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Conserved domains on  [gi|149031119|gb|EDL86146|]
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ectonucleoside triphosphate diphosphohydrolase 6, isoform CRA_e [Rattus norvegicus]

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 ...
 72-224 7.15e-106

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 cd24115:

Pssm-ID: 483947  Cd Length: 374  Bit Score: 309.82  E-value: 7.15e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  72 VFYGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24115    1 VFYGIMFDAGSTGTRIHIFKFTRPPNEAPKLTHETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDFWKATPLVL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149031119 152 KATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGAClqmeKANGSPSLG 224
Cdd:cd24115   81 KATAGLRLLPGEKAQKLLDKVKEVFKASPFLVGDDSVSIMDGTDEGISAWITVNFLTGSL----HGTGRSSVG 149
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
 72-224 7.15e-106

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: 309.82  E-value: 7.15e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  72 VFYGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24115    1 VFYGIMFDAGSTGTRIHIFKFTRPPNEAPKLTHETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDFWKATPLVL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149031119 152 KATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGAClqmeKANGSPSLG 224
Cdd:cd24115   81 KATAGLRLLPGEKAQKLLDKVKEVFKASPFLVGDDSVSIMDGTDEGISAWITVNFLTGSL----HGTGRSSVG 149
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
71-220 3.05e-44

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 152.97  E-value: 3.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119   71 EVFYGIMFDAGSTGTRIHVFQF-ARPPGETPTLTH-ETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATP 148
Cdd:pfam01150   7 NVKYGIIIDAGSSGTRLHVYKWpDEKEGLTPIVPLiEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPEEKRSETP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149031119  149 LVLKATAGLRLLPGEKAQKLLQKVKEVFKA-SPFLVGDDCVSIMNGTDEGVSAWITVNFLTGaclQMEKANGS 220
Cdd:pfam01150  87 VFLGATAGMRLLPDESKESILKALRNGLKSlTSFPVDDQGIRIIDGQEEGAYGWIAINYLLG---NFGKPKQS 156
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
 72-224 7.15e-106

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: 309.82  E-value: 7.15e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  72 VFYGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24115    1 VFYGIMFDAGSTGTRIHIFKFTRPPNEAPKLTHETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDFWKATPLVL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149031119 152 KATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGAClqmeKANGSPSLG 224
Cdd:cd24115   81 KATAGLRLLPGEKAQKLLDKVKEVFKASPFLVGDDSVSIMDGTDEGISAWITVNFLTGSL----HGTGRSSVG 149
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
 74-209 1.36e-82

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: 250.55  E-value: 1.36e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPP-GETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVLK 152
Cdd:cd24046    1 YAIVFDAGSTGSRVHVFKFSHSPsGGPLKLLDELFEEVKPGLSSYADDPKEAADSLKPLLEKAKTRIPKEKWSSTPLALK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149031119 153 ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTG 209
Cdd:cd24046   81 ATAGLRLLPEEKANAILDEVRKLFKKSPFLVGEDSVSIMDGTDEGIFSWFTVNFLLG 137
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
 73-209 2.20e-72

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: 224.69  E-value: 2.20e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  73 FYGIMFDAGSTGTRIHVFQFA-RPPGETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24114    2 FYGIMFDAGSTGTRIHIYTFVqKSPAELPELDGEIFESVKPGLSAYADQPEQGAETVRGLLDVAKKTIPSTQWKKTPVVL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149031119 152 KATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTG 209
Cdd:cd24114   82 KATAGLRLLPEEKAQALLSEVKEIFEESPFLVPEGSVSIMNGTYEGILAWVTVNFLTG 139
ASKHA_NBD_AtAPY1-like cd24041
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), ...
 74-209 7.23e-54

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: 177.52  E-value: 7.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETP-TLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVLK 152
Cdd:cd24041    2 YAVVFDAGSTGSRVHVFKFDQNLDLLHlGLDLELFEQIKPGLSSYADDPEQAAKSLRPLLDKALAVVPEELQSKTPVRLG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149031119 153 ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTG 209
Cdd:cd24041   82 ATAGLRLLPGDASENILQEVRDLLRNYSFKVQPDAVSIIDGTDEGSYQWVTVNYLLG 138
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 74-220 5.09e-52

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: 171.03  E-value: 5.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETPTLTHETF----KALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPL 149
Cdd:cd24003    1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIELVSsgkeKSGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDRRSSTPV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149031119 150 VLKATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGAcLQMEKANGS 220
Cdd:cd24003   81 YLLATAGMRLLPEEQQEAILDAVRTILRNSGFGFDDGWVRVISGEEEGLYGWLSVNYLLGN-LGSEPAKKT 150
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
 74-210 2.11e-50

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: 168.67  E-value: 2.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVLKA 153
Cdd:cd24040    1 YALMIDAGSTGSRIHVYRFNNCQPPIPKLEDEVFEMTKPGLSSYADDPKGAAASLDPLLQVALQAVPKELHSCTPIAVKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149031119 154 TAGLRLLPGEKAQKLLQKVKEVFKASPFLVGD--DCVSIMNGTDEGVSAWITVNFLTGA 210
Cdd:cd24040   81 TAGLRLLGEDKSKEILDAVRHRLEKEYPFVSVelDGVSIMDGKDEGVYAWITVNYLLGN 139
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
71-220 3.05e-44

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 152.97  E-value: 3.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119   71 EVFYGIMFDAGSTGTRIHVFQF-ARPPGETPTLTH-ETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATP 148
Cdd:pfam01150   7 NVKYGIIIDAGSSGTRLHVYKWpDEKEGLTPIVPLiEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPEEKRSETP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149031119  149 LVLKATAGLRLLPGEKAQKLLQKVKEVFKA-SPFLVGDDCVSIMNGTDEGVSAWITVNFLTGaclQMEKANGS 220
Cdd:pfam01150  87 VFLGATAGMRLLPDESKESILKALRNGLKSlTSFPVDDQGIRIIDGQEEGAYGWIAINYLLG---NFGKPKQS 156
ASKHA_NBD_AtAPY3-like cd24042
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar ...
 74-217 4.49e-36

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: 130.64  E-value: 4.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFAR-------PPGETPTLThetFKaLKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKA 146
Cdd:cd24042    1 YSVIIDAGSSGTRLHVFGYAAesgkpvfPFGEKDYAS---LK-TTPGLSSFADNPSGASASLTELLEFAKERVPKGKRKE 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149031119 147 TPLVLKATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGAcLQMEKA 217
Cdd:cd24042   77 TDIRLMATAGLRLLEVPVQEQILEVCRRVLRSSGFMFRDEWASVISGTDEGIYAWVAANYALGS-LGGDPL 146
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
 74-209 9.67e-31

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: 116.78  E-value: 9.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGET--PTLTHETFKA-----------------LKPGLSAYADDVEKSAQGIQELLNV 134
Cdd:cd24043    1 YAIVMDCGSTGTRVYVYSWARNPSKDslPVMVDPPTVAsaalvkkpkkraykrveTEPGLDKLADNETGLGAALGPLLDW 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149031119 135 AKQHIPYDFWKATPLVLKATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTG 209
Cdd:cd24043   81 AGKQIPRSQHPRTPVFLFATAGLRRLPPDDSAWLLDKAWGVLEASPFRFERSWVRIISGTEEAYYGWIALNYLTG 155
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
 74-209 2.52e-30

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: 116.25  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETP------TLTHETFKAL----KPGLSAYADDVEKSAQGIQELLNVAKQHIPYDF 143
Cdd:cd24045    3 YGVVIDCGSSGSRVFVYTWPRHSGNPHelldikPLRDENGKPVvkkiKPGLSSFADKPEKASDYLRPLLDFAAEHIPREK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149031119 144 WKATPLVLKATAGLRLLPgEKAQK-----LLQKVKEVFkasPFLVGDDCVSIMNGTDEGVSAWITVNFLTG 209
Cdd:cd24045   83 HKETPLYILATAGMRLLP-ESQQEailedLRTDIPKHF---NFLFSDSHAEVISGKQEGVYAWIAINYVLG 149
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
 74-210 6.59e-30

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: 114.68  E-value: 6.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETPTLTHETF--KALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24044    1 YGIVIDAGSSHTSLFVYKWPADKENGTGVVQQVStcRVKGGGISSYENNPSQAGESLEPCLDQAKKKVPEDRRHSTPLYL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149031119 152 KATAGLRLL----PgEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGA 210
Cdd:cd24044   81 GATAGMRLLnltnP-SAADAILESVRDALKSSKFGFDFRNARILSGEDEGLYGWITVNYLLGN 142
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
 74-209 1.80e-26

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: 104.74  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFKAL-----------------KPGLSAYADDVEKSAQGIQELLNVAK 136
Cdd:cd24039    3 YGIVIDAGSSGSRVQIYSWKDPESATSKASLEELKSLphietgigdgkdwtlkvEPGISSFADHPHVVGEHLKPLLDFAL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149031119 137 QHIPYDFWKATPLVLKATAGLRLLPGEKAQKLLQKVKEVFKA-SPFLVgDDC---VSIMNGTDEGVSAWITVNFLTG 209
Cdd:cd24039   83 NIIPPSVHSSTPIFLLATAGMRLLPQDQQNAILDAVCDYLRKnYPFLL-PDCsehVQVISGEEEGLYGWLAVNYLMG 158
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
 74-213 2.55e-24

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: 99.46  E-value: 2.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFK--ALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24112    1 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTYKcnVKGPGISSYAHNPQKAARALEECMNKVKEIIPSHLHNSTPVYL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149031119 152 KATAGLRLLPGE---KAQKLLQKVKEVFKASPFLVGDdcVSIMNGTDEGVSAWITVNFLTGACLQ 213
Cdd:cd24112   81 GATAGMRLLKLQnetAANEVLSSIENYFKTLPFDFRG--AHIITGQEEGVYGWITANYLMGNFLE 143
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
 74-225 1.77e-22

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: 94.47  E-value: 1.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFarpPGETPTLT-----HETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATP 148
Cdd:cd24110    7 YGIVLDAGSSHTSLYIYKW---PAEKENDTgvvqqLEECKVKGPGISSYSQKTTKAGASLAECMKKAKEVIPASQHHETP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119 149 LVLKATAGLRLLPGEK---AQKLLQKVKEVFKASPF-LVGddcVSIMNGTDEGVSAWITVNFLTGACLQMEKANGSPSLG 224
Cdd:cd24110   84 VYLGATAGMRLLRMESeqaAEEVLASVERSLKSYPFdFQG---ARIITGQEEGAYGWITINYLLGNFKQDSGWFTQLSGG 160


                 .
gi 149031119 225 K 225
Cdd:cd24110  161 K 161
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
 74-207 1.63e-20

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: 88.65  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQFarpPGETPTLT-----HETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATP 148
Cdd:cd24111    4 YGIVLDAGSSHTSMFVYKW---PADKENDTgivsqHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149031119 149 LVLKATAGLRLL---PGEKAQKLLQKVKEVFKASPFLVGDdcVSIMNGTDEGVSAWITVNFL 207
Cdd:cd24111   81 LYLGATAGMRLLnltSPEASARVLEAVTQTLTSYPFDFRG--ARILSGQEEGVFGWVTANYL 140
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
 74-210 2.75e-20

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: 87.40  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQF----ARPPGETPTLTHETfkaLKPGLSA-YADDVEKSAQGIQELLNVAKQHipydfwkATP 148
Cdd:cd24038    3 CTAVIDAGSSGSRLHLYQYdtddSNPPIHEIELKNNK---IKPGLASvNTTDVDAYLDPLFAKLPIAKTS-------NIP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149031119 149 LVLKATAGLRLLPGEKAQKLLQKVKEVFKASP--FLVgddCVSIMNGTDEGVSAWITVNFLTGA 210
Cdd:cd24038   73 VYFYATAGMRLLPPSEQKKLYQELKDWLAQQSkfQLV---EAKTITGHMEGLYDWIAVNYLLDT 133
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
 74-207 4.93e-20

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: 87.50  E-value: 4.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149031119  74 YGIMFDAGSTGTRIHVFQF-ARPPGETPTLTH-ETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVL 151
Cdd:cd24113   25 YGIVFDAGSSHTSLFLYQWpADKENGTGIVSQvLSCDVEGPGISSYAQNPAKAGESLKPCLDEALAAIPAEQQKETPVYL 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149031119 152 KATAGLRLLPGE---KAQKLLQKVKEVFKASPFLVGDdcVSIMNGTDEGVSAWITVNFL 207
Cdd:cd24113  105 GATAGMRLLRLQnstQSDEILAEVSKTIGSYPFDFQG--ARILTGMEEGAYGWITVNYL 161
 
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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