NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|517611610|ref|WP_018781818|]
View 

MULTISPECIES: dynamin family protein [Bacillus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 379-568 3.30e-14

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd09912:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 180  Bit Score: 71.81  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 379 RLLVTGTSGNGKASFINSILGENILEnsisnvvvfkndahteinaiTDSTITTtenfsdfhnmmslhrqtykDRACVefk 458
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLGEEVLP--------------------TGVTPTT-------------------AVITV--- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 459 lpCRFLSKNKLTFVVTPSFNRNNDTRDE-TFEYLNSVDELLFVLNADSPFTDKERDILLSIQEhTPNLQIHFLLNKIDNI 537
Cdd:cd09912   40 --LRYGLLKGVVLVDTPGLNSTIEHHTEiTESFLPRADAVIFVLSADQPLTESEREFLKEILK-WSGKKIFFVLNKIDLL 116

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517611610 538 ySEAEAKRVIHDTQ-----ARINAYFPhaRIFPYSS 568
Cdd:cd09912  117 -SEEELEEVLEYSReelgvLELGGGEP--RIFPVSA 149
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 12-175 1.47e-08

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: 57.05  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  12 YYETFLMENETHPP-LQVLGGAYLNEQKNE------------ISDGSYIRFAQGEFYYHHQDFETAIFKWEKV--SNELA 76
Cdd:COG2956   98 LLEKLLELDPDDAEaLRLLAEIYEQEGDWEkaievlerllklGPENAHAYCELAELYLEQGDYDEAIEALEKAlkLDPDC 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  77 PWAQKNIADAYFELNQLSVAENVYTSITTDNKILMtEIVLQLLSLYIEQNNLDSAFAVIKEAVSLNPDYPNVTTIARsFY 156
Cdd:COG2956  178 ARALLLLAELYLEQGDYEEAIAALERALEQDPDYL-PALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD-LL 255

                        170
                 ....*....|....*....
gi 517611610 157 EEQQDFDSAVELAVNELIR 175
Cdd:COG2956  256 ERKEGLEAALALLERQLRR 274
 
Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 379-568 3.30e-14

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 71.81  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 379 RLLVTGTSGNGKASFINSILGENILEnsisnvvvfkndahteinaiTDSTITTtenfsdfhnmmslhrqtykDRACVefk 458
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLGEEVLP--------------------TGVTPTT-------------------AVITV--- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 459 lpCRFLSKNKLTFVVTPSFNRNNDTRDE-TFEYLNSVDELLFVLNADSPFTDKERDILLSIQEhTPNLQIHFLLNKIDNI 537
Cdd:cd09912   40 --LRYGLLKGVVLVDTPGLNSTIEHHTEiTESFLPRADAVIFVLSADQPLTESEREFLKEILK-WSGKKIFFVLNKIDLL 116

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517611610 538 ySEAEAKRVIHDTQ-----ARINAYFPhaRIFPYSS 568
Cdd:cd09912  117 -SEEELEEVLEYSReelgvLELGGGEP--RIFPVSA 149
Dynamin_N pfam00350
Dynamin family;
380-515 5.66e-10

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 59.17  E-value: 5.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  380 LLVTGTSGNGKASFINSILGENILENSIS------NVVVFKNDAHTEINAITDSTITTTENFSDFHN--------MMSLH 445
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGpttrrpTVLRLGESPGASEGAVKVEYKDGEKKFEDFSElreeiekeTEKIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517611610  446 RQTYKDRACVEFKLPCRFLSKNkLTFVVTPSFNRNNDTRDE-TFEYLNSVDELLFVLNADSPFTDKERDIL 515
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPG-LTLVDTPGLDSVAVGDQElTKEYIKPADIILAVTPANVDLSTSEALFL 150
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 12-175 1.47e-08

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: 57.05  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  12 YYETFLMENETHPP-LQVLGGAYLNEQKNE------------ISDGSYIRFAQGEFYYHHQDFETAIFKWEKV--SNELA 76
Cdd:COG2956   98 LLEKLLELDPDDAEaLRLLAEIYEQEGDWEkaievlerllklGPENAHAYCELAELYLEQGDYDEAIEALEKAlkLDPDC 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  77 PWAQKNIADAYFELNQLSVAENVYTSITTDNKILMtEIVLQLLSLYIEQNNLDSAFAVIKEAVSLNPDYPNVTTIARsFY 156
Cdd:COG2956  178 ARALLLLAELYLEQGDYEEAIAALERALEQDPDYL-PALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD-LL 255

                        170
                 ....*....|....*....
gi 517611610 157 EEQQDFDSAVELAVNELIR 175
Cdd:COG2956  256 ERKEGLEAALALLERQLRR 274
era PRK00089
GTPase Era; Reviewed
 491-583 2.71e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 50.05  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 491 LNSVDELLFVLNADSPFTDKERDILLSIQE-HTPnlqiHFL-LNKIDNIYSEAEAKRVIhdtqARINAYFPHARIFPYSS 568
Cdd:PRK00089  82 LKDVDLVLFVVDADEKIGPGDEFILEKLKKvKTP----VILvLNKIDLVKDKEELLPLL----EELSELMDFAEIVPISA 153

                         90
                 ....*....|....*
gi 517611610 569 LytNSQQLNDLTEFI 583
Cdd:PRK00089 154 L--KGDNVDELLDVI 166
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
491-583 6.95e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 45.75  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 491 LNSVDELLFVLNADSPFTDKERDILLSIQE-HTPnlqiHFL-LNKIDNIYSEAEAKRVihdtqARINAYFPHARIFPYSS 568
Cdd:COG1159   80 LEDVDVILFVVDATEKIGEGDEFILELLKKlKTP----VILvINKIDLVKKEELLPLL-----AEYSELLDFAEIVPISA 150

                         90
                 ....*....|....*
gi 517611610 569 LytNSQQLNDLTEFI 583
Cdd:COG1159  151 L--KGDNVDELLDEI 163
 
Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 379-568 3.30e-14

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 71.81  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 379 RLLVTGTSGNGKASFINSILGENILEnsisnvvvfkndahteinaiTDSTITTtenfsdfhnmmslhrqtykDRACVefk 458
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLGEEVLP--------------------TGVTPTT-------------------AVITV--- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 459 lpCRFLSKNKLTFVVTPSFNRNNDTRDE-TFEYLNSVDELLFVLNADSPFTDKERDILLSIQEhTPNLQIHFLLNKIDNI 537
Cdd:cd09912   40 --LRYGLLKGVVLVDTPGLNSTIEHHTEiTESFLPRADAVIFVLSADQPLTESEREFLKEILK-WSGKKIFFVLNKIDLL 116

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517611610 538 ySEAEAKRVIHDTQ-----ARINAYFPhaRIFPYSS 568
Cdd:cd09912  117 -SEEELEEVLEYSReelgvLELGGGEP--RIFPVSA 149
Dynamin_N pfam00350
Dynamin family;
380-515 5.66e-10

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 59.17  E-value: 5.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  380 LLVTGTSGNGKASFINSILGENILENSIS------NVVVFKNDAHTEINAITDSTITTTENFSDFHN--------MMSLH 445
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGpttrrpTVLRLGESPGASEGAVKVEYKDGEKKFEDFSElreeiekeTEKIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517611610  446 RQTYKDRACVEFKLPCRFLSKNkLTFVVTPSFNRNNDTRDE-TFEYLNSVDELLFVLNADSPFTDKERDIL 515
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPG-LTLVDTPGLDSVAVGDQElTKEYIKPADIILAVTPANVDLSTSEALFL 150
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 12-175 1.47e-08

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: 57.05  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  12 YYETFLMENETHPP-LQVLGGAYLNEQKNE------------ISDGSYIRFAQGEFYYHHQDFETAIFKWEKV--SNELA 76
Cdd:COG2956   98 LLEKLLELDPDDAEaLRLLAEIYEQEGDWEkaievlerllklGPENAHAYCELAELYLEQGDYDEAIEALEKAlkLDPDC 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  77 PWAQKNIADAYFELNQLSVAENVYTSITTDNKILMtEIVLQLLSLYIEQNNLDSAFAVIKEAVSLNPDYPNVTTIARsFY 156
Cdd:COG2956  178 ARALLLLAELYLEQGDYEEAIAALERALEQDPDYL-PALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD-LL 255

                        170
                 ....*....|....*....
gi 517611610 157 EEQQDFDSAVELAVNELIR 175
Cdd:COG2956  256 ERKEGLEAALALLERQLRR 274
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 47-168 1.12e-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: 54.35  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  47 IRFAQGEFYYHHQDFETAIFKWEKV--SNELAPWAQKNIADAYFELNQLSVAENVYTSITTDNKILMtEIVLQLLSLYIE 124
Cdd:COG2956   78 ALLELAQDYLKAGLLDRAEELLEKLleLDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENA-HAYCELAELYLE 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517611610 125 QNNLDSAFAVIKEAVSLNPDYPNVTTIARSFYEEQQDFDSAVEL 168
Cdd:COG2956  157 QGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAA 200
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 491-583 1.49e-06

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 49.00  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 491 LNSVDELLFVLNADSPFTDKERDILLSIQE-HTPnlqiHFL-LNKIDNIYSEAEAKRVIHDtqarINAYFPHARIFPYSS 568
Cdd:cd04163   80 LKDVDLVLFVVDASEWIGEGDEFILELLKKsKTP----VILvLNKIDLVKDKEDLLPLLEK----LKELHPFAEIFPISA 151

                         90
                 ....*....|....*
gi 517611610 569 LytNSQQLNDLTEFI 583
Cdd:cd04163  152 L--KGENVDELLEYI 164
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 48-192 1.87e-06

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: 50.50  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  48 RFAQGEFYYHHQDFETAIFKWEKV--SNELAPWAQKNIADAYFELNQLSVAENVYTSITTDNKILmTEIVLQLLSLYIEQ 125
Cdd:COG2956   11 WYFKGLNYLLNGQPDKAIDLLEEAleLDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDR-AEALLELAQDYLKA 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 126 NNLDSAFAVIKEAVSLNPDYPNVTTIARSFYEEQQDFDSAVELAvNELIR---TESFPWFEVLKEYIDKG 192
Cdd:COG2956   90 GLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVL-ERLLKlgpENAHAYCELAELYLEQG 158
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 381-569 1.87e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 48.61  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 381 LVTGTSGNGKASFINSILGENILENSISNVVvfkndahteinaitdstiTTTENFSDFHNMMSLHrqtykdracvefklp 460
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGT------------------TRDPDVYVKELDKGKV--------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 461 crflsknKLTFVVTPSFNRNNDTRDE--TFEYLNSVDELLFVLNADSPFTDKERDILLSIQEHTPNLQIHFLLNKIDNIy 538
Cdd:cd00882   48 -------KLVLVDTPGLDEFGGLGREelARLLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLL- 119

                        170       180       190
                 ....*....|....*....|....*....|.
gi 517611610 539 seaEAKRVIHDTQARINAYFPHARIFPYSSL 569
Cdd:cd00882  120 ---EEREVEELLRLEELAKILGVPVFEVSAK 147
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 48-169 2.00e-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: 48.26  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  48 RFAQGEFYYHHQDFETAIFKWEKVSNELA--PWAQKNIADAYFELNQLSVAENVY---TSITTDNkilmTEIVLQLLSLY 122
Cdd:COG4783    7 LYALAQALLLAGDYDEAEALLEKALELDPdnPEAFALLGEILLQLGDLDEAIVLLheaLELDPDE----PEARLNLGLAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 517611610 123 IEQNNLDSAFAVIKEAVSLNPDYPNVTTIARSFYEEQQDFDSAVELA 169
Cdd:COG4783   83 LKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAAL 129
era PRK00089
GTPase Era; Reviewed
 491-583 2.71e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 50.05  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 491 LNSVDELLFVLNADSPFTDKERDILLSIQE-HTPnlqiHFL-LNKIDNIYSEAEAKRVIhdtqARINAYFPHARIFPYSS 568
Cdd:PRK00089  82 LKDVDLVLFVVDADEKIGPGDEFILEKLKKvKTP----VILvLNKIDLVKDKEELLPLL----EELSELMDFAEIVPISA 153

                         90
                 ....*....|....*
gi 517611610 569 LytNSQQLNDLTEFI 583
Cdd:PRK00089 154 L--KGDNVDELLDVI 166
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 77-168 2.10e-05

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: 45.00  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  77 PWAQKNIADAYFELNQLSVAENVYTSITT---DNkilmTEIVLQLLSLYIEQNNLDSAFAVIKEAVSLNPDYPNvttiAR 153
Cdd:COG4235   17 AEGWLLLGRAYLRLGRYDEALAAYEKALRldpDN----ADALLDLAEALLAAGDTEEAEELLERALALDPDNPE----AL 88

                         90
                 ....*....|....*....
gi 517611610 154 SF----YEEQQDFDSAVEL 168
Cdd:COG4235   89 YLlglaAFQQGDYAEAIAA 107
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
491-583 6.95e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 45.75  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610 491 LNSVDELLFVLNADSPFTDKERDILLSIQE-HTPnlqiHFL-LNKIDNIYSEAEAKRVihdtqARINAYFPHARIFPYSS 568
Cdd:COG1159   80 LEDVDVILFVVDATEKIGEGDEFILELLKKlKTP----VILvINKIDLVKKEELLPLL-----AEYSELLDFAEIVPISA 150

                         90
                 ....*....|....*
gi 517611610 569 LytNSQQLNDLTEFI 583
Cdd:COG1159  151 L--KGDNVDELLDEI 163
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
49-168 6.36e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.30  E-value: 6.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  49 FAQGEFYYHHQDFETAIFKWEKVSnELAP---WAQKNIADAYFELNQLSVAENVYT-SITTDNKILmtEIVLQLLSLYIE 124
Cdd:COG0457   46 YNLGLAYLRLGRYEEALADYEQAL-ELDPddaEALNNLGLALQALGRYEEALEDYDkALELDPDDA--EALYNLGLALLE 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517611610 125 QNNLDSAFAVIKEAVSLNPDYPNVTTIARSFYEEQQDFDSAVEL 168
Cdd:COG0457  123 LGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALEL 166
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
49-168 1.77e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.15  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  49 FAQGEFYYHHQDFETAIFKWEKVSnELAP---WAQKNIADAYFELNQLSVAENVYT-SITTDNKilMTEIVLQLLSLYIE 124
Cdd:COG0457   12 NNLGLAYRRLGRYEEAIEDYEKAL-ELDPddaEALYNLGLAYLRLGRYEEALADYEqALELDPD--DAEALNNLGLALQA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517611610 125 QNNLDSAFAVIKEAVSLNPDYPNVTTIARSFYEEQQDFDSAVEL 168
Cdd:COG0457   89 LGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEA 132
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 55-147 3.84e-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: 38.05  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517611610  55 YYHHQDFETAIFKWEKV-----SNELAPWAQKNIADAYFELNQLSVAENVYTSITTD--NKILMTEIVLQLLSLYIEQNN 127
Cdd:COG1729    3 LLKAGDYDEAIAAFKAFlkrypNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRypDSPKAPDALLKLGLSYLELGD 82

                         90       100
                 ....*....|....*....|
gi 517611610 128 LDSAFAVIKEAVSlnpDYPN 147
Cdd:COG1729   83 YDKARATLEELIK---KYPD 99
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 379-415 6.61e-03

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 38.74  E-value: 6.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 517611610  379 RLLVTGTSGNGKASFINSILGENILENSISNVVVFKN 415
Cdd:pfam04548   2 RIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKT 38
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH