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Conserved domains on  [gi|1953095599|ref|XP_038403262|]
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2',3'-cyclic-nucleotide 3'-phosphodiesterase isoform X3 [Canis lupus familiaris]

Protein Classification

ATP-binding protein( domain architecture ID 13597307)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CNPase pfam05881
2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the ...
 185-398 2.39e-152

2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the eukaryotic protein 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP). 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP) is one of the earliest myelin-related proteins expressed in differentiating oligodendrocytes and Schwann cells. CNP is abundant in the central nervous system and in oligodendrocytes. This protein is also found in mammalian photoreceptor cells, testis and lymphocytes. Although the biological function of CNP is unknown, it is thought to play a significant role in the formation of the myelin sheath, where it comprises 4% of total protein. CNP selectively cleaves 2',3'-cyclic nucleotides to produce 2'-nucleotides in vitro. Although physiologically relevant substrates with 2',3'-cyclic termini are still unknown, numerous cyclic phosphate containing RNAs occur transiently within eukaryotic cells. Other known protein families capable of hydrolysing 2',3'-cyclic nucleotides include tRNA ligases and plant cyclic phosphodiesterases. The catalytic domains from all these proteins contain two tetra-peptide motifs H-X-T/S-X, where X is usually a hydrophobic residue. Mutation of either histidine in CNP abolishes enzymatic activity. CNPases belong to the 2H phosphoesterase superfamily. They share a common active site, characterized by two conserved histidines, with the bacterial tRNA-ligating enzyme LigT, vertebrate myelin-associated 2',3' phosphodiesterases, plant Arabidopsis thaliana CPDases and several several bacteria and virus proteins.


:

Pssm-ID: 461769  Cd Length: 214  Bit Score: 429.64  E-value: 2.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 185 LPLYFGWFLTKKSSESLRKAGQAFLEELGNHKAFKKELRHFVSGDEPREKIELVTYFGKRPPGVLHCTTKFCDYGKAAGA 264
Cdd:pfam05881   1 LPLYFGWFLTKKSSEALRKTGQVFLEELGNHKAFKKELRHFQSGDEPKEKIDLTSYFGKRPPGVLHCTTKFCDYGKAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 265 DEYAQQDVVKKSYCKAFTLTITALFVTPKTAGARVELSEQELPLWPNDVDKLSPSDSLPRGSRAHITLGCAGDVEPVQTG 344
Cdd:pfam05881  81 EEYAQQDVVKKSYGKAFTLSISALFVTPKTVGARVELNEQQLALWPADVDKLSPSDSLPKGSRAHVTLGCASDVEAVQTG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953095599 345 IDLLEIVRQEKGGSRGEEVGELNRGKLYSLGNGRWLLSLAKKLEVRAIFTGYYG 398
Cdd:pfam05881 161 LDLLEIVKLEKGGSQGEEVGELGRGKLQSLGNGRWMLSLAKKIEVRAIFSGYYG 214
COG4639 super family cl44097
Predicted kinase [General function prediction only];
50-147 3.27e-13

Predicted kinase [General function prediction only];


The actual alignment was detected with superfamily member COG4639:

Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 66.78  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  50 KTLFILRGLPGSGKSTLARvivdRYRDGTKMVSADAY----KITPGARGDFSEEYKRLDEDLAAYCRRDvRVLVLDDTNH 125
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFAR----RLFAPTEVVSSDDIrallGGDENDQSAWGDVFQLAHEIARARLRAG-RLTVVDATNL 76

                          90       100
                  ....*....|....*....|..
gi 1953095599 126 ERERLEQLFELADQYQYQVVLV 147
Cdd:COG4639    77 QREARRRLLALARAYGALVVAV 98
 
Name Accession Description Interval E-value
CNPase pfam05881
2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the ...
 185-398 2.39e-152

2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the eukaryotic protein 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP). 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP) is one of the earliest myelin-related proteins expressed in differentiating oligodendrocytes and Schwann cells. CNP is abundant in the central nervous system and in oligodendrocytes. This protein is also found in mammalian photoreceptor cells, testis and lymphocytes. Although the biological function of CNP is unknown, it is thought to play a significant role in the formation of the myelin sheath, where it comprises 4% of total protein. CNP selectively cleaves 2',3'-cyclic nucleotides to produce 2'-nucleotides in vitro. Although physiologically relevant substrates with 2',3'-cyclic termini are still unknown, numerous cyclic phosphate containing RNAs occur transiently within eukaryotic cells. Other known protein families capable of hydrolysing 2',3'-cyclic nucleotides include tRNA ligases and plant cyclic phosphodiesterases. The catalytic domains from all these proteins contain two tetra-peptide motifs H-X-T/S-X, where X is usually a hydrophobic residue. Mutation of either histidine in CNP abolishes enzymatic activity. CNPases belong to the 2H phosphoesterase superfamily. They share a common active site, characterized by two conserved histidines, with the bacterial tRNA-ligating enzyme LigT, vertebrate myelin-associated 2',3' phosphodiesterases, plant Arabidopsis thaliana CPDases and several several bacteria and virus proteins.


Pssm-ID: 461769  Cd Length: 214  Bit Score: 429.64  E-value: 2.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 185 LPLYFGWFLTKKSSESLRKAGQAFLEELGNHKAFKKELRHFVSGDEPREKIELVTYFGKRPPGVLHCTTKFCDYGKAAGA 264
Cdd:pfam05881   1 LPLYFGWFLTKKSSEALRKTGQVFLEELGNHKAFKKELRHFQSGDEPKEKIDLTSYFGKRPPGVLHCTTKFCDYGKAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 265 DEYAQQDVVKKSYCKAFTLTITALFVTPKTAGARVELSEQELPLWPNDVDKLSPSDSLPRGSRAHITLGCAGDVEPVQTG 344
Cdd:pfam05881  81 EEYAQQDVVKKSYGKAFTLSISALFVTPKTVGARVELNEQQLALWPADVDKLSPSDSLPKGSRAHVTLGCASDVEAVQTG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953095599 345 IDLLEIVRQEKGGSRGEEVGELNRGKLYSLGNGRWLLSLAKKLEVRAIFTGYYG 398
Cdd:pfam05881 161 LDLLEIVKLEKGGSQGEEVGELGRGKLQSLGNGRWMLSLAKKIEVRAIFSGYYG 214
COG4639 COG4639
Predicted kinase [General function prediction only];
50-147 3.27e-13

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 66.78  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  50 KTLFILRGLPGSGKSTLARvivdRYRDGTKMVSADAY----KITPGARGDFSEEYKRLDEDLAAYCRRDvRVLVLDDTNH 125
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFAR----RLFAPTEVVSSDDIrallGGDENDQSAWGDVFQLAHEIARARLRAG-RLTVVDATNL 76

                          90       100
                  ....*....|....*....|..
gi 1953095599 126 ERERLEQLFELADQYQYQVVLV 147
Cdd:COG4639    77 QREARRRLLALARAYGALVVAV 98
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 52-165 1.84e-09

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 55.78  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  52 LFILRGLPGSGKSTLARVIVDRYrdGTKMVSADAY--KITPGARGDFS---EEYKRLDE---DLAAYCRRDVRVLVLDDT 123
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEEL--GAVRLSSDDErkRLFGEGRPSISyytDATDRTYErlhELARIALRAGRPVILDAT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953095599 124 NHERERLEQLFELADQYQYQVVLVEPKTAWrldcAQLKEKNQ 165
Cdd:pfam13671  79 NLRRDERARLLALAREYGVPVRIVVFEAPE----EVLRERLA 116
pseT PHA02530
polynucleotide kinase; Provisional
 50-147 1.21e-08

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 56.18  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  50 KTLFILRGLPGSGKSTLARVIVDRYRdGTKMVSADAYKIT---PGARGDFSeeYKRLDEDLAAYCRRDVRVL-------- 118
Cdd:PHA02530    2 MKIILTVGVPGSGKSTWAREFAAKNP-KAVNVNRDDLRQSlfgHGEWGEYK--FTKEKEDLVTKAQEAAALAalksgksv 78

                          90       100
                  ....*....|....*....|....*....
gi 1953095599 119 VLDDTNHERERLEQLFELADQYQYQVVLV 147
Cdd:PHA02530   79 IISDTNLNPERRRKWKELAKELGAEFEEK 107
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 53-132 3.19e-04

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: 40.98  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  53 FILRGLPGSGKSTLARVIVDR-YRDGTKMVSADAYKITPGARGDFSEEYKRLDEDLAAYCRRDVRVLVLDDTNHERERLE 131
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANElFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQ 101


                  .
gi 1953095599 132 Q 132
Cdd:cd00009   102 N 102
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 54-147 6.34e-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: 36.97  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599   54 ILRGLPGSGKSTLARVIVDRY-RDGTKMVSADaykitpgarGDFSEEYKRLDedlaaycRRDVRVLVLDDTNHERERLEQ 132
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELgPPGGGVIYID---------GEDILEEVLDQ-------LLLIIVGGKKASGSGELRLRL 69

                           90
                   ....*....|....*
gi 1953095599  133 LFELADQYQYQVVLV 147
Cdd:smart00382  70 ALALARKLKPDVLIL 84
 
Name Accession Description Interval E-value
CNPase pfam05881
2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the ...
 185-398 2.39e-152

2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the eukaryotic protein 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP). 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP) is one of the earliest myelin-related proteins expressed in differentiating oligodendrocytes and Schwann cells. CNP is abundant in the central nervous system and in oligodendrocytes. This protein is also found in mammalian photoreceptor cells, testis and lymphocytes. Although the biological function of CNP is unknown, it is thought to play a significant role in the formation of the myelin sheath, where it comprises 4% of total protein. CNP selectively cleaves 2',3'-cyclic nucleotides to produce 2'-nucleotides in vitro. Although physiologically relevant substrates with 2',3'-cyclic termini are still unknown, numerous cyclic phosphate containing RNAs occur transiently within eukaryotic cells. Other known protein families capable of hydrolysing 2',3'-cyclic nucleotides include tRNA ligases and plant cyclic phosphodiesterases. The catalytic domains from all these proteins contain two tetra-peptide motifs H-X-T/S-X, where X is usually a hydrophobic residue. Mutation of either histidine in CNP abolishes enzymatic activity. CNPases belong to the 2H phosphoesterase superfamily. They share a common active site, characterized by two conserved histidines, with the bacterial tRNA-ligating enzyme LigT, vertebrate myelin-associated 2',3' phosphodiesterases, plant Arabidopsis thaliana CPDases and several several bacteria and virus proteins.


Pssm-ID: 461769  Cd Length: 214  Bit Score: 429.64  E-value: 2.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 185 LPLYFGWFLTKKSSESLRKAGQAFLEELGNHKAFKKELRHFVSGDEPREKIELVTYFGKRPPGVLHCTTKFCDYGKAAGA 264
Cdd:pfam05881   1 LPLYFGWFLTKKSSEALRKTGQVFLEELGNHKAFKKELRHFQSGDEPKEKIDLTSYFGKRPPGVLHCTTKFCDYGKAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 265 DEYAQQDVVKKSYCKAFTLTITALFVTPKTAGARVELSEQELPLWPNDVDKLSPSDSLPRGSRAHITLGCAGDVEPVQTG 344
Cdd:pfam05881  81 EEYAQQDVVKKSYGKAFTLSISALFVTPKTVGARVELNEQQLALWPADVDKLSPSDSLPKGSRAHVTLGCASDVEAVQTG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953095599 345 IDLLEIVRQEKGGSRGEEVGELNRGKLYSLGNGRWLLSLAKKLEVRAIFTGYYG 398
Cdd:pfam05881 161 LDLLEIVKLEKGGSQGEEVGELGRGKLQSLGNGRWMLSLAKKIEVRAIFSGYYG 214
COG4639 COG4639
Predicted kinase [General function prediction only];
50-147 3.27e-13

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 66.78  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  50 KTLFILRGLPGSGKSTLARvivdRYRDGTKMVSADAY----KITPGARGDFSEEYKRLDEDLAAYCRRDvRVLVLDDTNH 125
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFAR----RLFAPTEVVSSDDIrallGGDENDQSAWGDVFQLAHEIARARLRAG-RLTVVDATNL 76

                          90       100
                  ....*....|....*....|..
gi 1953095599 126 ERERLEQLFELADQYQYQVVLV 147
Cdd:COG4639    77 QREARRRLLALARAYGALVVAV 98
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 52-165 1.84e-09

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 55.78  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  52 LFILRGLPGSGKSTLARVIVDRYrdGTKMVSADAY--KITPGARGDFS---EEYKRLDE---DLAAYCRRDVRVLVLDDT 123
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEEL--GAVRLSSDDErkRLFGEGRPSISyytDATDRTYErlhELARIALRAGRPVILDAT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953095599 124 NHERERLEQLFELADQYQYQVVLVEPKTAWrldcAQLKEKNQ 165
Cdd:pfam13671  79 NLRRDERARLLALAREYGVPVRIVVFEAPE----EVLRERLA 116
pseT PHA02530
polynucleotide kinase; Provisional
 50-147 1.21e-08

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 56.18  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  50 KTLFILRGLPGSGKSTLARVIVDRYRdGTKMVSADAYKIT---PGARGDFSeeYKRLDEDLAAYCRRDVRVL-------- 118
Cdd:PHA02530    2 MKIILTVGVPGSGKSTWAREFAAKNP-KAVNVNRDDLRQSlfgHGEWGEYK--FTKEKEDLVTKAQEAAALAalksgksv 78

                          90       100
                  ....*....|....*....|....*....
gi 1953095599 119 VLDDTNHERERLEQLFELADQYQYQVVLV 147
Cdd:PHA02530   79 IISDTNLNPERRRKWKELAKELGAEFEEK 107
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
52-148 2.15e-07

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 50.30  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  52 LFILRGLPGSGKSTLARVIVDRYrdGTKMVSADA-----YKITPGARGDFSE----EYKRLDEDLAAYCRRDVRVlVLDD 122
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERL--GAVRLRSDVvrkrlFGAGLAPLERSPEatarTYARLLALARELLAAGRSV-ILDA 77

                          90       100
                  ....*....|....*....|....*.
gi 1953095599 123 TNHERERLEQLFELADQYQYQVVLVE 148
Cdd:COG0645    78 TFLRRAQREAFRALAEEAGAPFVLIW 103
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 51-149 5.27e-07

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 49.34  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  51 TLFILRGLPGSGKSTLARVIVDRYR---DGTKMVSADAYKITPGARGDFSEEYKRLDEDLAAYCRRDVR----VLVLDDT 123
Cdd:COG4088     5 MLLILTGPPGSGKTTFAKALAQRLYaegIAVALLHSDDFRRFLVNESFPKETYEEVVEDVRTTTADNALdngySVIVDGT 84

                          90       100
                  ....*....|....*....|....*..
gi 1953095599 124 NHERERLEQLFELA-DQYQYQVVLVEP 149
Cdd:COG4088    85 FYYRSWQRDFRNLAkHKAPIHIIYLKA 111
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 57-147 1.90e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 40.68  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  57 GLPGSGKSTL------ARVIVDRY----RDG-TKMVSADAYKI----TPGARGDFSEEYkRLDEDLAAYCRRDVRVLVLD 121
Cdd:pfam01926   6 GRPNVGKSTLinaltgAKAIVSDYpgttRDPnEGRLELKGKQIilvdTPGLIEGASEGE-GLGRAFLAIIEADLILFVVD 84

                          90       100
                  ....*....|....*....|....*.
gi 1953095599 122 DTNHERERLEQLFELADQYQYQVVLV 147
Cdd:pfam01926  85 SEEGITPLDEELLELLRENKKPIILV 110
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 53-132 3.19e-04

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: 40.98  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  53 FILRGLPGSGKSTLARVIVDR-YRDGTKMVSADAYKITPGARGDFSEEYKRLDEDLAAYCRRDVRVLVLDDTNHERERLE 131
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANElFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQ 101


                  .
gi 1953095599 132 Q 132
Cdd:cd00009   102 N 102
PRK06762 PRK06762
hypothetical protein; Provisional
 51-84 8.70e-04

hypothetical protein; Provisional


Pssm-ID: 235858  Cd Length: 166  Bit Score: 39.95  E-value: 8.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953095599  51 TLFILRGLPGSGKSTLARVIVDRYRDGTKMVSAD 84
Cdd:PRK06762    3 TLIIIRGNSGSGKTTIAKQLQERLGRGTLLVSQD 36
AAA_18 pfam13238
AAA domain;
54-154 8.73e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 39.33  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  54 ILRGLPGSGKSTLARVIVDRYRDGTKMVSADAYKITPGARGDFSEEYKRLDEDLAAY---------CRRDVRVLVLDDTn 124
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRESKRLDEDKLDRlldlleenaALEEGGNLIIDGH- 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1953095599 125 hereRLEQLFELADQYQYQVVLVEPKTAWR 154
Cdd:pfam13238  81 ----LAELEPERAKDLVGIVLRASPEELLE 106
PRK04182 PRK04182
cytidylate kinase; Provisional
 57-83 3.54e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 38.25  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*..
gi 1953095599  57 GLPGSGKSTLARVIVDRYrdGTKMVSA 83
Cdd:PRK04182    7 GPPGSGKTTVARLLAEKL--GLKHVSA 31
AAA_22 pfam13401
AAA domain;
50-147 5.26e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  50 KTLFILRGLPGSGKSTLARvivdRYRDGTKMVSADAYKITP-----------------GARGDFSEEYKRLDEDLAAYC- 111
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLR----RLLEQLPEVRDSVVFVDLpsgtspkdllrallralGLPLSGRLSKEELLAALQQLLl 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953095599 112 -RRDVRVLVLDDTNH-ERERLEQLFELADQYQY--QVVLV 147
Cdd:pfam13401  81 aLAVAVVLIIDEAQHlSLEALEELRDLLNLSSKllQLILV 120
DUF87 pfam01935
Helicase HerA, central domain; This entry represents the central domain found in archaeal ...
 60-219 5.62e-03

Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.


Pssm-ID: 376671 [Multi-domain]  Cd Length: 220  Bit Score: 38.12  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  60 GSGKSTLARVIVDR--YRDGTKMVSADAYkitpGargdfseEYKRLDEDLAAYcrrDVRVLVLDDT---NHERERLEQLF 134
Cdd:pfam01935  33 GSGKSNTVAVLLEEllEKKGATVLIFDPH----G-------EYGTLFRDLGAE---NVNVITPDPElkiNPWLLSPEDLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599 135 ELAD-----QYQYQVVLVEpkTAWRldcaQLKEKNQWQLSADELkklkpgLEKDFLPLYFGWFLTKKSSESLRKAGQAFL 209
Cdd:pfam01935  99 DLLEelnlpNAEVQRSILE--EALD----QLKSEELGKLSIDEL------IEKILEELLTEAAELNKLSNDAIRRVLDKL 166

                         170
                  ....*....|
gi 1953095599 210 EELGNHKAFK 219
Cdd:pfam01935 167 ERLLRSGGLI 176
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 38-148 5.95e-03

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 38.09  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599  38 QDEETVATLQECKTLFILRGLPGSGKSTLARVI---------------VDRYRDGTKMVSADAYKITPgargdFSEEYKR 102
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLtrylnwlgvptkvfnVGEYRRSAVKAYSNYEFFRP-----DNPEAMK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953095599 103 LDEDLAAYCRRDVR---------VLVLDDTNHERERLEQLFELADQYQYQVVLVE 148
Cdd:pfam01591  76 IREQCALAALKDVLaylneesgqVAIFDATNTTRERRKNILDFAEENGLKVFFLE 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 54-147 6.34e-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: 36.97  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953095599   54 ILRGLPGSGKSTLARVIVDRY-RDGTKMVSADaykitpgarGDFSEEYKRLDedlaaycRRDVRVLVLDDTNHERERLEQ 132
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELgPPGGGVIYID---------GEDILEEVLDQ-------LLLIIVGGKKASGSGELRLRL 69

                           90
                   ....*....|....*
gi 1953095599  133 LFELADQYQYQVVLV 147
Cdd:smart00382  70 ALALARKLKPDVLIL 84
 
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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