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Conserved domains on  [gi|937424736|ref|YP_009167353|]
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2C [Kobuvirus cattle/Kagoshima-2-24-KoV/2015/JPN]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
128-230 6.48e-40

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


:

Pssm-ID: 459992  Cd Length: 102  Bit Score: 135.81  E-value: 6.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736  128 VYLTGPPGCGKSLLASILSATLAKELGGSVDDVYAPAAADcEFYDGYTGQSVHFIDDIGQDPEGKDWKNFPNLVCSAPFI 207
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDD-DFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYP 79
                          90       100
                  ....*....|....*....|...
gi 937424736  208 LPMAAIEDKGTYYTSRVIVCTSN 230
Cdd:pfam00910  80 PPMAALEEKGTPFTSKFVIVTSN 102
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
97-157 1.01e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member PRK09270:

Pssm-ID: 450170  Cd Length: 229  Bit Score: 39.92  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937424736  97 STYIQQSIKN-FTSVLTKAGKRYSgNRPEPFVVYLTGPPGCGKSLLASILsATLAKELGGSV 157
Cdd:PRK09270   5 AQYRDEEIEAvHKPLLRRLAALQA-EPQRRTIVGIAGPPGAGKSTLAEFL-EALLQQDGELP 64
 
Name Accession Description Interval E-value
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
128-230 6.48e-40

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 135.81  E-value: 6.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736  128 VYLTGPPGCGKSLLASILSATLAKELGGSVDDVYAPAAADcEFYDGYTGQSVHFIDDIGQDPEGKDWKNFPNLVCSAPFI 207
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDD-DFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYP 79
                          90       100
                  ....*....|....*....|...
gi 937424736  208 LPMAAIEDKGTYYTSRVIVCTSN 230
Cdd:pfam00910  80 PPMAALEEKGTPFTSKFVIVTSN 102
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
122-256 2.60e-06

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 46.76  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736 122 RPEPFVVYLTGPPGCGKSLLAsilsATLAKELGG--------SVDDVYAPAAADCEFYDGYTGQ----------SVHFID 183
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLA----RAIANELFRpgapflylNASDLLEGLVVAELFGHFLVRLlfelaekakpGVLFID 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937424736 184 DIGQDPEGKDWKNFPNlvcsapfilpMAAIEDKGTYYTSRVIVCTSNFDRANDRaarcMPALERRLHLRIQVR 256
Cdd:cd00009   92 EIDSLSRGAQNALLRV----------LETLNDLRIDRENVRVIGATNRPLLGDL----DRALYDRLDIRIVIP 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
130-255 5.89e-05

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 44.52  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736 130 LTGPPGCGKSLLASIlsatLAKELGGsvdDVYAPAAADceFYDGYTGQS-----------------VHFIDDI----GQD 188
Cdd:COG0464  196 LYGPPGTGKTLLARA----LAGELGL---PLIEVDLSD--LVSKYVGETeknlrevfdkarglapcVLFIDEAdalaGKR 266
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937424736 189 PEGKDwkNFPNLVCSApFILPMAAIEDKGtyytsrVIVCTSN-FDRANdraarcmPALERRLHLRIQV 255
Cdd:COG0464  267 GEVGD--GVGRRVVNT-LLTEMEELRSDV------VVIAATNrPDLLD-------PALLRRFDEIIFF 318
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
97-157 1.01e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 39.92  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937424736  97 STYIQQSIKN-FTSVLTKAGKRYSgNRPEPFVVYLTGPPGCGKSLLASILsATLAKELGGSV 157
Cdd:PRK09270   5 AQYRDEEIEAvHKPLLRRLAALQA-EPQRRTIVGIAGPPGAGKSTLAEFL-EALLQQDGELP 64
PRK08903 PRK08903
DnaA regulatory inactivator Hda; Validated
119-185 1.07e-03

DnaA regulatory inactivator Hda; Validated


Pssm-ID: 236347 [Multi-domain]  Cd Length: 227  Bit Score: 39.96  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937424736 119 SGNRPEPFVvYLTGPPGCGKSLLasiLSATLAKELGGSVDDVYAPAAADCEFYDGYTGQSVHFIDDI 185
Cdd:PRK08903  37 AGPVADRFF-YLWGEAGSGRSHL---LQALVADASYGGRNARYLDAASPLLAFDFDPEAELYAVDDV 99
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
97-151 4.93e-03

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 38.35  E-value: 4.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 937424736  97 STYIQQSIKNFTSVLTKAGKRysgNRPEPFVVYLTGPPGCGKSLLASILSATLAK 151
Cdd:COG1072   61 NLYVAATQRLHRATSAFLGQA---DKKTPFIIGIAGSVAVGKSTTARLLQALLSR 112
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
128-159 5.08e-03

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 38.54  E-value: 5.08e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 937424736  128 VYLTGPPGCGKSLLASILSATLAKELGGSVDD 159
Cdd:TIGR03689 219 VLLYGPPGCGKTLIAKAVANSLAARIGAEGGG 250
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
127-191 7.13e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 7.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937424736   127 VVYLTGPPGCGKSLLAsilsATLAKELGGSVDDVYapaAADCEFYDGYTGQSVHFIDDIGQDPEG 191
Cdd:smart00382   4 VILIVGPPGSGKTTLA----RALARELGPPGGGVI---YIDGEDILEEVLDQLLLIIVGGKKASG 61
 
Name Accession Description Interval E-value
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
128-230 6.48e-40

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 135.81  E-value: 6.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736  128 VYLTGPPGCGKSLLASILSATLAKELGGSVDDVYAPAAADcEFYDGYTGQSVHFIDDIGQDPEGKDWKNFPNLVCSAPFI 207
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDD-DFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYP 79
                          90       100
                  ....*....|....*....|...
gi 937424736  208 LPMAAIEDKGTYYTSRVIVCTSN 230
Cdd:pfam00910  80 PPMAALEEKGTPFTSKFVIVTSN 102
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
122-256 2.60e-06

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 46.76  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736 122 RPEPFVVYLTGPPGCGKSLLAsilsATLAKELGG--------SVDDVYAPAAADCEFYDGYTGQ----------SVHFID 183
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLA----RAIANELFRpgapflylNASDLLEGLVVAELFGHFLVRLlfelaekakpGVLFID 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937424736 184 DIGQDPEGKDWKNFPNlvcsapfilpMAAIEDKGTYYTSRVIVCTSNFDRANDRaarcMPALERRLHLRIQVR 256
Cdd:cd00009   92 EIDSLSRGAQNALLRV----------LETLNDLRIDRENVRVIGATNRPLLGDL----DRALYDRLDIRIVIP 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
130-255 5.89e-05

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 44.52  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736 130 LTGPPGCGKSLLASIlsatLAKELGGsvdDVYAPAAADceFYDGYTGQS-----------------VHFIDDI----GQD 188
Cdd:COG0464  196 LYGPPGTGKTLLARA----LAGELGL---PLIEVDLSD--LVSKYVGETeknlrevfdkarglapcVLFIDEAdalaGKR 266
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937424736 189 PEGKDwkNFPNLVCSApFILPMAAIEDKGtyytsrVIVCTSN-FDRANdraarcmPALERRLHLRIQV 255
Cdd:COG0464  267 GEVGD--GVGRRVVNT-LLTEMEELRSDV------VVIAATNrPDLLD-------PALLRRFDEIIFF 318
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
128-185 2.45e-04

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 40.27  E-value: 2.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 937424736  128 VYLTGPPGCGKSLLASIlsatLAKELGGSVDDVYAPaaadcEFYDGYTGQSVHFIDDI 185
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKA----VAKELGAPFIEISGS-----ELVSKYVGESEKRLREL 49
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
100-185 3.35e-04

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 40.73  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937424736 100 IQQSIKNFTSVLTKAGKRYSGNRPEPFVVYLTGPPGCGKSLLAsilsATLAKELGGSVddVYAPAAADCEFYDGYTGQSV 179
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLA----KALAGELGLPL--IVVKLSSLLSKYVGESEKNL 74
                         90       100
                 ....*....|....*....|
gi 937424736 180 H--------------FIDDI 185
Cdd:cd19481   75 RkiferarrlapcilFIDEI 94
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
97-157 1.01e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 39.92  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937424736  97 STYIQQSIKN-FTSVLTKAGKRYSgNRPEPFVVYLTGPPGCGKSLLASILsATLAKELGGSV 157
Cdd:PRK09270   5 AQYRDEEIEAvHKPLLRRLAALQA-EPQRRTIVGIAGPPGAGKSTLAEFL-EALLQQDGELP 64
PRK08903 PRK08903
DnaA regulatory inactivator Hda; Validated
119-185 1.07e-03

DnaA regulatory inactivator Hda; Validated


Pssm-ID: 236347 [Multi-domain]  Cd Length: 227  Bit Score: 39.96  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937424736 119 SGNRPEPFVvYLTGPPGCGKSLLasiLSATLAKELGGSVDDVYAPAAADCEFYDGYTGQSVHFIDDI 185
Cdd:PRK08903  37 AGPVADRFF-YLWGEAGSGRSHL---LQALVADASYGGRNARYLDAASPLLAFDFDPEAELYAVDDV 99
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
128-185 1.54e-03

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 38.80  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 937424736 128 VYLTGPPGCGKSLLASilsaTLAKELGGSVDDVYAPaaadcEFYDGYTGQSVHFIDDI 185
Cdd:cd19511   30 VLLYGPPGCGKTLLAK----ALASEAGLNFISVKGP-----ELFSKYVGESERAVREI 78
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
128-172 3.93e-03

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 37.41  E-value: 3.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937424736 128 VYLTGPPGCGKSLLASILSAT-------------LAKELGGS---VDDVY--APAAADC-EFYD 172
Cdd:cd19526   30 ILLYGPPGCGKTLLASAIASEcglnfisvkgpelLNKYIGASeqnVRDLFsrAQSAKPCiLFFD 93
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
97-151 4.93e-03

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 38.35  E-value: 4.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 937424736  97 STYIQQSIKNFTSVLTKAGKRysgNRPEPFVVYLTGPPGCGKSLLASILSATLAK 151
Cdd:COG1072   61 NLYVAATQRLHRATSAFLGQA---DKKTPFIIGIAGSVAVGKSTTARLLQALLSR 112
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
128-159 5.08e-03

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 38.54  E-value: 5.08e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 937424736  128 VYLTGPPGCGKSLLASILSATLAKELGGSVDD 159
Cdd:TIGR03689 219 VLLYGPPGCGKTLIAKAVANSLAARIGAEGGG 250
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
127-191 7.13e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 7.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937424736   127 VVYLTGPPGCGKSLLAsilsATLAKELGGSVDDVYapaAADCEFYDGYTGQSVHFIDDIGQDPEG 191
Cdd:smart00382   4 VILIVGPPGSGKTTLA----RALARELGPPGGGVI---YIDGEDILEEVLDQLLLIIVGGKKASG 61
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
100-160 9.94e-03

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 36.18  E-value: 9.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937424736 100 IQQSIKNFTSvltkaGKRYSGNRPEPFVVY--LTGPPGCGKSllaSILSAtLAKELGGSVDDV 160
Cdd:cd19510    1 IIDDLKDFIK-----NEDWYNDRGIPYRRGylLYGPPGTGKS---SFIAA-LAGELDYDICDL 54
 
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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