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Conserved domains on  [gi|2462521995|ref|XP_054223192|]
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ectonucleoside triphosphate diphosphohydrolase 1 isoform X11 [Homo sapiens]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 55-287 1.28e-168

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24110:

Pssm-ID: 483947  Cd Length: 422  Bit Score: 473.51  E-value: 1.28e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  55 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQ 134
Cdd:cd24110     1 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVQQLEECKVKGPGISSYSQKTTKAGASLAECMKKAKEVIPASQHH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 135 ETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSiVPYE 214
Cdd:cd24110    81 ETPVYLGATAGMRLLRMESEQAAEEVLASVERSLKSYPFDFQGARIITGQEEGAYGWITINYLLGNFKQDSGWFT-QLSG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521995 215 TNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQMPSA 287
Cdd:cd24110   160 GKPTETFGALDLGGASTQITFVPLNSTIESPENSLQFRLYGTDYTVYTHSFLCYGKDQALWQKLAQDIQSTSG 232
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
 55-287 1.28e-168

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and similar proteins; NTPDase1 (EC 3.6.1.5), also called Ecto-ATP diphosphohydrolase 1, Ecto-ATPDase 1, Ecto-ATPase 1, Ecto-apyrase, or lymphoid cell activation antigen CD39, is a known E-type apyrase that could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission in the nervous system. It could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. NTPDase1 hydrolyzes ATP and ADP equally well. In addition, NTPDase1 can also hydrolyze ATP to AMP without the release of ADP.


Pssm-ID: 466960  Cd Length: 422  Bit Score: 473.51  E-value: 1.28e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  55 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQ 134
Cdd:cd24110     1 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVQQLEECKVKGPGISSYSQKTTKAGASLAECMKKAKEVIPASQHH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 135 ETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSiVPYE 214
Cdd:cd24110    81 ETPVYLGATAGMRLLRMESEQAAEEVLASVERSLKSYPFDFQGARIITGQEEGAYGWITINYLLGNFKQDSGWFT-QLSG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521995 215 TNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQMPSA 287
Cdd:cd24110   160 GKPTETFGALDLGGASTQITFVPLNSTIESPENSLQFRLYGTDYTVYTHSFLCYGKDQALWQKLAQDIQSTSG 232
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
52-283 2.13e-129

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 373.68  E-value: 2.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  52 NKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRS 131
Cdd:pfam01150   1 NLALPENVKYGIIIDAGSSGTRLHVYKWPDEKEGLTPIVPLIEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 132 QHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFsqktrwfsiv 211
Cdd:pfam01150  81 KRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNF---------- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521995 212 pyETNNQETFGALDLGGASTQVTFVP-----QNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQ 283
Cdd:pfam01150 151 --GKPKQSTFGAIDLGGASTQIAFEPsnesaINSTVEDIELGLQFRLYDKDYTLYVHSFLGYGANEALRKYLAKLIQ 225
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
 55-287 1.28e-168

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and similar proteins; NTPDase1 (EC 3.6.1.5), also called Ecto-ATP diphosphohydrolase 1, Ecto-ATPDase 1, Ecto-ATPase 1, Ecto-apyrase, or lymphoid cell activation antigen CD39, is a known E-type apyrase that could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission in the nervous system. It could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. NTPDase1 hydrolyzes ATP and ADP equally well. In addition, NTPDase1 can also hydrolyze ATP to AMP without the release of ADP.


Pssm-ID: 466960  Cd Length: 422  Bit Score: 473.51  E-value: 1.28e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  55 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQ 134
Cdd:cd24110     1 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVQQLEECKVKGPGISSYSQKTTKAGASLAECMKKAKEVIPASQHH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 135 ETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSiVPYE 214
Cdd:cd24110    81 ETPVYLGATAGMRLLRMESEQAAEEVLASVERSLKSYPFDFQGARIITGQEEGAYGWITINYLLGNFKQDSGWFT-QLSG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521995 215 TNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQMPSA 287
Cdd:cd24110   160 GKPTETFGALDLGGASTQITFVPLNSTIESPENSLQFRLYGTDYTVYTHSFLCYGKDQALWQKLAQDIQSTSG 232
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
52-283 2.13e-129

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 373.68  E-value: 2.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  52 NKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRS 131
Cdd:pfam01150   1 NLALPENVKYGIIIDAGSSGTRLHVYKWPDEKEGLTPIVPLIEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 132 QHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFsqktrwfsiv 211
Cdd:pfam01150  81 KRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNF---------- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521995 212 pyETNNQETFGALDLGGASTQVTFVP-----QNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQ 283
Cdd:pfam01150 151 --GKPKQSTFGAIDLGGASTQIAFEPsnesaINSTVEDIELGLQFRLYDKDYTLYVHSFLGYGANEALRKYLAKLIQ 225
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
 61-283 1.96e-114

nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1)-like subfamily; The NTPDase1-like subfamily includes NTPDases 1, 2, 3 and 8, which are localized to the cell surface with their catalytic domain facing the extracellular matrix. They are the ecto-apyrase group with NTPase activities. They participate in the regulation of purinergic signaling mediated by extracellular ATP and/or ADP (eATP and eADP) through the degradation of eATP and/or eADP into AMP.


Pssm-ID: 466894  Cd Length: 411  Bit Score: 335.79  E-value: 1.96e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPVYL 140
Cdd:cd24044     1 YGIVIDAGSSHTSLFVYKWPADKENGTGVVQQVSTCRVKGGGISSYENNPSQAGESLEPCLDQAKKKVPEDRRHSTPLYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 141 GATAGMRLLRMESEELADRVLDVVERSLSNY--PFDFQGARIITGQEEGAYGWITINYLLGKFSQktrwFSIVPYETNNQ 218
Cdd:cd24044    81 GATAGMRLLNLTNPSAADAILESVRDALKSSkfGFDFRNARILSGEDEGLYGWITVNYLLGNLGK----YSISSIPRSRP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521995 219 ETFGALDLGGASTQVTFVPQNQTIESPDNaLQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQ 283
Cdd:cd24044   157 ETVGALDLGGASTQITFEPAEPSLPADYT-RKLRLYGKDYNVYTHSYLCYGKDEAERRYLASLVQ 220
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
 36-283 4.10e-112

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) and similar proteins; NTPDase8 (EC 3.6.1.5), also called E-NTPDase 8, or NTPDase 8, is a canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. NTPDase8 has activity toward ATP, ADP, UTP and UDP, but not toward AMP.


Pssm-ID: 466963  Cd Length: 433  Bit Score: 330.57  E-value: 4.10e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  36 SSIIAVIaLLAVGLtQNKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGI 115
Cdd:cd24113     2 SGIIALI-LSLVEI-QDVFLPPGIKYGIVFDAGSSHTSLFLYQWPADKENGTGIVSQVLSCDVEGPGISSYAQNPAKAGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 116 YLTDCMERAREVIPRSQHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITIN 195
Cdd:cd24113    80 SLKPCLDEALAAIPAEQQKETPVYLGATAGMRLLRLQNSTQSDEILAEVSKTIGSYPFDFQGARILTGMEEGAYGWITVN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 196 YLLG---KFSQKTRWfsIVPYETNnqeTFGALDLGGASTQVTFVPqNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQ 272
Cdd:cd24113   160 YLLEtfiKYSFEGKW--IHPKGGN---ILGALDLGGASTQITFVP-GGPIEDKNTEANFRLYGYNYTVYTHSYLCYGKDQ 233

                         250
                  ....*....|.
gi 2462521995 273 ALWQKLAKDIQ 283
Cdd:cd24113   234 MLKRLLAALLQ 244
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
 59-283 4.08e-105

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) and similar proteins; NTPDase2 (EC 3.6.1.-), also called CD39 antigen-like 1 (CD39L1), Ecto-ATP diphosphohydrolase 2 (ENTPD2), Ecto-ATPDase 2, or Ecto-ATPase 2, has E-type ecto-ATPase activity, by hydrolyzing extracellular ATP and other nucleotides to regulate purinergic neurotransmission in the nervous system. It hydrolyzes ADP only to a marginal extent.


Pssm-ID: 466961  Cd Length: 418  Bit Score: 312.06  E-value: 4.08e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  59 VKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPV 138
Cdd:cd24111     2 LKYGIVLDAGSSHTSMFVYKWPADKENDTGIVSQHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 139 YLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKT---RWFsivpyeT 215
Cdd:cd24111    82 YLGATAGMRLLNLTSPEASARVLEAVTQTLTSYPFDFRGARILSGQEEGVFGWVTANYLLENFIKYGwvgQWI------R 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521995 216 NNQETFGALDLGGASTQVTFVpQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQ 283
Cdd:cd24111   156 PRKGTLGAMDLGGASTQITFE-TTSPSEDPGNEVHLRLYGQHYRVYTHSFLCYGRDQVLLRLLASALQ 222
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
 61-286 2.84e-95

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) and similar proteins; NTPDase3 (EC 3.6.1.5), also called CD39 antigen-like 3 (CD39L3), Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, or HB6, has a threefold preference for the hydrolysis of ATP over ADP.


Pssm-ID: 466962  Cd Length: 411  Bit Score: 286.67  E-value: 2.84e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPVYL 140
Cdd:cd24112     1 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTYKCNVKGPGISSYAHNPQKAARALEECMNKVKEIIPSHLHNSTPVYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 141 GATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSIV-PYetnNQE 219
Cdd:cd24112    81 GATAGMRLLKLQNETAANEVLSSIENYFKTLPFDFRGAHIITGQEEGVYGWITANYLMGNFLEKNLWNAWVhPH---GVE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521995 220 TFGALDLGGASTQVTFVPQNQTiESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQMPS 286
Cdd:cd24112   158 TVGALDLGGASTQIAFIPEDSL-ENLNDTVKVSLYGYKYNVYTHSFQCYGKDEAEKRFLANLAQASE 223
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 61-274 8.78e-75

nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family contains a group of apyrases (also known as adenylpyrophophatase, or ATP-diphosphohydrolases; EC 3.6.1.5), which are enzymes that catalyze the hydrolysis of phosphoanhydride bonds of nucleoside tri- and diphosphates (NTPs and NDPs) in the presence of divalent cations. In vertebrate systems, especially in mammals, apyrases are more widely referred to as nucleoside triphosphate diphosphohydrolases (NTPDases). There are eight homologs of NTPDases (NTPDases 1-8) in mammals, two apyrase enzymes from yeast, GDA1 and YND1, and a total of seven homologs of apyrase, namely AtAPY1-7, found in Arabidopsis. The GDA1/CD39 NTPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466853  Cd Length: 332  Bit Score: 231.89  E-value: 8.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGI--SKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPV 138
Cdd:cd24003     1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIELVSSGKEKSGKIssSSYADDPDEAKKYLQPLLEFAKAVVPEDRRSSTPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 139 YLGATAGMRLLrmeSEELADRVLDVVERSLSNYPFDFQ--GARIITGQEEGAYGWITINYLLGKFSqktrwfsivpyETN 216
Cdd:cd24003    81 YLLATAGMRLL---PEEQQEAILDAVRTILRNSGFGFDdgWVRVISGEEEGLYGWLSVNYLLGNLG-----------SEP 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521995 217 NQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQAL 274
Cdd:cd24003   147 AKKTVGVLDLGGASTQIAFEPPEDDLSSLSNVYPLRLGGKTYDLYSHSFLGYGLNEAR 204
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
 61-266 4.70e-51

nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5)-like subfamily; The NTPDase5-like subfamily includes NTPDase5 and NTPDase6. NTPDase5 (EC 3.6.1.6), also called nucleoside diphosphate phosphatase ENTPD5, CD39 antigen-like 4 (CD39L4), ER-UDPase, guanosine-diphosphatase ENTPD5, GDPase ENTPD5, inosine diphosphate phosphatase ENTPD5, nucleoside diphosphatase, uridine-diphosphatase ENTPD5, or UDPase ENTPD5, hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP. NTPDase6 (EC 3.6.1.6), also called CD39 antigen-like 2 (CD39L2), catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. It has a strong preference for nucleoside diphosphates, preferentially hydrolyzes GDP, IDP, and UDP, with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP. The membrane bound form might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides.


Pssm-ID: 466896  Cd Length: 372  Bit Score: 171.59  E-value: 4.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKWpaEKENDTGVVHQVEEC--RVKgPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPV 138
Cdd:cd24046     1 YAIVFDAGSTGSRVHVFKF--SHSPSGGPLKLLDELfeEVK-PGLSSYADDPKEAADSLKPLLEKAKTRIPKEKWSSTPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 139 YLGATAGMRLLrmeSEELADRVLDVVERSLSNYPFDFQ--GARIITGQEEGAYGWITINYLLGKFSQKTrwfsivpyetn 216
Cdd:cd24046    78 ALKATAGLRLL---PEEKANAILDEVRKLFKKSPFLVGedSVSIMDGTDEGIFSWFTVNFLLGRLGGSA----------- 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521995 217 nQETFGALDLGGASTQVTFVPQNQT--IESPDNAL-QFRLYGKDYNVYTHSFL 266
Cdd:cd24046   144 -SNTVAALDLGGGSTQITFAPSDKEtlSASPKGYLhKVSIFGKKIKLYTHSYL 195
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
 60-273 1.71e-50

nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar proteins; YND1 (EC 3.6.1.5), also called Golgi apyrase, ATP-diphosphatase, ATP-diphosphohydrolase, adenosine diphosphatase, ADPase, or Golgi nucleoside diphosphatase, catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. YND1 is required for Golgi glycosylation and cell wall integrity.


Pssm-ID: 466889  Cd Length: 373  Bit Score: 170.23  E-value: 1.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  60 KYGIVLDAGSSHTSLYIYKW--PAEKENDT-----GVVHQVEECRVKG--------PGISKFVQKVNEIGIYLTDCMERA 124
Cdd:cd24039     2 KYGIVIDAGSSGSRVQIYSWkdPESATSKAsleelKSLPHIETGIGDGkdwtlkvePGISSFADHPHVVGEHLKPLLDFA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 125 REVIPRSQHQETPVYLGATAGMRLL-RMESEELADRVLDVVERslsNYPFDFQGA----RIITGQEEGAYGWITINYLLG 199
Cdd:cd24039    82 LNIIPPSVHSSTPIFLLATAGMRLLpQDQQNAILDAVCDYLRK---NYPFLLPDCsehvQVISGEEEGLYGWLAVNYLMG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 200 KFSQKTRwfsivPYETNNQETFGALDLGGASTQVTFVPQ-NQTIESPDNALQFRLYGKD-----YNVYTHSFLCYGKDQA 273
Cdd:cd24039   159 GFDDAPK-----HSIAHDHHTFGFLDMGGASTQIAFEPNaSAAKEHADDLKTVHLRTLDgsqveYPVFVTTWLGFGTNEA 233
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
 60-275 2.62e-46

nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 (NTPDase4)-like subfamily; The NTPDase4-like subfamily includes NTPDase4 and NTPDase7. NTPDase4 (EC 3.6.1.15/EC 3.6.1.6/EC 3.6.1.42), also called Golgi UDPase, lysosomal apyrase-like protein of 70 kDa (LALP70), uridine-diphosphatase (UDPase), is located in the Golgi. It catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner, with a preference for pyrimidines. It preferentially hydrolyzes UTP and TTP. NTPDase4 has at least one alternatively spliced variant, which has a broad substrate specificity with the ability of cleaving all nucleotide di- and triphosphates except for adenosine di- and triphosphate (ADP and ATP). It preferentially hydrolyzes CTP, UDP, CDP, GTP and GDP, and can use either calcium or magnesium equally. NTPDase7 (EC 3.6.1.15), also called lysosomal apyrase-like protein 1 (LALP1), is a novel mammalian endo-apyrase with substrate preference for nucleoside 5'-triphosphates UTP, GTP, and CTP.


Pssm-ID: 466895  Cd Length: 450  Bit Score: 161.32  E-value: 2.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  60 KYGIVLDAGSSHTSLYIYKWP--------------AEKENDTGVVHQVEecrvkgPGISKFVQKVNEIGIYLTDCMERAR 125
Cdd:cd24045     2 HYGVVIDCGSSGSRVFVYTWPrhsgnphelldikpLRDENGKPVVKKIK------PGLSSFADKPEKASDYLRPLLDFAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 126 EVIPRSQHQETPVYLGATAGMRLLrmeSEELADRVL-DVVERSLSNYPFDF--QGARIITGQEEGAYGWITINYLLGKFS 202
Cdd:cd24045    76 EHIPREKHKETPLYILATAGMRLL---PESQQEAILeDLRTDIPKHFNFLFsdSHAEVISGKQEGVYAWIAINYVLGRFD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 203 QKTRWFSIVPYETNNQE------TFGALDLGGASTQVTF-VPQNQTIESP---DNALQFRLYGKD------YNVYTHSFL 266
Cdd:cd24045   153 HSEDDDPAVVVVSDNKEailrkrTVGILDMGGASTQIAFeVPKTVEFASPvakNLLAEFNLGCDAhdtehvYRVYVTTFL 232


                  ....*....
gi 2462521995 267 CYGKDQALW 275
Cdd:cd24045   233 GYGANEARQ 241
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
 60-286 8.81e-45

nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate diphosphohydrolase I (Lp1NTPDase/Lpg1905) and similar proteins; The family corresponds to a group of proteins similar to Lp1NTPDase, which is a structural and functional homolog of the eukaryotic nucleoside triphosphate diphosphohydrolases (NTPDases) that control the extracellular levels of nucleotides (NTPs). Lp1NTPDase contributes to host-pathogen interactions through its NTPDase activity. Unlike most of the mammalian NTPDases, Lp1NTPDase is soluble and does not require membrane association to regulate its catalytic activity.


Pssm-ID: 466888  Cd Length: 346  Bit Score: 154.81  E-value: 8.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  60 KYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKgPGI-SKFVQKVNEigiYLTDCMERAREViprsQHQETPV 138
Cdd:cd24038     2 SCTAVIDAGSSGSRLHLYQYDTDDSNPPIHEIELKNNKIK-PGLaSVNTTDVDA---YLDPLFAKLPIA----KTSNIPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 139 YLGATAGMRLLrmeSEELADRVLDVVERSLSN-YPFDFQGARIITGQEEGAYGWITINYLLGKFSqktrwfsivpyetNN 217
Cdd:cd24038    74 YFYATAGMRLL---PPSEQKKLYQELKDWLAQqSKFQLVEAKTITGHMEGLYDWIAVNYLLDTLK-------------SS 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521995 218 QETFGALDLGGASTQVTFVPQNqtIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKL------AKDIQMPS 286
Cdd:cd24038   138 KKTVGVLDLGGASTQIAFAVPN--NASKDNTVEVKIGNKTINLYSHSYLGLGQDQARHQFLnnpdcfPKGYPLPS 210
ASKHA_NBD_AtAPY3-like cd24042
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar ...
 61-283 2.88e-44

nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar proteins; Apyrase (APY; EC 3.6.1.5), also called ATP-diphosphatase, ATP-diphosphohydrolase, adenosine diphosphatase, ADPase, NTPDase, or nucleoside triphosphate diphosphohydrolase, catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates (NTPs and NDPs). AtAPY3-5 exhibits a single putative N-terminal transmembrane domain typical of type II membrane proteins, whereas AtAPY6 appears to possess both an N- and a C- terminal transmembrane domain and to be type IV-A membrane protein. AtAPY5 exhibits the highest specific activities for NDPs of all the Arabidopsis apyrases. AtAPY4 may have the lowest NDPase activity, exhibiting a substrate preference for CTP. AtAPY6 plays an endo-apyrase role and is important in pollen exine formation.


Pssm-ID: 466892  Cd Length: 393  Bit Score: 154.52  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKWPAEkeNDTGVVHQVEE--CRVK-GPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETP 137
Cdd:cd24042     1 YSVIIDAGSSGTRLHVFGYAAE--SGKPVFPFGEKdyASLKtTPGLSSFADNPSGASASLTELLEFAKERVPKGKRKETD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 138 VYLGATAGMRLLRMeseELADRVLDVVERSLSNYPFDFQG--ARIITGQEEGAYGWITINYLLGKFSqktrwfsivpyeT 215
Cdd:cd24042    79 IRLMATAGLRLLEV---PVQEQILEVCRRVLRSSGFMFRDewASVISGTDEGIYAWVAANYALGSLG------------G 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521995 216 NNQETFGALDLGGASTQVTFVPQNQTieSPDNALQFRLYGKDYNVYTHSFLCYGKDQAlWQKLAKDIQ 283
Cdd:cd24042   144 DPLETTGIVELGGASAQVTFVPSEAV--PPEFSRTLVYGGVSYKLYSHSFLDFGQEAA-WDKLLESLL 208
ASKHA_NBD_AtAPY1-like cd24041
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), ...
 60-269 9.86e-41

nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), and similar proteins; Apyrase (APY; EC 3.6.1.5), also called ATP-diphosphatase, ATP-diphosphohydrolase, adenosine diphosphatase, ADPase, NTPDase, or nucleoside triphosphate diphosphohydrolase, catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates (NTPs and NDPs) in the presence of divalent cations. AtAPY1 and AtAPY2 are typical type II membrane proteins and function at the plasma membrane as ATPases and ADPases regulating ecto-ATP/ADP concentrations. They also act as endo-apyrases residing in the Golgi lumen with UDPase and GDPase activities. AtAPY1 and AtAPY2 play roles in the regulation of stomatal function by modulating extracellular ATP levels in guard cells. They work together to reduce extracellular ATP level which is essential for pollen germination and normal plant development.


Pssm-ID: 466891  Cd Length: 399  Bit Score: 145.54  E-value: 9.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  60 KYGIVLDAGSSHTSLYIYKWpaekENDTGVVH---QVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQET 136
Cdd:cd24041     1 RYAVVFDAGSTGSRVHVFKF----DQNLDLLHlglDLELFEQIKPGLSSYADDPEQAAKSLRPLLDKALAVVPEELQSKT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 137 PVYLGATAGMRLLrmeSEELADRVLDVVERSLSNYPFDFQ--GARIITGQEEGAYGWITINYLLGKFSQktrwfsivPYE 214
Cdd:cd24041    77 PVRLGATAGLRLL---PGDASENILQEVRDLLRNYSFKVQpdAVSIIDGTDEGSYQWVTVNYLLGNLGK--------PFT 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521995 215 tnnqETFGALDLGGASTQVTF-VPQNQTIESPDNALQFRLY-------GKDYNVYTHSFLCYG 269
Cdd:cd24041   146 ----KTVGVVDLGGGSVQMAYaVSDETAKNAPKPTDGEDGYirklvlkGKTYDLYVHSYLGYG 204
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
 61-273 1.93e-40

nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar proteins; Apyrase 7 (APY7; EC 3.6.1.5), also called ATP-diphosphatase, ATP-diphosphohydrolase, adenosine diphosphatase, ADPase, NTPDase, or nucleoside triphosphate diphosphohydrolase 7, catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates (NTPs and NDPs). AtAPY7 has been classified as a type IV-A membrane protein. It is important in pollen exine formation. AtAPY7 does not appear to function as a typical apyrase.


Pssm-ID: 466893  Cd Length: 418  Bit Score: 144.90  E-value: 1.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKW---------------------PAEKENDTGVVHQVEecrvKGPGISKFVQKVNEIGIYLTD 119
Cdd:cd24043     1 YAIVMDCGSTGTRVYVYSWarnpskdslpvmvdpptvasaALVKKPKKRAYKRVE----TEPGLDKLADNETGLGAALGP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 120 CMERAREVIPRSQHQETPVYLGATAGMRLLRmesEELADRVLDVVERSLSNYPFDFQG--ARIITGQEEGAYGWITINYL 197
Cdd:cd24043    77 LLDWAGKQIPRSQHPRTPVFLFATAGLRRLP---PDDSAWLLDKAWGVLEASPFRFERswVRIISGTEEAYYGWIALNYL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521995 198 LGKFSQktrwfsivpyETNNQETFGALDLGGASTQVTFVPQNQTieSPDNALQFRLYGKDYNVYTHSFLCYGKDQA 273
Cdd:cd24043   154 TGRLGQ----------GPGKGATVGSLDLGGSSLEVTFEPEAVP--RGEYGVNLSVGSTEHHLYAHSHAGYGLNDA 217
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
 61-269 1.54e-37

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) and similar proteins; NTPDase5 (EC 3.6.1.6), also called nucleoside diphosphate phosphatase ENTPD5, CD39 antigen-like 4 (CD39L4), ER-UDPase, guanosine-diphosphatase ENTPD5, GDPase ENTPD5, inosine diphosphate phosphatase ENTPD5, nucleoside diphosphatase, uridine-diphosphatase ENTPD5, or UDPase ENTPD5, hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP.


Pssm-ID: 466964  Cd Length: 375  Bit Score: 136.48  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKW----PAE-KENDTGVVHQVEecrvkgPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQE 135
Cdd:cd24114     3 YGIMFDAGSTGTRIHIYTFvqksPAElPELDGEIFESVK------PGLSAYADQPEQGAETVRGLLDVAKKTIPSTQWKK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 136 TPVYLGATAGMRLLrmeSEELADRVLDVVERSLSNYPFDF--QGARIITGQEEGAYGWITINYLLGKFSQKtrwfsivpy 213
Cdd:cd24114    77 TPVVLKATAGLRLL---PEEKAQALLSEVKEIFEESPFLVpeGSVSIMNGTYEGILAWVTVNFLTGQLYGQ--------- 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521995 214 etnNQETFGALDLGGASTQVTFVPQ-NQTIE-SPDNAL-QFRLYGKDYNVYTHSFLCYG 269
Cdd:cd24114   145 ---NQRTVGILDLGGASTQITFLPRfEKTLKqAPEDYLtSFEMFNSTYKLYTHSYLGFG 200
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
 59-269 6.28e-33

nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) and similar proteins; NTPDase6 (EC 3.6.1.6), also called CD39 antigen-like 2 (CD39L2), catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. It has a strong preference for nucleoside diphosphates, preferentially hydrolyzes GDP, IDP, and UDP, with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP. The membrane bound form might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides.


Pssm-ID: 466965  Cd Length: 374  Bit Score: 124.16  E-value: 6.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  59 VKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHqvEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPV 138
Cdd:cd24115     1 VFYGIMFDAGSTGTRIHIFKFTRPPNEAPKLTH--ETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDFWKATPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 139 YLGATAGMRLLRMESeelADRVLDVVERSLSNYPFDFQ--GARIITGQEEGAYGWITINYLLGKFsqktrwfsivpyETN 216
Cdd:cd24115    79 VLKATAGLRLLPGEK---AQKLLDKVKEVFKASPFLVGddSVSIMDGTDEGISAWITVNFLTGSL------------HGT 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521995 217 NQETFGALDLGGASTQVTFVPQNQ-TIES--PDNALQFRLYGKDYNVYTHSFLCYG 269
Cdd:cd24115   144 GRSSVGMLDLGGGSTQITFSPHSEgTLQTspIDYITSFQMFNRTYTLYSHSYLGLG 199
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
 61-282 1.40e-32

nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; After transfer of sugars to endogenous macromolecular acceptors, GDA1 (EC 3.6.1.42), also called GDPase, converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.


Pssm-ID: 466890  Cd Length: 409  Bit Score: 123.60  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995  61 YGIVLDAGSSHTSLYIYKW-----PAEKENDtgvvhqvEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQE 135
Cdd:cd24040     1 YALMIDAGSTGSRIHVYRFnncqpPIPKLED-------EVFEMTKPGLSSYADDPKGAAASLDPLLQVALQAVPKELHSC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 136 TPVYLGATAGMRLLrmeSEELADRVLDVVERSLSN----YPFDFQGARIITGQEEGAYGWITINYLLGKFSQKtrwfsiv 211
Cdd:cd24040    74 TPIAVKATAGLRLL---GEDKSKEILDAVRHRLEKeypfVSVELDGVSIMDGKDEGVYAWITVNYLLGNIGGN------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521995 212 pyetNNQETFGALDLGGASTQVTFVPQ-NQTIESPDNALQFRLY--GKDYNVYTHSFLCYGKDQALwQKLAKDI 282
Cdd:cd24040   144 ----EKLPTAAVLDLGGGSTQIVFEPDfPSDEEDPEGDHKYELTfgGKDYVLYQHSYLGYGLMEAR-KKIHKLV 212
ASKHA_NBD_TgNTPase-like cd24037
nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) ...
 137-235 1.92e-10

nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) isoforms and similar proteins; The family corresponds a group of proteins similar to Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) isoforms, NTPase-I and NTPase-II. NTPase (EC 3.6.1.15), also called nucleoside-triphosphatase, may perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite and may contribute to intracellular survival and virulence. NTPAse-I has a specific activity 4.5-fold higher than NTPAse-II in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).


Pssm-ID: 466887  Cd Length: 565  Bit Score: 61.03  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 137 PVYLGATAGMRllrmESEELADRVLDVVERSLSNYPFDFQG---------ARIITGQEEGAYGWITINYLLGKFSQKTRW 207
Cdd:cd24037   124 PVMLCSTAGVR----DFHDWYRDALFVLLRHLINNPSPAHGykfftnpfwTRPITGAEEGLFAFITLNHLSRRLGEDPAR 199

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462521995 208 FSIVPYETNN--QETFGALDLGGASTQVTF 235
Cdd:cd24037   200 CMIDEYGVKQcrNDLAGVVEVGGASAQIVF 229
ASKHA_NBD_MtPPX1-like cd24056
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
 121-253 7.02e-04

nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Mycobacterium tuberculosis encodes two PPX/GppA homologues, Rv0496 (MtPPX1) and Rv1026 (MtPPX2), which are analogous to the Escherichia coli PPX and GppA enzymes. MtPPX1 functions as an exopolyphosphatase, showing a distinct preference for relatively short-chain poly-P substrates. The exopolyphosphatase activities of MtPPX1 are inhibited by pppGpp. In contrast, MtPPX2 has no detectable exopolyphosphatase activities. Neither MtPPX1 nor MtPPX2 can hydrolyze pppGpp to ppGpp, which is a reaction catalyzed by E. coli PPX and GppA enzymes. Both the MtPPX1 and MtPPX2 proteins have modest ATPase and to a lesser extent ADPase activities. The family corresponds a group of proteins similar to MtPPX1.


Pssm-ID: 466906 [Multi-domain]  Cd Length: 302  Bit Score: 40.29  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521995 121 MERAREVIPR-----SQHQETPVYLGATAGMRLLRmESEELADRVLDVVERSLsnypfdfqgaRIITGQEEGAYGWITIn 195
Cdd:cd24056    52 IDRAAEAVRRfvelaRRLGAEELLAVATSALREAE-NGPEVLDRVEAETGVPV----------RVLSGEEEARLTFLGA- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521995 196 yllgkfsqkTRWFSIVPYETnnqetfGALDLGGASTQVTFVpqnqTIESPDNALQFRL 253
Cdd:cd24056   120 ---------RAALGWSSGPL------LVLDLGGGSLELAVG----VDGRPEWAASLPL 158
 
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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