RIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG2956   175 PDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 301-531 5.13e-12

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 66.68  E-value: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 301 RIAERAAETETNDPEAMLNLAGHYMMGsqpEEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAA 380
Cdd:COG2956    63 RIHQKLLERDPDRAEALLELAQDYLKA---GLLDRAEELLEKLLELDPDDAEALRLLAEIYEQE----------GDWEKA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 381 DAGLSKAVSLNDQSDYVHLIRGiFHYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGsfsL 460
Cdd:COG2956   130 IEVLERLLKLGPENAHAYCELA-ELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERA---L 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840721581 461 AKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAqLYLASAAGQAGLPDQGVRAREALLASD 531
Cdd:COG2956   206 EQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLL-LALADLLERKEGLEAALALLERQLRRH 275
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 7-130 7.55e-12

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: 62.76  E-value: 7.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   7 SILAADIVGFSRLVEAAEEATLARQKELRVSVFDPGVAQAGGKIIKSTGDGFLAEFS--SVVEAVRFAIAAQEAVRAEEE 84
Cdd:cd07556     3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGldHPAAAVAFAEDMREAVSALNQ 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1840721581  85 SVPQDrqISYRMGLHIGDVVVD------DGDIYGDGVNLAARLEGAAPTGGI 130
Cdd:cd07556    83 SEGNP--VRVRIGIHTGPVVVGvigsrpQYDVWGALVNLASRMESQAKAGQV 132
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
 7-138 1.19e-11

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: 63.82  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581    7 SILAADIVGFSRLVEAAE-EATLARQKELrVSVFDPGVAQAGGKIIKSTGDGFLAEFSSVVEAVrfaiaAQEAVRAEEES 85
Cdd:smart00044  38 TILFSDIVGFTSLCSTSTpEQVVNLLNDL-YSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAL-----VDHAELIADEA 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840721581   86 -----------VP-QDRQISYRMGLHIGDVVVD-DG------DIYGDGVNLAARLEGAAPTGGICISAAVRD 138
Cdd:smart00044 112 ldmveelktvlVQhREEGLRVRIGIHTGPVVAGvVGirmpryCLFGDTVNLASRMESAGDPGQIQVSEETYS 183
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 375-534 1.98e-11

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 64.75  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 375 EDIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGiTGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIK 454
Cdd:COG2956    22 GQPDKAIDLLEEALELDPETVEAHLALGNLYRR-RGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 455 KgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG2956   101 K---LLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDC 177
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
388-534 2.58e-11

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.87  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 388 VSLNDQSDYVHLIRGIFHYGItGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgsfSLAKNRIYH 467
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRL-GRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQ---ALELDPDDA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840721581 468 RVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG0457    77 EALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDD 143
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 414-533 4.03e-11

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 60.79  E-value: 4.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 414 AAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgSFSLAKNRIYHRVpqALAQTYLVMGDFENAIANANRA 493
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEK-ALRLDPDNADALL--DLAEALLAAGDTEEAEELLERA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1840721581 494 LQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG4235    78 LALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPA 117
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
7-157 6.22e-11

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 61.49  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581   7 SILAADIVGFSRLVEAAE-EATLARQKELrVSVFDPGVAQAGGKIIKSTGDGFLA-------EFSSVVEAVRFAIAAQEA 78
Cdd:pfam00211  10 TILFADIVGFTALSSRHSpEQVVRLLNEL-YTRFDRLLDKHKVYKVKTIGDAYMVvsglpepSPAHARKIAEMALDMLEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581  79 vrAEEESVPQDRQISYRMGLHIGDVVVD-DG------DIYGDGVNLAARLEGAAPTGGICISAAVRDqIVGVMDELFGDV 151
Cdd:pfam00211  89 --IGEVNVESSEGLRVRVGIHTGPVVAGvIGarmpryDLWGNTVNLASRMESTGVPGKIHVSEETYR-LLKTEGFEFTER 165


                  ....*.
gi 1840721581 152 GELTLK 157
Cdd:pfam00211 166 GEIEVK 171
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 410-534 1.26e-10

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 59.44  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 410 GDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGsfsLAKNRIYHRVPQALAQTYLVMGDFENAIAN 489
Cdd:COG4783    18 GDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEA---LELDPDEPEARLNLGLALLKAGDYDEALAL 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1840721581 490 ANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG4783    95 LEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
376-536 1.50e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.56  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 376 DIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGItGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKK 455
Cdd:COG0457    23 RYEEAIEDYEKALELDPDDAEALYNLGLAYLRL-GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 456 gsfSLAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDFR 535
Cdd:COG0457   102 ---ALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAAL 178


                  .
gi 1840721581 536 I 536
Cdd:COG0457   179 L 179
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 409-534 1.53e-10

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 63.86  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 409 TGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIA 488
Cdd:COG3914    91 LGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRR---ALALNPDFAEAYLNLGEALRRLGRLEEAIA 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1840721581 489 NANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG3914   168 ALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDN 213
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 376-547 1.89e-10

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 63.47  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 376 DIEAADAGLSKAVSLNDQSDYVHLIRGIfHYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKK 455
Cdd:COG3914    93 RYEEALALYRRALALNPDNAEALFNLGN-LLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 456 GsFSLAKNRIYHRvpQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDFR 535
Cdd:COG3914   172 A-LELDPDNAEAL--NNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELLAALARGPS 248

                         170
                  ....*....|..
gi 1840721581 536 ISGVRSFHFQDP 547
Cdd:COG3914   249 ELSPFALLYLPD 260
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 331-534 2.19e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 61.67  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 331 EEWEAAGRLLDRILTVQPRNFmavgmKANTLIGELvwgYRpiRPEDIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGiTG 410
Cdd:COG2956    22 GQPDKAIDLLEEALELDPETV-----EAHLALGNL---YR--RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLK-AG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 411 DLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGSFSLAKNRIYHRvpqALAQTYLVMGDFENAIANA 490
Cdd:COG2956    91 LLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYC---ELAELYLEQGDYDEAIEAL 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1840721581 491 NRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG2956   168 EKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
304-531 1.09e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.25  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 304 ERAAETETNDPEAMLNLAG-HYMMGsqpeEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAADA 382
Cdd:COG0457    32 EKALELDPDDAEALYNLGLaYLRLG----RYEEALADYEQALELDPDDAEALNNLGLALQAL----------GRYEEALE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 383 GLSKAVSLNDQSDYVHLIRGIFHYGItGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGSFSLAK 462
Cdd:COG0457    98 DYDKALELDPDDAEALYNLGLALLEL-GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840721581 463 NRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASD 531
Cdd:COG0457   177 ALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYRA 245
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 375-498 1.69e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 53.27  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 375 EDIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGiTGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIK 454
Cdd:COG4783    18 GDYDEAEALLEKALELDPDNPEAFALLGEILLQ-LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLE 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840721581 455 KgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSP 498
Cdd:COG4783    97 K---ALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 303-534 3.95e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 56.25  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 303 AERAAETETNDPEAMLnLAG--HYMMGSqpeeWEAAGRLLDRILTVQPRNFMAVGMKANTLIgelvwgyrpiRPEDIEAA 380
Cdd:TIGR02917 284 LQDALKSAPEYLPALL-LAGasEYQLGN----LEQAYQYLNQILKYAPNSHQARRLLASIQL----------RLGRVDEA 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 381 DAGLSKAVSLNDQSDYVHLIRGIFHYGiTGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGSfSL 460
Cdd:TIGR02917 349 IATLSPALGLDPDDPAALSLLGEAYLA-LGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAA-QL 426

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840721581 461 AKNRIyhRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:TIGR02917 427 DPELG--RADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDF 498
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 396-533 1.16e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 53.19  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 396 YVHLIRGIFHYgITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGsfsLAKNRIYHRVPQALAQ 475
Cdd:COG2956     9 LGWYFKGLNYL-LNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKL---LERDPDRAEALLELAQ 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840721581 476 TYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG2956    85 DYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPE 142
TolBN COG5616
TolB amino-terminal domain (function unknown) [Signal transduction mechanisms];
182-295 1.68e-07

TolB amino-terminal domain (function unknown) [Signal transduction mechanisms];


Pssm-ID: 444347  Cd Length: 135  Bit Score: 50.27  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 182 PPIGGTSRKPTIAIAAFEALGNNDDAKMLAEACNHTVEAALANLTGVDLIA---------LDADPDHIA---------TA 243
Cdd:COG5616     2 SPAPAAPDRPSIAVLPFENLSGDPEQEYFADGLTEELITALSRLRGLRVIArtssfafkgRAVDLREIArelgvryvlEG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1840721581 244 VFQASGNQVRATLKLRETSTSATYLTQRMNGDISNPFVAEDLLSGEIATTIR 295
Cdd:COG5616    82 SVRRSGDRVRVTAQLIDAATGRHLWSERYDRDLDDLFALQDEIARAIAAALA 133
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
410-500 2.21e-07

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.01  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 410 GDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKkgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIAN 489
Cdd:COG3063     6 GDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEK----ALKLDPNNAEALLNLAELLLELGDYDEALAY 81

                          90
                  ....*....|.
gi 1840721581 490 ANRALQNSPGL 500
Cdd:COG3063    82 LERALELDPSA 92
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 430-534 6.44e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 49.03  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 430 AQGHMVLGWIQNLMGQPELALKSIKKGsfsLAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLAS 509
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKA---LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGL 80

                          90       100
                  ....*....|....*....|....*
gi 1840721581 510 AAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG4783    81 ALLKAGDYDEALALLEKALKLDPEH 105
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 375-498 1.13e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 48.80  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 375 EDIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIK 454
Cdd:COG5010    33 GANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYE 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840721581 455 KgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSP 498
Cdd:COG5010   113 K---ALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 331-455 3.21e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 46.72  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 331 EEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGiTG 410
Cdd:COG4783    18 GDYDEAEALLEKALELDPDNPEAFALLGEILLQL----------GDLDEAIVLLHEALELDPDEPEARLNLGLALLK-AG 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1840721581 411 DLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKK 455
Cdd:COG4783    87 DYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEK 131
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 304-518 6.28e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 49.31  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 304 ERAAETETNDPEAMLNLAghyMMGSQPEEWEAAGRLLDRILTVQPRNfmavgMKANTLIGELVwgyrpIRPEDIEAADAG 383
Cdd:TIGR02917 489 EKALSIEPDFFPAAANLA---RIDIQEGNPDDAIQRFEKVLTIDPKN-----LRAILALAGLY-----LRTGNEEEAVAW 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 384 LSKAVSLN--DQSDYVHLIRgifHYGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgsfsLA 461
Cdd:TIGR02917 556 LEKAAELNpqEIEPALALAQ---YYLGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKK----LL 628

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840721581 462 KNRIYHRVPQA-LAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPD 518
Cdd:TIGR02917 629 ALQPDSALALLlLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTE 686
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 304-533 5.74e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 46.23  E-value: 5.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 304 ERAAETETNDPEAMLNLAGHYMmgsQPEEWEAAGRLLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAADAG 383
Cdd:TIGR02917 421 ETAAQLDPELGRADLLLILSYL---RSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGK----------GDLAKAREA 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 384 LSKAVSLNdqSDYVHLIRGIFHYGI-TGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgSFSLAK 462
Cdd:TIGR02917 488 FEKALSIE--PDFFPAAANLARIDIqEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEK-AAELNP 564

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840721581 463 NRIYHRVpqALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:TIGR02917 565 QEIEPAL--ALAQYYLGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPD 633
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
443-535 7.14e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 41.69  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 443 MGQPELALKSIKKgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIAnANRALQNSPGLPVAQLYLASAAGQAGLPDQGVR 522
Cdd:COG3063     5 LGDLEEAEEYYEK---ALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                          90
                  ....*....|...
gi 1840721581 523 AREALLASDPDFR 535
Cdd:COG3063    81 YLERALELDPSAL 93
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
375-495 1.14e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 43.75  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 375 EDIEAADAGLSKAVSLNDQSDYVHLIRGIFHYGItGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIK 454
Cdd:COG4785    87 GDYDLAIADFDQALELDPDLAEAYNNRGLAYLLL-GDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLE 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1840721581 455 KgSFSLAKNRIYHRVPQALAQ------------------TYLVMGDFENAIANANRALQ 495
Cdd:COG4785   166 K-ALELDPNDPERALWLYLAErkldpekalallledwatAYLLQGDTEEARELFKLALA 223
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
466-535 1.41e-04

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 43.72  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840721581 466 YHRVpqALAQTYLVMGDFENAIANANRALQ-NSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDFR 535
Cdd:COG4700    90 QNRV--RLADALLELGRYDEAIELYEEALTgIFADDPHILLGLAQALFELGRYAEALETLEKLIAKNPDFK 158
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 438-532 2.13e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 41.87  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 438 WIQNLMGQPELALKSIKKgsfSLAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLP 517
Cdd:COG5010    62 NLYNKLGDFEESLALLEQ---ALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQD 138

                          90
                  ....*....|....*
gi 1840721581 518 DQGVRAREALLASDP 532
Cdd:COG5010   139 DEAKAALQRALGTSP 153
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 410-546 1.08e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.99  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 410 GDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKgSFSLAKNRIYHRVpqALAQTYLVMGDFENAIAN 489
Cdd:TIGR02917 173 NRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRK-AIALRPNNIAVLL--ALATILIEAGEFEEAEKH 249

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840721581 490 ANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDFRIS----GVRSFHFQD 546
Cdd:TIGR02917 250 ADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDALKSAPEYLPAlllaGASEYQLGN 310
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 460-534 1.22e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.90  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840721581 460 LAKNRIYHRVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDF 534
Cdd:COG3914    71 AAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDF 145
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
477-534 1.86e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.84  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840721581 477 YLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREAlLASDPDF 534
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKA-LKLDPNN 58
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 468-533 2.59e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840721581 468 RVPQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG5010    55 AIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPD 120
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 302-535 3.42e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.45  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 302 IAERAAETETNDPEAMLNLAGHYMMGSQPEEWEAAgrlLDRILTVQPRNFMAVGMKANTLIGElvwgyrpirpEDIEAAD 381
Cdd:TIGR02917 453 AAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREA---FEKALSIEPDFFPAAANLARIDIQE----------GNPDDAI 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 382 AGLSKAVSLNDQSdyVHLIRGIFH-YGITGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNLMGQPELALKSIKKGSFSL 460
Cdd:TIGR02917 520 QRFEKVLTIDPKN--LRAILALAGlYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAA 597

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840721581 461 AKNRIYHrvpQALAQTYLVMGDFENAIANANRALQNSPGLPVAQLYLASAAGQAGLPDQGVRAREALLASDPDFR 535
Cdd:TIGR02917 598 PDSPEAW---LMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNT 669
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 473-533 4.20e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 37.28  E-value: 4.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840721581 473 LAQTYLVMGDFENAIANANRALQNSPG---LPVAQLYLASAAGQAGLPDQGVRAREALLASDPD 533
Cdd:COG1729    36 LGEAYYALGDYDEAAEAFEKLLKRYPDspkAPDALLKLGLSYLELGDYDKARATLEELIKKYPD 99
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 303-442 5.21e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 37.29  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 303 AERAAETETNDPEAMLNLAGHYMmgsQPEEWEAAGRLLDRILTVQPRNFMAVGMKANTLigelvwgyrpIRPEDIEAADA 382
Cdd:COG4235     6 LRQALAANPNDAEGWLLLGRAYL---RLGRYDEALAAYEKALRLDPDNADALLDLAEAL----------LAAGDTEEAEE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840721581 383 GLSKAVSLNDQSDYVHLIRGIFHYGiTGDLDAAVRCVERGFEISPQFAQGHMVLGWIQNL 442
Cdd:COG4235    73 LLERALALDPDNPEALYLLGLAAFQ-QGDYAEAIAAWQKLLALLPADAPARLLEASIAEA 131
 
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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