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Conserved domains on  [gi|258597746|ref|XP_001348471|]
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apyrase, putative [Plasmodium falciparum 3D7]

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_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 76-321 1.20e-64

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: 220.34  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKREYELSNKKEENNLIELKeifNAKVKKSISTISYNEIKDILIYLINKVIDHLIEKKiyv 155
Cdd:cd24003    1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIELVSSGKEK---SGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDR--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 ynkqkWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFS-K 234
Cdd:cd24003   75 -----RSSTPVYLLATAGMRLLPEEQQEAILDAVRTILRN---SGFGFDDGWVRVISGEEEGLYGWLSVNYLLGNLGSeP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 235 PNNTYGAIDLGGSSTQITFYPMDHNILENYN--SILLNNILIRLYSHSFIGYGWIDSLFRVNIYLCLEIIKKLSTRN--- 309
Cdd:cd24003  147 AKKTVGVLDLGGASTQIAFEPPEDDLSSLSNvyPLRLGGKTYDLYSHSFLGYGLNEARKRVLESLINNSEGGNVTNPclp 226

                        250
                 ....*....|....*
gi 258597746 310 ---IKNIYQLENYYD 321
Cdd:cd24003  227 kgyTGPFYAFSNFYY 241
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 631-767 1.53e-13

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 cd24044:

Pssm-ID: 483947  Cd Length: 411  Bit Score: 73.47  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 631 INITVRIVGSNDFKKCLENTKKLFYE-QPCFLSSCSFNGIYQPNLeNNKFVLHGQFKKVITYLGFKKYVDLNQMKIYIQK 709
Cdd:cd24044  263 NNTNFTFNGTSNPDQCRELVRKLFNFtSCCSSGCCSFNGVFQPPL-NGNFYAFSGFYYTADFLNLTSNGSLDEFREAVDD 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 710 LCNMNlYELTYNMSNKImHNQIPTFCWKSIWSYSLLFYGFKFKETT--KLLIINDNTNIS 767
Cdd:cd24044  342 FCNKP-WDEVSELPPKG-AKFLANYCFDANYILTLLTDGYGFTEETwrNIHFVKKVNGTE 399
 
Name Accession Description Interval E-value
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 76-321 1.20e-64

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: 220.34  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKREYELSNKKEENNLIELKeifNAKVKKSISTISYNEIKDILIYLINKVIDHLIEKKiyv 155
Cdd:cd24003    1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIELVSSGKEK---SGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDR--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 ynkqkWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFS-K 234
Cdd:cd24003   75 -----RSSTPVYLLATAGMRLLPEEQQEAILDAVRTILRN---SGFGFDDGWVRVISGEEEGLYGWLSVNYLLGNLGSeP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 235 PNNTYGAIDLGGSSTQITFYPMDHNILENYN--SILLNNILIRLYSHSFIGYGWIDSLFRVNIYLCLEIIKKLSTRN--- 309
Cdd:cd24003  147 AKKTVGVLDLGGASTQIAFEPPEDDLSSLSNvyPLRLGGKTYDLYSHSFLGYGLNEARKRVLESLINNSEGGNVTNPclp 226

                        250
                 ....*....|....*
gi 258597746 310 ---IKNIYQLENYYD 321
Cdd:cd24003  227 kgyTGPFYAFSNFYY 241
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
70-349 1.44e-31

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 128.31  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746   70 LQNEKEYGIIIDAGSNGTRIHLFEWKKREYELSNKkeENNLIELKeifnaKVKKSISTISyNEIKDILIYLinkviDHLI 149
Cdd:pfam01150   4 LPENVKYGIIIDAGSSGTRLHVYKWPDEKEGLTPI--VPLIEEFK-----KLEPGLSSFA-TKPDAAANYL-----TPLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  150 EKKIYVYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDNynPFYFLNEYARILSGEEEGIYGWLAVNNLLN 229
Cdd:pfam01150  71 EFAEEHIPEEKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLT--SFPVDDQGIRIIDGQEEGAYGWIAINYLLG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  230 SiFSKPNN-TYGAIDLGGSSTQITFYPMD-----------------HNILENYNsillnnilirLYSHSFIGYGWIDSLF 291
Cdd:pfam01150 149 N-FGKPKQsTFGAIDLGGASTQIAFEPSNesainstvedielglqfRLYDKDYT----------LYVHSFLGYGANEALR 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258597746  292 RVNIYLcleiIKKLSTRNIK------NIYQLENYYDDYINDYFYNNLPNYNWFFYSTKKIINNN 349
Cdd:pfam01150 218 KYLAKL----IQNLSNGILNdpcmppGYNKTVEVSTLEGKQFAIQGTGNWEQCRQSILELLNKN 277
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
 631-767 1.53e-13

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: 73.47  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 631 INITVRIVGSNDFKKCLENTKKLFYE-QPCFLSSCSFNGIYQPNLeNNKFVLHGQFKKVITYLGFKKYVDLNQMKIYIQK 709
Cdd:cd24044  263 NNTNFTFNGTSNPDQCRELVRKLFNFtSCCSSGCCSFNGVFQPPL-NGNFYAFSGFYYTADFLNLTSNGSLDEFREAVDD 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 710 LCNMNlYELTYNMSNKImHNQIPTFCWKSIWSYSLLFYGFKFKETT--KLLIINDNTNIS 767
Cdd:cd24044  342 FCNKP-WDEVSELPPKG-AKFLANYCFDANYILTLLTDGYGFTEETwrNIHFVKKVNGTE 399
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
591-757 8.65e-08

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 55.51  E-value: 8.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  591 GY-LNNVLKKVNdNKISNTLKNEIIK-----RLFEKIINEKikKLYINItVRIVGSNDFKKCLENTKKLFYEQ-PCFLSS 663
Cdd:pfam01150 209 GYgANEALRKYL-AKLIQNLSNGILNdpcmpPGYNKTVEVS--TLEGKQ-FAIQGTGNWEQCRQSILELLNKNaHCPYEP 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  664 CSFNGIYQPNLENNK---------FVLHGQFKKVITYLGFKKYVDLnqmkiyIQKLCNMNlYELTYNMSNKIMHNQIP-- 732
Cdd:pfam01150 285 CAFNGVHAPSIGSLQksfgassyfYTVMDFFGLGGEYSSQEKFTDI------ARKFCSKN-WNDIKAGFPKVLDKNISee 357

                         170       180
                  ....*....|....*....|....*
gi 258597746  733 TFCWKSIWSYSLLFYGFKFKETTKL 757
Cdd:pfam01150 358 TYCFKGAYILSLLHDGFNFPKTEEI 382
 
Name Accession Description Interval E-value
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 76-321 1.20e-64

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: 220.34  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKREYELSNKKEENNLIELKeifNAKVKKSISTISYNEIKDILIYLINKVIDHLIEKKiyv 155
Cdd:cd24003    1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIELVSSGKEK---SGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDR--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 ynkqkWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFS-K 234
Cdd:cd24003   75 -----RSSTPVYLLATAGMRLLPEEQQEAILDAVRTILRN---SGFGFDDGWVRVISGEEEGLYGWLSVNYLLGNLGSeP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 235 PNNTYGAIDLGGSSTQITFYPMDHNILENYN--SILLNNILIRLYSHSFIGYGWIDSLFRVNIYLCLEIIKKLSTRN--- 309
Cdd:cd24003  147 AKKTVGVLDLGGASTQIAFEPPEDDLSSLSNvyPLRLGGKTYDLYSHSFLGYGLNEARKRVLESLINNSEGGNVTNPclp 226

                        250
                 ....*....|....*
gi 258597746 310 ---IKNIYQLENYYD 321
Cdd:cd24003  227 kgyTGPFYAFSNFYY 241
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
 76-351 5.97e-36

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: 140.00  E-value: 5.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEwkkreyeLSNKKEENNLIELKEIFNaKVKKSIStiSYNEIKDILIylinKVIDHLIEKKIYV 155
Cdd:cd24046    1 YAIVFDAGSTGSRVHVFK-------FSHSPSGGPLKLLDELFE-EVKPGLS--SYADDPKEAA----DSLKPLLEKAKTR 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 YNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFSKP 235
Cdd:cd24046   67 IPKEKWSSTPLALKATAGLRLLPEEKANAILDEVRKLFKK---SPFLVGEDSVSIMDGTDEGIFSWFTVNFLLGRLGGSA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 236 NNTYGAIDLGGSSTQITFYPMDHNILENY-----NSILLNNILIRLYSHSFIGYGWIDSlfRvniylcLEIIKKLSTRNI 310
Cdd:cd24046  144 SNTVAALDLGGGSTQITFAPSDKETLSASpkgylHKVSIFGKKIKLYTHSYLGLGLMAA--R------LAILQGSSTNSN 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258597746 311 KNIYQL---------ENYYDDYINDYFYNNLPNYNWFF----YSTKKIINNNKE 351
Cdd:cd24046  216 SGTTELkspcfppnfKGEWWFGGKKYTSSIGGSSEYSFdacyKLAKKVVDSSVI 269
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
 75-285 3.40e-32

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: 128.62  E-value: 3.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  75 EYGIIIDAGSNGTRIHLFEWkkreyelsNKKEENNLIELKEIFNAKVKKSISTISYNEIKDILIYLINKVidhliekkiy 154
Cdd:cd24038    2 SCTAVIDAGSSGSRLHLYQY--------DTDDSNPPIHEIELKNNKIKPGLASVNTTDVDAYLDPLFAKL---------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 155 vyNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDnynpFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFSK 234
Cdd:cd24038   64 --PIAKTSNIPVYFYATAGMRLLPPSEQKKLYQELKDWLAQQ----SKFQLVEAKTITGHMEGLYDWIAVNYLLDTLKSS 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 258597746 235 pNNTYGAIDLGGSSTQITFYPMDHNILENYNSILLNNILIRLYSHSFIGYG 285
Cdd:cd24038  138 -KKTVGVLDLGGASTQIAFAVPNNASKDNTVEVKIGNKTINLYSHSYLGLG 187
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
70-349 1.44e-31

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 128.31  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746   70 LQNEKEYGIIIDAGSNGTRIHLFEWKKREYELSNKkeENNLIELKeifnaKVKKSISTISyNEIKDILIYLinkviDHLI 149
Cdd:pfam01150   4 LPENVKYGIIIDAGSSGTRLHVYKWPDEKEGLTPI--VPLIEEFK-----KLEPGLSSFA-TKPDAAANYL-----TPLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  150 EKKIYVYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDNynPFYFLNEYARILSGEEEGIYGWLAVNNLLN 229
Cdd:pfam01150  71 EFAEEHIPEEKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLT--SFPVDDQGIRIIDGQEEGAYGWIAINYLLG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  230 SiFSKPNN-TYGAIDLGGSSTQITFYPMD-----------------HNILENYNsillnnilirLYSHSFIGYGWIDSLF 291
Cdd:pfam01150 149 N-FGKPKQsTFGAIDLGGASTQIAFEPSNesainstvedielglqfRLYDKDYT----------LYVHSFLGYGANEALR 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258597746  292 RVNIYLcleiIKKLSTRNIK------NIYQLENYYDDYINDYFYNNLPNYNWFFYSTKKIINNN 349
Cdd:pfam01150 218 KYLAKL----IQNLSNGILNdpcmppGYNKTVEVSTLEGKQFAIQGTGNWEQCRQSILELLNKN 277
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
 76-285 1.50e-31

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: 127.47  E-value: 1.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKREYELSNKKEENnLIELKEI---------FNAKVKKSISTI--SYNEIKDILIYLInkv 144
Cdd:cd24039    3 YGIVIDAGSSGSRVQIYSWKDPESATSKASLEE-LKSLPHIetgigdgkdWTLKVEPGISSFadHPHVVGEHLKPLL--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 145 iDHLIEkkiyVYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMK----YIKNilsndNYNpfyFL----NEYARILSGEEE 216
Cdd:cd24039   79 -DFALN----IIPPSVHSSTPIFLLATAGMRLLPQDQQNAILDavcdYLRK-----NYP---FLlpdcSEHVQVISGEEE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 217 GIYGWLAVNNLLNSIFSKPNN-------TYGAIDLGGSSTQITFYPMDHNILENYNSI------LLNNILI--RLYSHSF 281
Cdd:cd24039  146 GLYGWLAVNYLMGGFDDAPKHsiahdhhTFGFLDMGGASTQIAFEPNASAAKEHADDLktvhlrTLDGSQVeyPVFVTTW 225


                 ....
gi 258597746 282 IGYG 285
Cdd:cd24039  226 LGFG 229
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
 76-285 3.22e-31

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: 127.01  E-value: 3.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKreyelsNKKEENNLIElkEIFNAKVKKSISTISYNEIKDILIYLINKVidHLIEKKIYv 155
Cdd:cd24044    1 YGIVIDAGSSHTSLFVYKWPA------DKENGTGVVQ--QVSTCRVKGGGISSYENNPSQAGESLEPCL--DQAKKKVP- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 ynKQKWKSYPFYFQATGGMRNLKQEDR---NLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIF 232
Cdd:cd24044   70 --EDRRHSTPLYLGATAGMRLLNLTNPsaaDAILESVRDALKS---SKFGFDFRNARILSGEDEGLYGWITVNYLLGNLG 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258597746 233 SKPN--------NTYGAIDLGGSSTQITFYPMDHNILENYNSIL-LNNILIRLYSHSFIGYG 285
Cdd:cd24044  145 KYSIssiprsrpETVGALDLGGASTQITFEPAEPSLPADYTRKLrLYGKDYNVYTHSYLCYG 206
ASKHA_NBD_AtAPY3-like cd24042
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar ...
 76-285 1.05e-28

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: 119.47  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFE-WKKREYELSNKKEENNLielkeifNAKVKKSISTISYNEIKdiliylINKVIDHLIEKKIY 154
Cdd:cd24042    1 YSVIIDAGSSGTRLHVFGyAAESGKPVFPFGEKDYA-------SLKTTPGLSSFADNPSG------ASASLTELLEFAKE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 155 VYNKQKWKSYPFYFQATGGMRNLK---QED------RNLRMkyiknilsndnyNPFYFLNEYARILSGEEEGIYGWLAVN 225
Cdd:cd24042   68 RVPKGKRKETDIRLMATAGLRLLEvpvQEQilevcrRVLRS------------SGFMFRDEWASVISGTDEGIYAWVAAN 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 226 NLLNSIFSKPNNTYGAIDLGGSSTQITFYPMDHNILENYNSILLNNILIRLYSHSFIGYG 285
Cdd:cd24042  136 YALGSLGGDPLETTGIVELGGASAQVTFVPSEAVPPEFSRTLVYGGVSYKLYSHSFLDFG 195
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
 76-285 4.49e-27

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: 114.14  E-value: 4.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKreyelsnkKEENNLIEL-KEIFNAkVKKSISTISYNEIKDiliyliNKVIDHLIEKKIY 154
Cdd:cd24114    3 YGIMFDAGSTGTRIHIYTFVQ--------KSPAELPELdGEIFES-VKPGLSAYADQPEQG------AETVRGLLDVAKK 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 155 VYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFSK 234
Cdd:cd24114   68 TIPSTQWKKTPVVLKATAGLRLLPEEKAQALLSEVKEIFEE---SPFLVPEGSVSIMNGTYEGILAWVTVNFLTGQLYGQ 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 258597746 235 PNNTYGAIDLGGSSTQITFYPMDHNILEN-----YNSILLNNILIRLYSHSFIGYG 285
Cdd:cd24114  145 NQRTVGILDLGGASTQITFLPRFEKTLKQapedyLTSFEMFNSTYKLYTHSYLGFG 200
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
 76-285 5.46e-27

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: 113.76  E-value: 5.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKREYELSNKKEEnnlielkeIFNAkVKKSISTISYNEIKDiliyliNKVIDHLIEKKIYV 155
Cdd:cd24115    3 YGIMFDAGSTGTRIHIFKFTRPPNEAPKLTHE--------TFKA-LKPGLSAYADEPEKC------AEGIQELLDVAKQD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 YNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFSKP 235
Cdd:cd24115   68 IPSDFWKATPLVLKATAGLRLLPGEKAQKLLDKVKEVFKA---SPFLVGDDSVSIMDGTDEGISAWITVNFLTGSLHGTG 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 258597746 236 NNTYGAIDLGGSSTQITFYPMDHNILEN-----YNSILLNNILIRLYSHSFIGYG 285
Cdd:cd24115  145 RSSVGMLDLGGGSTQITFSPHSEGTLQTspidyITSFQMFNRTYTLYSHSYLGLG 199
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
 76-292 6.62e-25

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: 108.31  E-value: 6.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKreyelSNKKEENNLIE--LKEIFNAKVKKSISTiSYNEIK-----DILIY---LINKVI 145
Cdd:cd24043    1 YAIVMDCGSTGTRVYVYSWAR-----NPSKDSLPVMVdpPTVASAALVKKPKKR-AYKRVEtepglDKLADnetGLGAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 146 DHLIEKKIYVYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVN 225
Cdd:cd24043   75 GPLLDWAGKQIPRSQHPRTPVFLFATAGLRRLPPDDSAWLLDKAWGVLEA---SPFRFERSWVRIISGTEEAYYGWIALN 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258597746 226 NLLNSIFSKPNN--TYGAIDLGGSSTQITFYPMDHNILENYNSILLNNILIRLYSHSFIGYGWIDSLFR 292
Cdd:cd24043  152 YLTGRLGQGPGKgaTVGSLDLGGSSLEVTFEPEAVPRGEYGVNLSVGSTEHHLYAHSHAGYGLNDAFDK 220
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
 71-285 6.39e-24

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: 105.64  E-value: 6.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  71 QNEKeYGIIIDAGSNGTRIHLFEWKKreyelsnkKEENNLIELKEIFNAKVK-KSISTISyNEIKDILIYLinkviDHLI 149
Cdd:cd24110    3 ENVK-YGIVLDAGSSHTSLYIYKWPA--------EKENDTGVVQQLEECKVKgPGISSYS-QKTTKAGASL-----AECM 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 150 EKKIYVYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDNYNPFYFlnEYARILSGEEEGIYGWLAVNNLLN 229
Cdd:cd24110   68 KKAKEVIPASQHHETPVYLGATAGMRLLRMESEQAAEEVLASVERSLKSYPFDF--QGARIITGQEEGAYGWITINYLLG 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258597746 230 SI-----------FSKPNNTYGAIDLGGSSTQITFYPMDHNILENYNSIL--LNNILIRLYSHSFIGYG 285
Cdd:cd24110  146 NFkqdsgwftqlsGGKPTETFGALDLGGASTQITFVPLNSTIESPENSLQfrLYGTDYTVYTHSFLCYG 214
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
 76-285 5.00e-23

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: 102.54  E-value: 5.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKreyelsnkKEENNLIELKEIFNAKVKKS-ISTISYNEIKdiliylINKVIDHLIEKKIY 154
Cdd:cd24112    1 YGIVLDAGSSRTTVYVYQWPA--------EKENNTGVVSQTYKCNVKGPgISSYAHNPQK------AARALEECMNKVKE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 155 VYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDNYNPFYFLNeyARILSGEEEGIYGWLAVNNLLNSIFSK 234
Cdd:cd24112   67 IIPSHLHNSTPVYLGATAGMRLLKLQNETAANEVLSSIENYFKTLPFDFRG--AHIITGQEEGVYGWITANYLMGNFLEK 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258597746 235 PN----------NTYGAIDLGGSSTQITFYPMDhnILENYNSIL---LNNILIRLYSHSFIGYG 285
Cdd:cd24112  145 NLwnawvhphgvETVGALDLGGASTQIAFIPED--SLENLNDTVkvsLYGYKYNVYTHSFQCYG 206
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
 76-285 4.85e-21

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: 96.99  E-value: 4.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKK---REYELSNKKEENNliELKEIFNAKVKKSISTISYN--EIKDILIYLINKVIDHLIE 150
Cdd:cd24045    3 YGVVIDCGSSGSRVFVYTWPRhsgNPHELLDIKPLRD--ENGKPVVKKIKPGLSSFADKpeKASDYLRPLLDFAAEHIPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 151 KKIyvynkqkwKSYPFYFQATGGMRNLKQEDR-----NLRmkyiKNILSNDNynpFYFLNEYARILSGEEEGIYGWLAVN 225
Cdd:cd24045   81 EKH--------KETPLYILATAGMRLLPESQQeaileDLR----TDIPKHFN---FLFSDSHAEVISGKQEGVYAWIAIN 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 226 NLLNSiFSKPNN-------------------TYGAIDLGGSSTQITF-YPMDHNILENYNSILLNNILI----------- 274
Cdd:cd24045  146 YVLGR-FDHSEDddpavvvvsdnkeailrkrTVGILDMGGASTQIAFeVPKTVEFASPVAKNLLAEFNLgcdahdtehvy 224

                        250
                 ....*....|.
gi 258597746 275 RLYSHSFIGYG 285
Cdd:cd24045  225 RVYVTTFLGYG 235
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
 75-297 1.23e-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: 95.59  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  75 EYGIIIDAGSNGTRIHLFEWkkreyeLSNKkeENNLIELKEIFNAKVKKS-IStiSYNEIKDILIYLINKVIDhliEKKI 153
Cdd:cd24113   24 KYGIVFDAGSSHTSLFLYQW------PADK--ENGTGIVSQVLSCDVEGPgIS--SYAQNPAKAGESLKPCLD---EALA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 154 YVYNKQKWKSyPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDNYNPFYFlnEYARILSGEEEGIYGWLAVNNLLNS--- 230
Cdd:cd24113   91 AIPAEQQKET-PVYLGATAGMRLLRLQNSTQSDEILAEVSKTIGSYPFDF--QGARILTGMEEGAYGWITVNYLLETfik 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 231 -------IFSKPNNTYGAIDLGGSSTQITFYP----MDHNI-----LENYNSIllnnilirLYSHSFIGYGWIDSLFRVN 294
Cdd:cd24113  168 ysfegkwIHPKGGNILGALDLGGASTQITFVPggpiEDKNTeanfrLYGYNYT--------VYTHSYLCYGKDQMLKRLL 239


                 ...
gi 258597746 295 IYL 297
Cdd:cd24113  240 AAL 242
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
 76-285 2.79e-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: 94.43  E-value: 2.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKkreyelSNKkeENNLIELKEIFNAKVKKS-ISTISYNEIKdiliylINKVIDHLIEKKIY 154
Cdd:cd24111    4 YGIVLDAGSSHTSMFVYKWP------ADK--ENDTGIVSQHSSCDVQGGgISSYANDPSK------AGQSLVRCLEQALR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 155 VYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDNYNPFYFLNeyARILSGEEEGIYGWLAVNNLL-NSI-- 231
Cdd:cd24111   70 DVPRDRHASTPLYLGATAGMRLLNLTSPEASARVLEAVTQTLTSYPFDFRG--ARILSGQEEGVFGWVTANYLLeNFIky 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258597746 232 ------FSKPNNTYGAIDLGGSSTQITFYPMDHniLENYNSIL---LNNILIRLYSHSFIGYG 285
Cdd:cd24111  148 gwvgqwIRPRKGTLGAMDLGGASTQITFETTSP--SEDPGNEVhlrLYGQHYRVYTHSFLCYG 208
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
 76-285 7.18e-20

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: 93.17  E-value: 7.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLfewkkreYELSNKKEENNLIElKEIFNaKVKKSISTISYNEIKdiliylINKVIDHLIEKKIYV 155
Cdd:cd24040    1 YALMIDAGSTGSRIHV-------YRFNNCQPPIPKLE-DEVFE-MTKPGLSSYADDPKG------AAASLDPLLQVALQA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 156 YNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNDnYNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFSKP 235
Cdd:cd24040   66 VPKELHSCTPIAVKATAGLRLLGEDKSKEILDAVRHRLEKE-YPFVSVELDGVSIMDGKDEGVYAWITVNYLLGNIGGNE 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 258597746 236 NN-TYGAIDLGGSSTQITFYPMDHNILENYNS-----ILLNNILIRLYSHSFIGYG 285
Cdd:cd24040  145 KLpTAAVLDLGGGSTQIVFEPDFPSDEEDPEGdhkyeLTFGGKDYVLYQHSYLGYG 200
ASKHA_NBD_AtAPY1-like cd24041
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), ...
 76-285 4.11e-15

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: 78.13  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  76 YGIIIDAGSNGTRIHLFEWKKREYELsnkkEENNLIELKEifnaKVKKSISTISYNEIK--DILIYLINKVIDhliekki 153
Cdd:cd24041    2 YAVVFDAGSTGSRVHVFKFDQNLDLL----HLGLDLELFE----QIKPGLSSYADDPEQaaKSLRPLLDKALA------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 154 yVYNKQKWKSYPFYFQATGGMRNLKQEDRNLRMKYIKNILSNdnyNPFYFLNEYARILSGEEEGIYGWLAVNNLLNSIFS 233
Cdd:cd24041   67 -VVPEELQSKTPVRLGATAGLRLLPGDASENILQEVRDLLRN---YSFKVQPDAVSIIDGTDEGSYQWVTVNYLLGNLGK 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258597746 234 KPNNTYGAIDLGGSSTQITFY---------PMDHNILENY-NSILLNNILIRLYSHSFIGYG 285
Cdd:cd24041  143 PFTKTVGVVDLGGGSVQMAYAvsdetaknaPKPTDGEDGYiRKLVLKGKTYDLYVHSYLGYG 204
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
 631-767 1.53e-13

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: 73.47  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 631 INITVRIVGSNDFKKCLENTKKLFYE-QPCFLSSCSFNGIYQPNLeNNKFVLHGQFKKVITYLGFKKYVDLNQMKIYIQK 709
Cdd:cd24044  263 NNTNFTFNGTSNPDQCRELVRKLFNFtSCCSSGCCSFNGVFQPPL-NGNFYAFSGFYYTADFLNLTSNGSLDEFREAVDD 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 710 LCNMNlYELTYNMSNKImHNQIPTFCWKSIWSYSLLFYGFKFKETT--KLLIINDNTNIS 767
Cdd:cd24044  342 FCNKP-WDEVSELPPKG-AKFLANYCFDANYILTLLTDGYGFTEETwrNIHFVKKVNGTE 399
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
 621-755 1.19e-09

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: 61.30  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 621 IINEKIKKLYINITVRIVGSNDFKKCLENTKKLFYEQPCFLSSCSFNGIYQPNLENNkFVLHGQFKKVITYLG--FKKYV 698
Cdd:cd24111  254 TMGQRPRAFNGSAIVSLSGTSNATLCRDLVSRLFNFSSCPFSQCSFNGVFQPPVTGN-FIAFSAFYYTVDFLTtvMGLPV 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 258597746 699 D-LNQMKIYIQKLCNMNLYELTYNMSNKImhNQIPTFCWKSIWSYSLLFYGFKFKETT 755
Cdd:cd24111  333 GtPKQLEEATEIICNQTWTELQAKVPGQE--TRLADYCAVAMFIHQLLSRGYHFDERS 388
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
 648-765 1.55e-09

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: 60.48  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 648 ENTKKLFYEQPCFLSSCsfngiyqpnleNNKFVLHGQFKKVITYLGFKKY--VDLNQMKIYIQKLCNMNLYELTYnMSNK 725
Cdd:cd24003  213 NNSEGGNVTNPCLPKGY-----------TGPFYAFSNFYYTAKFLGLVDSgtFTLEELEEAAREFCSLDWAELKA-KYPG 280

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 258597746 726 IMHNQIPTFCWKSIWSYSLLFYGFKFKETTKLLIINDNTN 765
Cdd:cd24003  281 VDDDFLPNLCFDAAYIYSLLEDGFGLDDDSPIIKFVDKIN 320
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
 568-751 2.03e-09

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: 60.58  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 568 LKLKIINNNMSLMDNIYED--FkNKGYLNNVlkkvndnKISNTLKNEIIKRLFEKIINEKIKklyinitvrIVGSNDFKK 645
Cdd:cd24110  219 LWQKLAQDIQSTSGGILKDpcF-HPGYKRVV-------NVSELYGTPCTKRFEKKLPFNQFQ---------VQGTGNYEQ 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 646 CLENTKKLFYEQPCFLSSCSFNGIYQPNLEnNKFVLHGQFKKVITYLGFKKYVD-LNQMKIYIQKLCNMNLYELTYNMSn 724
Cdd:cd24110  282 CHQSILKIFNNSHCPYSQCSFNGVFLPPLQ-GSFGAFSAFYFVMDFLNLTANVSsLDKMKETIKNFCSKPWEEVKASYP- 359

                        170       180
                 ....*....|....*....|....*..
gi 258597746 725 KIMHNQIPTFCWKSIWSYSLLFYGFKF 751
Cdd:cd24110  360 KVKEKYLSEYCFSGTYILSLLEQGYNF 386
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
591-757 8.65e-08

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 55.51  E-value: 8.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  591 GY-LNNVLKKVNdNKISNTLKNEIIK-----RLFEKIINEKikKLYINItVRIVGSNDFKKCLENTKKLFYEQ-PCFLSS 663
Cdd:pfam01150 209 GYgANEALRKYL-AKLIQNLSNGILNdpcmpPGYNKTVEVS--TLEGKQ-FAIQGTGNWEQCRQSILELLNKNaHCPYEP 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  664 CSFNGIYQPNLENNK---------FVLHGQFKKVITYLGFKKYVDLnqmkiyIQKLCNMNlYELTYNMSNKIMHNQIP-- 732
Cdd:pfam01150 285 CAFNGVHAPSIGSLQksfgassyfYTVMDFFGLGGEYSSQEKFTDI------ARKFCSKN-WNDIKAGFPKVLDKNISee 357

                         170       180
                  ....*....|....*....|....*
gi 258597746  733 TFCWKSIWSYSLLFYGFKFKETTKL 757
Cdd:pfam01150 358 TYCFKGAYILSLLHDGFNFPKTEEI 382
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
 632-755 2.07e-07

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: 54.38  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 632 NITVriVGSNDFKKCLENTKKLFYEQPCFLS-SCSFNGIYQPNLeNNKFVLHGQFKKVITYLGFKKYVDLNQMKIYIQKL 710
Cdd:cd24113  287 NITV--EGTGNPAECLSAIRNLFNFTACGGSqTCAFNGVYQPPV-NGEFFAFSAFYYTFDFLNLTSGQSLSTVNSTIWEF 363

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 258597746 711 CNMNLYELTYNMSnKIMHNQIPTFCWKSIWSYSLLFYGFKFKETT 755
Cdd:cd24113  364 CSKPWTELEASYP-KEKDKRLKDYCASGLYILTLLVDGYKFDSET 407
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
 79-267 1.03e-05

nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (HpPPX/GppA) 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 a group of proteins similar to Helicobacter pylori PPX/GppA (HpPPX/GppA). HpPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, H. pylori encodes only one PPX/GppA homolog, HpPPX/GppA. As such, HpPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.


Pssm-ID: 466902 [Multi-domain]  Cd Length: 298  Bit Score: 48.25  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746  79 IIDAGSNGTRIHLFEWKKREY-ELSNKKE----ENNLIELKEIFNAKVKKSISTIsyNEIKDILiyLINKVidhlieKKI 153
Cdd:cd24052    3 IIDIGSNSIRLVIYEIEGGSFrLLFNEKEtvglGEYLDEDGKLSEEGIERAIKAL--KRFKKIC--EALGV------DEI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 154 YVYnkqkwksypfyfqATGGMRNLKqeDRNLRMKYIKNILsndNYNPfyflneyaRILSGEEEGIYGWLAVnnlLNSIfs 233
Cdd:cd24052   73 IAF-------------ATAALRNAK--NGEEFLERIKKET---GIDI--------RVLSGEEEAYYGFLGV---LNSL-- 121

                        170       180       190
                 ....*....|....*....|....*....|....
gi 258597746 234 kPNNTYGAIDLGGSSTQITFYpmDHNILENYNSI 267
Cdd:cd24052  122 -PLADGLVVDIGGGSTELVLF--KNGKIKESISL 152
ASKHA_NBD_TgNTPase-like cd24037
nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) ...
 140-257 1.99e-05

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: 48.32  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 140 LINKVIDhLIEKKIYVYNKQKWKSY--PFYFQATGGMRNLKQEDRN----LRMKYIKNILSNDNYNpfYFLN-EYARILS 212
Cdd:cd24037   98 LEEDTVA-ILDSQLNEEQKVQVKALgvPVMLCSTAGVRDFHDWYRDalfvLLRHLINNPSPAHGYK--FFTNpFWTRPIT 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 258597746 213 GEEEGIYGWLAVNNLLN--SIFSKP------------NNTYGAIDLGGSSTQITFyPMD 257
Cdd:cd24037  175 GAEEGLFAFITLNHLSRrlGEDPARcmideygvkqcrNDLAGVVEVGGASAQIVF-PLQ 232
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
 623-755 1.13e-04

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: 45.53  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 623 NEKIKKLYINITVRIVGSNDFKKCLENTKKLFYEQPCF-LSSCSFNGIYQPNLeNNKFVLHGQFKKVITYLGFKKYVDLN 701
Cdd:cd24112  254 SQRPANYDPDDSITFTGTGDPALCKEKVSLLFDFKSCQgKENCSFDGIYQPKV-KGKFVAFAGFYYTASALNLTGSFTLT 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258597746 702 QMKIYIQKLCNMNLYELTYNMSNKiMHNQIPTFCWKSIWSYSLLFYGFKFKETT 755
Cdd:cd24112  333 TFNSSMWSFCSQSWAQLKVMLPKF-EERYARSYCFSANYIYTLLVRGYKFDPET 385
ASKHA_NBD_AaPPX-GppA_MtPPX2-like cd24054
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, ...
 209-253 2.07e-04

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: 44.39  E-value: 2.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 258597746 209 RILSGEEEGIYGWLAVNNLLNSifskPNNTYGAIDLGGSSTQITF 253
Cdd:cd24054  102 EIISGEEEARLSFLGALSGLPL----PDGPILVIDIGGGSTELIL 142
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
 634-758 3.03e-04

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: 44.22  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 634 TVRIVGSNDFKKCLENTKKLF-YEQPCFLSSCSFNGIYQP--NLENNKF------------VLH--GQFKkvitYLGFKK 696
Cdd:cd24045  287 TIHLRGTGDFELCRQSLKPLLnKTNPCQKSPCSLNGVYQPpiDFSNSEFygfsefwyttedVLRmgGPYD----YEKFTK 362

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258597746 697 YVdlnqmKIY-------IQKLCNMNLYeltYNMSNKIMHNQiptfCWKSIWSYSLLFYGFKFKETTKLL 758
Cdd:cd24045  363 AA-----KDYcatrwslLEERFKKGLY---PKADEHRLKTQ----CFKSAWMTSVLHDGFSFPKNYKNL 419
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
 616-674 2.65e-03

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: 41.17  E-value: 2.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597746 616 RLFEKIINEKIKKLYINITvrIVGSNDFKKCLENTKKLFYEQP-CFLSSCSFNGIYQPNL 674
Cdd:cd24040  240 YTKTVDLVQPEKSKKNVMV--GGGKGSFEACRRLVEKVLNKDAeCESKPCSFNGVHQPSL 297
 
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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