NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15029671|gb|AAH11046|]
View 

CNP protein [Homo sapiens]

Protein Classification

NUDIX hydrolase( domain architecture ID 13597307)

NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg2+ or Mn2+ for its activity; contains an AAA domain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 166-379 1.60e-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: 1.60e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   166 LPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRQFVPGDEPREKMDLVTYFGKRPPGVLHCTTKFCDYGKAPGA 245
Cdd:pfam05881   1 LPLYFGWFLTKKSSEALRKTGQVFLEELGNHKAFKKELRHFQSGDEPKEKIDLTSYFGKRPPGVLHCTTKFCDYGKAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   246 EEYAQQDVLKKSYSKAFTLTISALFVTPKTTGARVELSEQQLQLWPSDVDKLSPTDNLPRGSRAHITLGCAADVEAVQTG 325
Cdd:pfam05881  81 EEYAQQDVVKKSYGKAFTLSISALFVTPKTVGARVELNEQQLALWPADVDKLSPSDSLPKGSRAHVTLGCASDVEAVQTG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15029671   326 LDLLEILRQEKGGSRGEEVGELSRGKLYSLGNGRWMLTLAKNMEVRAIFTGYYG 379
Cdd:pfam05881 161 LDLLEIVKLEKGGSQGEEVGELGRGKLQSLGNGRWMLSLAKKIEVRAIFSGYYG 214
COG4639 super family cl44097
Predicted kinase [General function prediction only];
30-128 1.12e-12

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: 64.85  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  30 KTLFILRGLPGSGKSTLARvivdKYRDGTKMVSADAY----KITPGARGAFSEEYKRLDEDLAAYCRRRdiRILVLDDTN 105
Cdd:COG4639   2 LSLVVLIGLPGSGKSTFAR----RLFAPTEVVSSDDIrallGGDENDQSAWGDVFQLAHEIARARLRAG--RLTVVDATN 75

                        90       100
                ....*....|....*....|...
gi 15029671 106 HERERLEQLFEMADQYQYQVVLV 128
Cdd:COG4639  76 LQREARRRLLALARAYGALVVAV 98
 
Name Accession Description Interval E-value
CNPase pfam05881
2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the ...
 166-379 1.60e-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: 1.60e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   166 LPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRQFVPGDEPREKMDLVTYFGKRPPGVLHCTTKFCDYGKAPGA 245
Cdd:pfam05881   1 LPLYFGWFLTKKSSEALRKTGQVFLEELGNHKAFKKELRHFQSGDEPKEKIDLTSYFGKRPPGVLHCTTKFCDYGKAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   246 EEYAQQDVLKKSYSKAFTLTISALFVTPKTTGARVELSEQQLQLWPSDVDKLSPTDNLPRGSRAHITLGCAADVEAVQTG 325
Cdd:pfam05881  81 EEYAQQDVVKKSYGKAFTLSISALFVTPKTVGARVELNEQQLALWPADVDKLSPSDSLPKGSRAHVTLGCASDVEAVQTG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15029671   326 LDLLEILRQEKGGSRGEEVGELSRGKLYSLGNGRWMLTLAKNMEVRAIFTGYYG 379
Cdd:pfam05881 161 LDLLEIVKLEKGGSQGEEVGELGRGKLQSLGNGRWMLSLAKKIEVRAIFSGYYG 214
COG4639 COG4639
Predicted kinase [General function prediction only];
30-128 1.12e-12

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 64.85  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  30 KTLFILRGLPGSGKSTLARvivdKYRDGTKMVSADAY----KITPGARGAFSEEYKRLDEDLAAYCRRRdiRILVLDDTN 105
Cdd:COG4639   2 LSLVVLIGLPGSGKSTFAR----RLFAPTEVVSSDDIrallGGDENDQSAWGDVFQLAHEIARARLRAG--RLTVVDATN 75

                        90       100
                ....*....|....*....|...
gi 15029671 106 HERERLEQLFEMADQYQYQVVLV 128
Cdd:COG4639  76 LQREARRRLLALARAYGALVVAV 98
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 32-146 1.40e-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: 56.16  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671    32 LFILRGLPGSGKSTLARVIV----------DKYRdgTKMVSADAYKITPGARgAFSEEYKRLDEDLAAYCRRRdiRILVL 101
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLeelgavrlssDDER--KRLFGEGRPSISYYTD-ATDRTYERLHELARIALRAG--RPVIL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15029671   102 DDTNHERERLEQLFEMADQYQYQVVLVEPKTAWrldcAQLKEKNQ 146
Cdd:pfam13671  76 DATNLRRDERARLLALAREYGVPVRIVVFEAPE----EVLRERLA 116
pseT PHA02530
polynucleotide kinase; Provisional
 30-128 4.48e-07

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 51.18  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   30 KTLFILRGLPGSGKSTLARVIVDKYRdGTKMVSADAYKITP-GARGAFSEEYKRLDEDL----------AAYCRRRDIri 98
Cdd:PHA02530   2 MKIILTVGVPGSGKSTWAREFAAKNP-KAVNVNRDDLRQSLfGHGEWGEYKFTKEKEDLvtkaqeaaalAALKSGKSV-- 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 15029671   99 lVLDDTNHERERLEQLFEMADQYQYQVVLV 128
Cdd:PHA02530  79 -IISDTNLNPERRRKWKELAKELGAEFEEK 107
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 33-118 2.32e-03

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: 38.28  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  33 FILRGLPGSGKSTLARVIVDK-YRDGTKMVSADAYKITPGARGAFSEEYkRLDEDLAAYCRRRDIRILVLDDTNHERERL 111
Cdd:cd00009  22 LLLYGPPGTGKTTLARAIANElFRPGAPFLYLNASDLLEGLVVAELFGH-FLVRLLFELAEKAKPGVLFIDEIDSLSRGA 100


                ....*..
gi 15029671 112 EQLFEMA 118
Cdd:cd00009 101 QNALLRV 107
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 34-122 8.59e-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: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671     34 ILRGLPGSGKSTLARVIVDKY-RDGTKMVSADAYKITPGARGAFSEEYKRLD----------EDLAAYCRRRDIRILVLD 102
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQLLLIIVGGKkasgsgelrlRLALALARKLKPDVLILD 85

                           90       100
                   ....*....|....*....|.
gi 15029671    103 D-TNHERERLEQLFEMADQYQ 122
Cdd:smart00382  86 EiTSLLDAEQEALLLLLEELR 106
 
Name Accession Description Interval E-value
CNPase pfam05881
2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase); This family consists of the ...
 166-379 1.60e-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: 1.60e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   166 LPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRQFVPGDEPREKMDLVTYFGKRPPGVLHCTTKFCDYGKAPGA 245
Cdd:pfam05881   1 LPLYFGWFLTKKSSEALRKTGQVFLEELGNHKAFKKELRHFQSGDEPKEKIDLTSYFGKRPPGVLHCTTKFCDYGKAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   246 EEYAQQDVLKKSYSKAFTLTISALFVTPKTTGARVELSEQQLQLWPSDVDKLSPTDNLPRGSRAHITLGCAADVEAVQTG 325
Cdd:pfam05881  81 EEYAQQDVVKKSYGKAFTLSISALFVTPKTVGARVELNEQQLALWPADVDKLSPSDSLPKGSRAHVTLGCASDVEAVQTG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15029671   326 LDLLEILRQEKGGSRGEEVGELSRGKLYSLGNGRWMLTLAKNMEVRAIFTGYYG 379
Cdd:pfam05881 161 LDLLEIVKLEKGGSQGEEVGELGRGKLQSLGNGRWMLSLAKKIEVRAIFSGYYG 214
COG4639 COG4639
Predicted kinase [General function prediction only];
30-128 1.12e-12

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 64.85  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  30 KTLFILRGLPGSGKSTLARvivdKYRDGTKMVSADAY----KITPGARGAFSEEYKRLDEDLAAYCRRRdiRILVLDDTN 105
Cdd:COG4639   2 LSLVVLIGLPGSGKSTFAR----RLFAPTEVVSSDDIrallGGDENDQSAWGDVFQLAHEIARARLRAG--RLTVVDATN 75

                        90       100
                ....*....|....*....|...
gi 15029671 106 HERERLEQLFEMADQYQYQVVLV 128
Cdd:COG4639  76 LQREARRRLLALARAYGALVVAV 98
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 32-146 1.40e-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: 56.16  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671    32 LFILRGLPGSGKSTLARVIV----------DKYRdgTKMVSADAYKITPGARgAFSEEYKRLDEDLAAYCRRRdiRILVL 101
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLeelgavrlssDDER--KRLFGEGRPSISYYTD-ATDRTYERLHELARIALRAG--RPVIL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15029671   102 DDTNHERERLEQLFEMADQYQYQVVLVEPKTAWrldcAQLKEKNQ 146
Cdd:pfam13671  76 DATNLRRDERARLLALAREYGVPVRIVVFEAPE----EVLRERLA 116
pseT PHA02530
polynucleotide kinase; Provisional
 30-128 4.48e-07

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 51.18  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671   30 KTLFILRGLPGSGKSTLARVIVDKYRdGTKMVSADAYKITP-GARGAFSEEYKRLDEDL----------AAYCRRRDIri 98
Cdd:PHA02530   2 MKIILTVGVPGSGKSTWAREFAAKNP-KAVNVNRDDLRQSLfGHGEWGEYKFTKEKEDLvtkaqeaaalAALKSGKSV-- 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 15029671   99 lVLDDTNHERERLEQLFEMADQYQYQVVLV 128
Cdd:PHA02530  79 -IISDTNLNPERRRKWKELAKELGAEFEEK 107
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 31-130 2.13e-06

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: 47.80  E-value: 2.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  31 TLFILRGLPGSGKSTLARVIVDKYR---DGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAYCRRRDIR---ILVLDDT 104
Cdd:COG4088   5 MLLILTGPPGSGKTTFAKALAQRLYaegIAVALLHSDDFRRFLVNESFPKETYEEVVEDVRTTTADNALDngySVIVDGT 84

                        90       100
                ....*....|....*....|....*..
gi 15029671 105 NHERERLEQLFEMA-DQYQYQVVLVEP 130
Cdd:COG4088  85 FYYRSWQRDFRNLAkHKAPIHIIYLKA 111
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
32-129 2.56e-05

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 44.13  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  32 LFILRGLPGSGKSTLARVIVDkyRDGTKMVSADaykitpgargafsEEYKRL-DEDLAAYCRRRDIRIL----------- 99
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAE--RLGAVRLRSD-------------VVRKRLfGAGLAPLERSPEATARtyarllalare 65

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15029671 100 --------VLDDTNHERERLEQLFEMADQYQYQVVLVE 129
Cdd:COG0645  66 llaagrsvILDATFLRRAQREAFRALAEEAGAPFVLIW 103
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 37-128 9.15e-05

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: 41.45  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671    37 GLPGSGKSTL------ARVIVDKY----RDG-TKMVSADAYKI----TPGARGAFSEEYKRLDEDLAAycRRRDIRILVL 101
Cdd:pfam01926   6 GRPNVGKSTLinaltgAKAIVSDYpgttRDPnEGRLELKGKQIilvdTPGLIEGASEGEGLGRAFLAI--IEADLILFVV 83

                          90       100
                  ....*....|....*....|....*..
gi 15029671   102 DDTNHERERLEQLFEMADQYQYQVVLV 128
Cdd:pfam01926  84 DSEEGITPLDEELLELLRENKKPIILV 110
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 18-129 4.50e-04

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: 41.17  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671    18 QDEDTVATLLECKTLFILRGLPGSGKSTLARVI---------------VDKYRDGTKMVSADAYKITP-GARG-AFSEEY 80
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLtrylnwlgvptkvfnVGEYRRSAVKAYSNYEFFRPdNPEAmKIREQC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15029671    81 KRLD-EDLAAYCRRRDIRILVLDDTNHERERLEQLFEMADQYQYQVVLVE 129
Cdd:pfam01591  81 ALAAlKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLE 130
AAA_18 pfam13238
AAA domain;
34-135 5.79e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 39.72  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671    34 ILRGLPGSGKSTLARVIVDKYRDGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAY--------CRRRDIRILVLDDTn 105
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRESKRLDEDKLDRlldlleenAALEEGGNLIIDGH- 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 15029671   106 hereRLEQLFEMADQYQYQVVLVEPKTAWR 135
Cdd:pfam13238  81 ----LAELEPERAKDLVGIVLRASPEELLE 106
PRK04182 PRK04182
cytidylate kinase; Provisional
 37-63 2.27e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 38.63  E-value: 2.27e-03
                         10        20
                 ....*....|....*....|....*..
gi 15029671   37 GLPGSGKSTLARVIVDKYrdGTKMVSA 63
Cdd:PRK04182   7 GPPGSGKTTVARLLAEKL--GLKHVSA 31
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 33-118 2.32e-03

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: 38.28  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  33 FILRGLPGSGKSTLARVIVDK-YRDGTKMVSADAYKITPGARGAFSEEYkRLDEDLAAYCRRRDIRILVLDDTNHERERL 111
Cdd:cd00009  22 LLLYGPPGTGKTTLARAIANElFRPGAPFLYLNASDLLEGLVVAELFGH-FLVRLLFELAEKAKPGVLFIDEIDSLSRGA 100


                ....*..
gi 15029671 112 EQLFEMA 118
Cdd:cd00009 101 QNALLRV 107
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 37-145 3.22e-03

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: 38.21  E-value: 3.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671  37 GLPGSGKSTLARVIVDKYRD--------------GTKMVSADAYKI----TPgarGAFSEEYKRLDEDLAAYCRRRDIRI 98
Cdd:cd00882   4 GRGGVGKSSLLNALLGGEVGevsdvpgttrdpdvYVKELDKGKVKLvlvdTP---GLDEFGGLGREELARLLLRGADLIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15029671  99 LVLDDTNHERERLEQLFEMADQYQYQ----VV-----LVEPKTAWRLDCAQLKEKN 145
Cdd:cd00882  81 LVVDSTDRESEEDAKLLILRRLRKEGipiiLVgnkidLLEEREVEELLRLEELAKI 136
PRK06762 PRK06762
hypothetical protein; Provisional
 31-64 3.24e-03

hypothetical protein; Provisional


Pssm-ID: 235858  Cd Length: 166  Bit Score: 38.03  E-value: 3.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15029671   31 TLFILRGLPGSGKSTLARVIVDKYRDGTKMVSAD 64
Cdd:PRK06762   3 TLIIIRGNSGSGKTTIAKQLQERLGRGTLLVSQD 36
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 34-122 8.59e-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: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029671     34 ILRGLPGSGKSTLARVIVDKY-RDGTKMVSADAYKITPGARGAFSEEYKRLD----------EDLAAYCRRRDIRILVLD 102
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQLLLIIVGGKkasgsgelrlRLALALARKLKPDVLILD 85

                           90       100
                   ....*....|....*....|.
gi 15029671    103 D-TNHERERLEQLFEMADQYQ 122
Cdd:smart00382  86 EiTSLLDAEQEALLLLLEELR 106
AAA_17 pfam13207
AAA domain;
37-63 8.63e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 36.45  E-value: 8.63e-03
                          10        20
                  ....*....|....*....|....*..
gi 15029671    37 GLPGSGKSTLARVIVDKYrdGTKMVSA 63
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKL--GFPHISA 26
 
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