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Conserved domains on  [gi|767924674|ref|XP_011532568|]
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ectonucleoside triphosphate diphosphohydrolase 3 isoform X1 [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 ...
 57-283 1.05e-161

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 cd24112:

Pssm-ID: 483947  Cd Length: 411  Bit Score: 455.38  E-value: 1.05e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHL 136
Cdd:cd24112    1 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTYKCNVKGPGISSYAHNPQKAARALEECMNKVKEIIPSHLHNSTPVYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 137 GATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTG 216
Cdd:cd24112   81 GATAGMRLLKLQNETAANEVLSSIENYFKTLPFDFRGAHIITGQEEGVYGWITANYLMGNFLEKNLWNAWVHPHGVETVG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924674 217 ALDLGGASTQISFVAGEKMdLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTEKK 283
Cdd:cd24112  161 ALDLGGASTQIAFIPEDSL-ENLNDTVKVSLYGYKYNVYTHSFQCYGKDEAEKRFLANLAQASESKS 226
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
 57-283 1.05e-161

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: 455.38  E-value: 1.05e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHL 136
Cdd:cd24112    1 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTYKCNVKGPGISSYAHNPQKAARALEECMNKVKEIIPSHLHNSTPVYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 137 GATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTG 216
Cdd:cd24112   81 GATAGMRLLKLQNETAANEVLSSIENYFKTLPFDFRGAHIITGQEEGVYGWITANYLMGNFLEKNLWNAWVHPHGVETVG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924674 217 ALDLGGASTQISFVAGEKMdLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTEKK 283
Cdd:cd24112  161 ALDLGGASTQIAFIPEDSL-ENLNDTVKVSLYGYKYNVYTHSFQCYGKDEAEKRFLANLAQASESKS 226
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
56-281 1.01e-73

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 231.55  E-value: 1.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674   56 KYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIH 135
Cdd:pfam01150   9 KYGIIIDAGSSGTRLHVYKWPDEKEGLTPIVPLIEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPEEKRSETPVF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  136 LGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLwhmwvhphgvETT 215
Cdd:pfam01150  89 LGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPKQ----------STF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924674  216 GALDLGGASTQISFVAGEKMDLNTS--DI---MQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTE 281
Cdd:pfam01150 159 GAIDLGGASTQIAFEPSNESAINSTveDIelgLQFRLYDKDYTLYVHSFLGYGANEALRKYLAKLIQNLSN 229
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
 57-283 1.05e-161

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: 455.38  E-value: 1.05e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHL 136
Cdd:cd24112    1 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTYKCNVKGPGISSYAHNPQKAARALEECMNKVKEIIPSHLHNSTPVYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 137 GATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTG 216
Cdd:cd24112   81 GATAGMRLLKLQNETAANEVLSSIENYFKTLPFDFRGAHIITGQEEGVYGWITANYLMGNFLEKNLWNAWVHPHGVETVG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924674 217 ALDLGGASTQISFVAGEKMdLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTEKK 283
Cdd:cd24112  161 ALDLGGASTQIAFIPEDSL-ENLNDTVKVSLYGYKYNVYTHSFQCYGKDEAEKRFLANLAQASESKS 226
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
 57-279 1.08e-119

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: 348.88  E-value: 1.08e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHL 136
Cdd:cd24044    1 YGIVIDAGSSHTSLFVYKWPADKENGTGVVQQVSTCRVKGGGISSYENNPSQAGESLEPCLDQAKKKVPEDRRHSTPLYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 137 GATAGMRLLRLQNETAANEVLESIQSYFKSQ--PFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHmwVHPHGVET 214
Cdd:cd24044   81 GATAGMRLLNLTNPSAADAILESVRDALKSSkfGFDFRNARILSGEDEGLYGWITVNYLLGNLGKYSISS--IPRSRPET 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924674 215 TGALDLGGASTQISFVAGEKMdLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQS 279
Cdd:cd24044  159 VGALDLGGASTQITFEPAEPS-LPADYTRKLRLYGKDYNVYTHSYLCYGKDEAERRYLASLVQES 222
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
 51-277 5.28e-104

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: 309.76  E-value: 5.28e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  51 LPPGLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHG 130
Cdd:cd24113   19 LPPGIKYGIVFDAGSSHTSLFLYQWPADKENGTGIVSQVLSCDVEGPGISSYAQNPAKAGESLKPCLDEALAAIPAEQQK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 131 STPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPH 210
Cdd:cd24113   99 ETPVYLGATAGMRLLRLQNSTQSDEILAEVSKTIGSYPFDFQGARILTGMEEGAYGWITVNYLLETFIKYSFEGKWIHPK 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924674 211 GVETTGALDLGGASTQISFVAGEKM-DLNTSdiMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQ 277
Cdd:cd24113  179 GGNILGALDLGGASTQITFVPGGPIeDKNTE--ANFRLYGYNYTVYTHSYLCYGKDQMLKRLLAALLQ 244
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
 54-277 3.09e-101

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: 302.05  E-value: 3.09e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  54 GLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTP 133
Cdd:cd24111    1 ALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVSQHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 134 IHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPhGVE 213
Cdd:cd24111   81 LYLGATAGMRLLNLTSPEASARVLEAVTQTLTSYPFDFRGARILSGQEEGVFGWVTANYLLENFIKYGWVGQWIRP-RKG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924674 214 TTGALDLGGASTQISFVAGEKMDlNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQ 277
Cdd:cd24111  160 TLGAMDLGGASTQITFETTSPSE-DPGNEVHLRLYGQHYRVYTHSFLCYGRDQVLLRLLASALQ 222
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
 51-280 4.24e-100

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: 299.40  E-value: 4.24e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  51 LPPGLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHG 130
Cdd:cd24110    1 LPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVQQLEECKVKGPGISSYSQKTTKAGASLAECMKKAKEVIPASQHH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 131 STPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWhMWVHPH 210
Cdd:cd24110   81 ETPVYLGATAGMRLLRMESEQAAEEVLASVERSLKSYPFDFQGARIITGQEEGAYGWITINYLLGNFKQDSGW-FTQLSG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767924674 211 G--VETTGALDLGGASTQISFVAGEKMDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQST 280
Cdd:cd24110  160 GkpTETFGALDLGGASTQITFVPLNSTIESPENSLQFRLYGTDYTVYTHSFLCYGKDQALWQKLAQDIQSTS 231
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
56-281 1.01e-73

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 231.55  E-value: 1.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674   56 KYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIH 135
Cdd:pfam01150   9 KYGIIIDAGSSGTRLHVYKWPDEKEGLTPIVPLIEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPEEKRSETPVF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  136 LGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLwhmwvhphgvETT 215
Cdd:pfam01150  89 LGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPKQ----------STF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924674  216 GALDLGGASTQISFVAGEKMDLNTS--DI---MQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTE 281
Cdd:pfam01150 159 GAIDLGGASTQIAFEPSNESAINSTveDIelgLQFRLYDKDYTLYVHSFLGYGANEALRKYLAKLIQNLSN 229
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 57-283 9.92e-70

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: 218.80  E-value: 9.92e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEKEN--NTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPI 134
Cdd:cd24003    1 YGVVIDAGSSGTRLHVYKWKARSDDlpSIIELVSSGKEKSGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDRRSSTPV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 135 HLGATAGMRLLRlqnETAANEVLESIQSYFKSQPFDFR--GAQIISGQEEGVYGWITANYLMGNFLeknlwhmwvHPHGV 212
Cdd:cd24003   81 YLLATAGMRLLP---EEQQEAILDAVRTILRNSGFGFDdgWVRVISGEEEGLYGWLSVNYLLGNLG---------SEPAK 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924674 213 ETTGALDLGGASTQISFVAGEKMDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTEKK 283
Cdd:cd24003  149 KTVGVLDLGGASTQIAFEPPEDDLSSLSNVYPLRLGGKTYDLYSHSFLGYGLNEARKRVLESLINNSEGGN 219
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
 56-282 1.97e-47

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: 162.14  E-value: 1.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  56 KYGIVLDAGSSRTTVYVYQW--PAEKENNTG--------VVSQ--------TFKCSvkgSGISSYGNNPQDVPRAFEECM 117
Cdd:cd24039    2 KYGIVIDAGSSGSRVQIYSWkdPESATSKASleelkslpHIETgigdgkdwTLKVE---PGISSFADHPHVVGEHLKPLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 118 QKVKGQVPSHLHGSTPIHLGATAGMRLLRLQNETAaneVLESIQSYFKsQPFDFRGA------QIISGQEEGVYGWITAN 191
Cdd:cd24039   79 DFALNIIPPSVHSSTPIFLLATAGMRLLPQDQQNA---ILDAVCDYLR-KNYPFLLPdcsehvQVISGEEEGLYGWLAVN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 192 YLMGNFLEKNLWHmwvHPHGVETTGALDLGGASTQISFVAGEKMDLNTS-DIMQVSLY---GYV--YTLYTHSFQCYGRN 265
Cdd:cd24039  155 YLMGGFDDAPKHS---IAHDHHTFGFLDMGGASTQIAFEPNASAAKEHAdDLKTVHLRtldGSQveYPVFVTTWLGFGTN 231

                        250
                 ....*....|....*..
gi 767924674 266 EAEKKFLAMLLQQSTEK 282
Cdd:cd24039  232 EARRRYVESLIEQAGSD 248
ASKHA_NBD_AtAPY3-like cd24042
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar ...
 57-276 4.75e-46

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: 159.15  E-value: 4.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEkeNNTGVVSQTFK--CSVKGS-GISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTP 133
Cdd:cd24042    1 YSVIIDAGSSGTRLHVFGYAAE--SGKPVFPFGEKdyASLKTTpGLSSFADNPSGASASLTELLEFAKERVPKGKRKETD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 134 IHLGATAGMRLLRLQnetAANEVLESIQSYFKSQPFDFRG--AQIISGQEEGVYGWITANYLMGNfleknlwhmwVHPHG 211
Cdd:cd24042   79 IRLMATAGLRLLEVP---VQEQILEVCRRVLRSSGFMFRDewASVISGTDEGIYAWVAANYALGS----------LGGDP 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924674 212 VETTGALDLGGASTQISFVAGEKMDLNTSDimQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLL 276
Cdd:cd24042  146 LETTGIVELGGASAQVTFVPSEAVPPEFSR--TLVYGGVSYKLYSHSFLDFGQEAAWDKLLESLL 208
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
 57-259 1.19e-45

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: 157.33  E-value: 1.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWpaeKENNTG----VVSQTFKCsVKgSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGST 132
Cdd:cd24046    1 YAIVFDAGSTGSRVHVFKF---SHSPSGgplkLLDELFEE-VK-PGLSSYADDPKEAADSLKPLLEKAKTRIPKEKWSST 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 133 PIHLGATAGMRLLRlqnETAANEVLESIQSYFKSQPFDFR--GAQIISGQEEGVYGWITANYLMGNFleknlwhmwvHPH 210
Cdd:cd24046   76 PLALKATAGLRLLP---EEKANAILDEVRKLFKKSPFLVGedSVSIMDGTDEGIFSWFTVNFLLGRL----------GGS 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767924674 211 GVETTGALDLGGASTQISFVAGEKMDLNTS---DIMQVSLYGYVYTLYTHSF 259
Cdd:cd24046  143 ASNTVAALDLGGGSTQITFAPSDKETLSASpkgYLHKVSIFGKKIKLYTHSY 194
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
 57-278 3.36e-40

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: 144.02  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWpaekeNNTGVVSQTFKCSVK---GSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTP 133
Cdd:cd24040    1 YALMIDAGSTGSRIHVYRF-----NNCQPPIPKLEDEVFemtKPGLSSYADDPKGAAASLDPLLQVALQAVPKELHSCTP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 134 IHLGATAGMRLLrlqNETAANEVLESIQSYFKSQPFDF----RGAQIISGQEEGVYGWITANYLMGnfleknlwhmWVHP 209
Cdd:cd24040   76 IAVKATAGLRLL---GEDKSKEILDAVRHRLEKEYPFVsvelDGVSIMDGKDEGVYAWITVNYLLG----------NIGG 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924674 210 HGVETTGA-LDLGGASTQISFVAGEKMDLNTSDimQVSLY-----GYVYTLYTHSFQCYGRNEAEKKFLAMLLQQ 278
Cdd:cd24040  143 NEKLPTAAvLDLGGGSTQIVFEPDFPSDEEDPE--GDHKYeltfgGKDYVLYQHSYLGYGLMEARKKIHKLVAEN 215
ASKHA_NBD_AtAPY1-like cd24041
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), ...
 56-273 3.32e-38

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: 138.61  E-value: 3.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  56 KYGIVLDAGSSRTTVYVYQWPAE-KENNTGVVSQTFKcSVKgSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPI 134
Cdd:cd24041    1 RYAVVFDAGSTGSRVHVFKFDQNlDLLHLGLDLELFE-QIK-PGLSSYADDPEQAAKSLRPLLDKALAVVPEELQSKTPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 135 HLGATAGMRLLrlqNETAANEVLESIQSYFKSQPFDFR--GAQIISGQEEGVYGWITANYLMGNFLEKnlwhmwvhphGV 212
Cdd:cd24041   79 RLGATAGLRLL---PGDASENILQEVRDLLRNYSFKVQpdAVSIIDGTDEGSYQWVTVNYLLGNLGKP----------FT 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924674 213 ETTGALDLGGASTQISFVAGEK--------MDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLA 273
Cdd:cd24041  146 KTVGVVDLGGGSVQMAYAVSDEtaknapkpTDGEDGYIRKLVLKGKTYDLYVHSYLGYGLMAARAEILK 214
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
 57-263 7.51e-36

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: 131.86  E-value: 7.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKcSVKgSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHL 136
Cdd:cd24115    3 YGIMFDAGSTGTRIHIFKFTRPPNEAPKLTHETFK-ALK-PGLSAYADEPEKCAEGIQELLDVAKQDIPSDFWKATPLVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 137 GATAGMRLLRLQNetaANEVLESIQSYFKSQPFDFR--GAQIISGQEEGVYGWITANYLMGNfleknlwhmwVHPHGVET 214
Cdd:cd24115   81 KATAGLRLLPGEK---AQKLLDKVKEVFKASPFLVGddSVSIMDGTDEGISAWITVNFLTGS----------LHGTGRSS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767924674 215 TGALDLGGASTQISFVAGEKMDLNTSDIMQVS---LYGYVYTLYTHSFQCYG 263
Cdd:cd24115  148 VGMLDLGGGSTQITFSPHSEGTLQTSPIDYITsfqMFNRTYTLYSHSYLGLG 199
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
 56-272 2.80e-35

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: 129.78  E-value: 2.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  56 KYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGsGISSYgnNPQDVPRAFEECMQKVKGQVPShlhgSTPIH 135
Cdd:cd24038    2 SCTAVIDAGSSGSRLHLYQYDTDDSNPPIHEIELKNNKIKP-GLASV--NTTDVDAYLDPLFAKLPIAKTS----NIPVY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 136 LGATAGMRLLrlqNETAANEVLESIQSYFKSQ-PFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNlwhmwvhphgvET 214
Cdd:cd24038   75 FYATAGMRLL---PPSEQKKLYQELKDWLAQQsKFQLVEAKTITGHMEGLYDWIAVNYLLDTLKSSK-----------KT 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 215 TGALDLGGASTQISFvageKMDLNTS--DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFL 272
Cdd:cd24038  141 VGVLDLGGASTQIAF----AVPNNASkdNTVEVKIGNKTINLYSHSYLGLGQDQARHQFL 196
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
 55-282 1.99e-34

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: 129.35  E-value: 1.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  55 LKYGIVLDAGSSRTTVYVYQWPAEKENN------TGVVSQTFKCSVK--GSGISSYGNNPQDVPRAFEECMQKVKGQVPS 126
Cdd:cd24045    1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPhelldiKPLRDENGKPVVKkiKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 127 HLHGSTPIHLGATAGMRLLrlqNETAANEVLESIQSYFKSQpFDFR----GAQIISGQEEGVYGWITANYLMGNF-LEKN 201
Cdd:cd24045   81 EKHKETPLYILATAGMRLL---PESQQEAILEDLRTDIPKH-FNFLfsdsHAEVISGKQEGVYAWIAINYVLGRFdHSED 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 202 LWHMWVHPHGVE-------TTGALDLGGASTQISFVAGEKMDLnTSDIMQVSLY-----------GYVYTLYTHSFQCYG 263
Cdd:cd24045  157 DDPAVVVVSDNKeailrkrTVGILDMGGASTQIAFEVPKTVEF-ASPVAKNLLAefnlgcdahdtEHVYRVYVTTFLGYG 235

                        250
                 ....*....|....*....
gi 767924674 264 RNEAEKKFLAMLLQQSTEK 282
Cdd:cd24045  236 ANEARQRYEDSLVSSTKST 254
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
 57-279 2.13e-33

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: 126.03  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQWPAE--KENNTGVVSQTFKCS---VKGSGISSYG------------NNPQDVPRAFEECMQK 119
Cdd:cd24043    1 YAIVMDCGSTGTRVYVYSWARNpsKDSLPVMVDPPTVASaalVKKPKKRAYKrvetepgldklaDNETGLGAALGPLLDW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 120 VKGQVPSHLHGSTPIHLGATAGMRllRLQNETAAnEVLESIQSYFKSQPFDFRG--AQIISGQEEGVYGWITANYLMGNF 197
Cdd:cd24043   81 AGKQIPRSQHPRTPVFLFATAGLR--RLPPDDSA-WLLDKAWGVLEASPFRFERswVRIISGTEEAYYGWIALNYLTGRL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 198 LEKnlwhmwvhPHGVETTGALDLGGASTQISFVAGEKMdlNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQ 277
Cdd:cd24043  158 GQG--------PGKGATVGSLDLGGSSLEVTFEPEAVP--RGEYGVNLSVGSTEHHLYAHSHAGYGLNDAFDKSVALLLK 227


                 ..
gi 767924674 278 QS 279
Cdd:cd24043  228 DQ 229
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
 57-283 6.77e-33

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: 123.77  E-value: 6.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674  57 YGIVLDAGSSRTTVYVYQW----PAEKENNTGVVSQtfkcSVKgSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGST 132
Cdd:cd24114    3 YGIMFDAGSTGTRIHIYTFvqksPAELPELDGEIFE----SVK-PGLSAYADQPEQGAETVRGLLDVAKKTIPSTQWKKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 133 PIHLGATAGMRLLrlqNETAANEVLESIQSYFKSQPFDF--RGAQIISGQEEGVYGWITANYLMGNfleknlwhmwVHPH 210
Cdd:cd24114   78 PVVLKATAGLRLL---PEEKAQALLSEVKEIFEESPFLVpeGSVSIMNGTYEGILAWVTVNFLTGQ----------LYGQ 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924674 211 GVETTGALDLGGASTQISFV--AGEKMDLNTSD-IMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQQSTEKK 283
Cdd:cd24114  145 NQRTVGILDLGGASTQITFLprFEKTLKQAPEDyLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALGTEDQEKQ 220
ASKHA_NBD_TgNTPase-like cd24037
nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) ...
 177-229 1.58e-03

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: 39.84  E-value: 1.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767924674 177 ISGQEEGVYGWITANYLMGNFLEkNLWHMWVHPHGVET-----TGALDLGGASTQISF 229
Cdd:cd24037  173 ITGAEEGLFAFITLNHLSRRLGE-DPARCMIDEYGVKQcrndlAGVVEVGGASAQIVF 229
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
 129-235 2.47e-03

nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, Fusobacterium nucleatum AroB, 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). The family corresponds to a group of proteins similar to Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA), Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2), Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins.


Pssm-ID: 466904 [Multi-domain]  Cd Length: 296  Bit Score: 38.61  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 129 HGSTPIHLGATAGMRllrlqneTAAN--EVLESIQSYFKsqpFDFRgaqIISGQEEGVYGWITANYLMGNFLEKNLwhmw 206
Cdd:cd24054   67 YGVEKIRAVATSALR-------DAKNrdEFLERVKEETG---LEIE---IISGEEEARLSFLGALSGLPLPDGPIL---- 129

                         90       100
                 ....*....|....*....|....*....
gi 767924674 207 vhphgvettgALDLGGASTQISFVAGEKM 235
Cdd:cd24054  130 ----------VIDIGGGSTELILGKGGGI 148
ASKHA_NBD_MtPPX1-like cd24056
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
 126-236 2.55e-03

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: 38.75  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924674 126 SHLHGSTPIHLGATAGMRllrlqneTAAN--EVLESIQSYFKSQPfdfrgaQIISGQEEGVYGWITAnylmgnfleknlw 203
Cdd:cd24056   66 ARRLGAEELLAVATSALR-------EAENgpEVLDRVEAETGVPV------RVLSGEEEARLTFLGA------------- 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767924674 204 hmwVHPHGVETTGAL--DLGGASTQISFVAGEKMD 236
Cdd:cd24056  120 ---RAALGWSSGPLLvlDLGGGSLELAVGVDGRPE 151
 
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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