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Conserved domains on  [gi|1013384490|ref|NP_001308914|]
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nucleoside diphosphate phosphatase ENTPD5 isoform 1 precursor [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_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
47-421 0e+00

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: 787.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  47 TLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVV 126
Cdd:cd24114     1 TFYGIMFDAGSTGTRIHIYTFVQKSPAELPELDGEIFESVKPGLSAYADQPEQGAETVRGLLDVAKKTIPSTQWKKTPVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 127 LKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQ 206
Cdd:cd24114    81 LKATAGLRLLPEEKAQALLSEVKEIFEESPFLVPEGSVSIMNGTYEGILAWVTVNFLTGQLYGQNQRTVGILDLGGASTQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 207 ITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGV 286
Cdd:cd24114   161 ITFLPRFEKTLKQAPEDYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALGTEDQEKQVFRSSCLPKGLKAEWKFGGV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 287 KYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNL 366
Cdd:cd24114   241 TYKYGGNKEGETGFKSCYSEVLKVVKGKLHQPEEMQHSSFYAFSYYYDRAVDTGLIDYEQGGVLEVKDFEKKAKEVCENL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1013384490 367 ENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLL 421
Cdd:cd24114   321 ERYSSGSPFLCMDLTYITALLKEGFGFEDNTVLQLTKKVNNVETSWTLGAIFHLL 375
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
47-421 0e+00

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: 787.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  47 TLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVV 126
Cdd:cd24114     1 TFYGIMFDAGSTGTRIHIYTFVQKSPAELPELDGEIFESVKPGLSAYADQPEQGAETVRGLLDVAKKTIPSTQWKKTPVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 127 LKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQ 206
Cdd:cd24114    81 LKATAGLRLLPEEKAQALLSEVKEIFEESPFLVPEGSVSIMNGTYEGILAWVTVNFLTGQLYGQNQRTVGILDLGGASTQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 207 ITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGV 286
Cdd:cd24114   161 ITFLPRFEKTLKQAPEDYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALGTEDQEKQVFRSSCLPKGLKAEWKFGGV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 287 KYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNL 366
Cdd:cd24114   241 TYKYGGNKEGETGFKSCYSEVLKVVKGKLHQPEEMQHSSFYAFSYYYDRAVDTGLIDYEQGGVLEVKDFEKKAKEVCENL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1013384490 367 ENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLL 421
Cdd:cd24114   321 ERYSSGSPFLCMDLTYITALLKEGFGFEDNTVLQLTKKVNNVETSWTLGAIFHLL 375
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
39-424 1.46e-83

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 261.98  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  39 CPINVSastlYGIMFDAGSTGTRIHVYTFVQKMPGQLPI-LEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPR 117
Cdd:pfam01150   4 LPENVK----YGIIIDAGSSGTRLHVYKWPDEKEGLTPIvPLIEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 118 SHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRK-SPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVG 196
Cdd:pfam01150  80 EKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSlTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPKQSTFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 197 TLDLGGASTQITFLPQFE----KTLEQTPRGYLTSFEMFNstYKLYTHSYLGFGLKAARLATLGALETEGTDGhTFRSAC 272
Cdd:pfam01150 160 AIDLGGASTQIAFEPSNEsainSTVEDIELGLQFRLYDKD--YTLYVHSFLGYGANEALRKYLAKLIQNLSNG-ILNDPC 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 273 LPRWLEAEWIFGGVKY-QYGGNQEGEvgFEPCYAEVLRVVRGKLHQPEE-------------VQRGSFYAFSYYYdravd 338
Cdd:pfam01150 237 MPPGYNKTVEVSTLEGkQFAIQGTGN--WEQCRQSILELLNKNAHCPYEpcafngvhapsigSLQKSFGASSYFY----- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 339 TDMIDYEKGG-ILKVEDFERKAREVCD-NLENFTSGSP----------FLCMDLSYITALLKDGFGFADSTVLQLTKKVN 406
Cdd:pfam01150 310 TVMDFFGLGGeYSSQEKFTDIARKFCSkNWNDIKAGFPkvldkniseeTYCFKGAYILSLLHDGFNFPKTEEIQSVGKIA 389
                         410
                  ....*....|....*...
gi 1013384490 407 NIETGWALGATFHLLQSL 424
Cdd:pfam01150 390 GKEAGWTLGAMLNLTSMI 407
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
47-421 0e+00

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: 787.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  47 TLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVV 126
Cdd:cd24114     1 TFYGIMFDAGSTGTRIHIYTFVQKSPAELPELDGEIFESVKPGLSAYADQPEQGAETVRGLLDVAKKTIPSTQWKKTPVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 127 LKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQ 206
Cdd:cd24114    81 LKATAGLRLLPEEKAQALLSEVKEIFEESPFLVPEGSVSIMNGTYEGILAWVTVNFLTGQLYGQNQRTVGILDLGGASTQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 207 ITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGV 286
Cdd:cd24114   161 ITFLPRFEKTLKQAPEDYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALGTEDQEKQVFRSSCLPKGLKAEWKFGGV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 287 KYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNL 366
Cdd:cd24114   241 TYKYGGNKEGETGFKSCYSEVLKVVKGKLHQPEEMQHSSFYAFSYYYDRAVDTGLIDYEQGGVLEVKDFEKKAKEVCENL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1013384490 367 ENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLL 421
Cdd:cd24114   321 ERYSSGSPFLCMDLTYITALLKEGFGFEDNTVLQLTKKVNNVETSWTLGAIFHLL 375
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
49-421 0e+00

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: 599.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLK 128
Cdd:cd24046     1 YAIVFDAGSTGSRVHVFKFSHSPSGGPLKLLDELFEEVKPGLSSYADDPKEAADSLKPLLEKAKTRIPKEKWSSTPLALK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 129 ATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQIT 208
Cdd:cd24046    81 ATAGLRLLPEEKANAILDEVRKLFKKSPFLVGEDSVSIMDGTDEGIFSWFTVNFLLGRLGGSASNTVAALDLGGGSTQIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 209 FLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHT-FRSACLPRWLEAEWIFGGVK 287
Cdd:cd24046   161 FAPSDKETLSASPKGYLHKVSIFGKKIKLYTHSYLGLGLMAARLAILQGSSTNSNSGTTeLKSPCFPPNFKGEWWFGGKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 288 YQYGGNQEGEVGFEPCYAEVLRVVRGK-LHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNL 366
Cdd:cd24046   241 YTSSIGGSSEYSFDACYKLAKKVVDSSvIHKPEELKSREIYAFSYFYDRAVDAGLIDEQEGGTVTVGDFKKAAKKACSNP 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1013384490 367 EnftSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLL 421
Cdd:cd24046   321 N---PEQPFLCLDLTYIYALLHDGYGLPDDKKLTLVKKINGVEISWALGAAFDLL 372
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
48-419 5.88e-176

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: 496.26  E-value: 5.88e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  48 LYGIMFDAGSTGTRIHVYTFVQKmPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVL 127
Cdd:cd24115     2 FYGIMFDAGSTGTRIHIFKFTRP-PNEAPKLTHETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDFWKATPLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 128 KATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQI 207
Cdd:cd24115    81 KATAGLRLLPGEKAQKLLDKVKEVFKASPFLVGDDSVSIMDGTDEGISAWITVNFLTGSLHGTGRSSVGMLDLGGGSTQI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 208 TFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETE-GTDGHTFRSACLPRWLEAEWIFGGV 286
Cdd:cd24115   161 TFSPHSEGTLQTSPIDYITSFQMFNRTYTLYSHSYLGLGLMSARLAILGGVEGKpLKEGQELVSPCLAPEYKGEWEHAEI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 287 KYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNL 366
Cdd:cd24115   241 TYKIKGQKAEEPLYESCYARVEKMLYKKVHKAEEVKNLDFYAFSYYYDRAVDVGLIDEEKGGSLKVGDFEIAAKKVCKTM 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1013384490 367 ENFTSGSPFLCMDLSYITALLKDgFGFADSTVLQLTKKVNNIETGWALGATFH 419
Cdd:cd24115   321 ESQPGEKPFLCMDLTYISVLLQE-LGFPKDKELKLARKIDNVETSWALGATFH 372
ASKHA_NBD_AtAPY1-like cd24041
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), ...
49-416 3.03e-104

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: 314.65  E-value: 3.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKMpGQLPI-LEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVL 127
Cdd:cd24041     2 YAVVFDAGSTGSRVHVFKFDQNL-DLLHLgLDLELFEQIKPGLSSYADDPEQAAKSLRPLLDKALAVVPEELQSKTPVRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 128 KATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQI 207
Cdd:cd24041    81 GATAGLRLLPGDASENILQEVRDLLRNYSFKVQPDAVSIIDGTDEGSYQWVTVNYLLGNLGKPFTKTVGVVDLGGGSVQM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 208 TFLPQfEKTLEQTPR------GYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGAleTEGTDGHtfrsACLPRWLEAEW 281
Cdd:cd24041   161 AYAVS-DETAKNAPKptdgedGYIRKLVLKGKTYDLYVHSYLGYGLMAARAEILKL--TEGTSAS----PCIPAGFDGTY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 282 IFGGVKYQYGGNQEGeVGFEPCYAEVLRVVrgKLHQPEEVQRGSF---------------YAFSYYYDRAVDTDMI-DYE 345
Cdd:cd24041   234 TYGGEEYKAVAGESG-ADFDKCKKLALKAL--KLDEPCGYEQCTFggvwnggggggqkklFVASYFFDRASEVGIIdDQA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 346 KGGILKVEDFERKAREVCD-NLENFTS--------GSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVN----NIETGW 412
Cdd:cd24041   311 SQAVVRPSDFEKAAKKACKlNVEEIKSkyplveekDAPFLCMDLTYQYTLLVDGFGLDPDQEITLVKQIEyqgaLVEAAW 390

                  ....
gi 1013384490 413 ALGA 416
Cdd:cd24041   391 PLGA 394
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
49-421 2.74e-102

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: 310.04  E-value: 2.74e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKMPGQlPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLK 128
Cdd:cd24040     1 YALMIDAGSTGSRIHVYRFNNCQPPI-PKLEDEVFEMTKPGLSSYADDPKGAAASLDPLLQVALQAVPKELHSCTPIAVK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 129 ATAGLRLLPEHKAKALLFEVKEIFRKSPFLVP--KGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQ-ETVGTLDLGGAST 205
Cdd:cd24040    80 ATAGLRLLGEDKSKEILDAVRHRLEKEYPFVSveLDGVSIMDGKDEGVYAWITVNYLLGNIGGNEKlPTAAVLDLGGGST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 206 QITFLPQFEKTlEQTPRGYLTSFEMFN-STYKLYTHSYLGFGLKAAR---------LATLGALETEGTDGHTFRSACLPR 275
Cdd:cd24040   160 QIVFEPDFPSD-EEDPEGDHKYELTFGgKDYVLYQHSYLGYGLMEARkkihklvaeNASTGGSEGEATEGGLIANPCLPP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 276 WLEAE--WIFGGVKYQYGGNQEGEVGFEPCyAEVLRVVRGK-------------LHQP---EEVQRGSFYAFSYYYDRAV 337
Cdd:cd24040   239 GYTKTvdLVQPEKSKKNVMVGGGKGSFEAC-RRLVEKVLNKdaeceskpcsfngVHQPslaETFKDGPIYAFSYFYDRLN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 338 DTDMidyeKGGILKVEDFERKAREVC----------------DNLENftsgSPFLCMDLSYITALLKDGFGFADSTVLQL 401
Cdd:cd24040   318 PLGM----EPSSFTLGELQKLAEQVCkgetswddffgidvllDELKD----NPEWCLDLTFMLSLLRTGYELPLDRELKI 389
                         410       420
                  ....*....|....*....|
gi 1013384490 402 TKKVNNIETGWALGATFHLL 421
Cdd:cd24040   390 AKKIDGFELGWCLGASLAML 409
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
49-416 5.51e-96

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: 291.21  E-value: 5.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPG---LSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPV 125
Cdd:cd24003     1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIELVSSGKEKSGkisSSSYADDPDEAKKYLQPLLEFAKAVVPEDRRSSTPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 126 VLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGH-RQETVGTLDLGGAS 204
Cdd:cd24003    81 YLLATAGMRLLPEEQQEAILDAVRTILRNSGFGFDDGWVRVISGEEEGLYGWLSVNYLLGNLGSEpAKKTVGVLDLGGAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 205 TQITFLPqfeKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFrSACLPRwleaewifg 284
Cdd:cd24003   161 TQIAFEP---PEDDLSSLSNVYPLRLGGKTYDLYSHSFLGYGLNEARKRVLESLINNSEGGNVT-NPCLPK--------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 285 gvkyqyggnqegevGFepcyaevlrvvrgklhqpeevqRGSFYAFSYYYDRAVDTDMIDYEKggiLKVEDFERKAREVCD 364
Cdd:cd24003   228 --------------GY----------------------TGPFYAFSNFYYTAKFLGLVDSGT---FTLEELEEAAREFCS 268
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013384490 365 N----LENFTSGS-----PFLCMDLSYITALLKDGFGFAD-STVLQLTKKVNNIETGWALGA 416
Cdd:cd24003   269 LdwaeLKAKYPGVdddflPNLCFDAAYIYSLLEDGFGLDDdSPIIKFVDKINGVELSWTLGA 330
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
39-424 1.46e-83

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 261.98  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  39 CPINVSastlYGIMFDAGSTGTRIHVYTFVQKMPGQLPI-LEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPR 117
Cdd:pfam01150   4 LPENVK----YGIIIDAGSSGTRLHVYKWPDEKEGLTPIvPLIEEFKKLEPGLSSFATKPDAAANYLTPLLEFAEEHIPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 118 SHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRK-SPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVG 196
Cdd:pfam01150  80 EKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSlTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPKQSTFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 197 TLDLGGASTQITFLPQFE----KTLEQTPRGYLTSFEMFNstYKLYTHSYLGFGLKAARLATLGALETEGTDGhTFRSAC 272
Cdd:pfam01150 160 AIDLGGASTQIAFEPSNEsainSTVEDIELGLQFRLYDKD--YTLYVHSFLGYGANEALRKYLAKLIQNLSNG-ILNDPC 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 273 LPRWLEAEWIFGGVKY-QYGGNQEGEvgFEPCYAEVLRVVRGKLHQPEE-------------VQRGSFYAFSYYYdravd 338
Cdd:pfam01150 237 MPPGYNKTVEVSTLEGkQFAIQGTGN--WEQCRQSILELLNKNAHCPYEpcafngvhapsigSLQKSFGASSYFY----- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 339 TDMIDYEKGG-ILKVEDFERKAREVCD-NLENFTSGSP----------FLCMDLSYITALLKDGFGFADSTVLQLTKKVN 406
Cdd:pfam01150 310 TVMDFFGLGGeYSSQEKFTDIARKFCSkNWNDIKAGFPkvldkniseeTYCFKGAYILSLLHDGFNFPKTEEIQSVGKIA 389
                         410
                  ....*....|....*...
gi 1013384490 407 NIETGWALGATFHLLQSL 424
Cdd:pfam01150 390 GKEAGWTLGAMLNLTSMI 407
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
49-415 1.40e-71

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: 231.01  E-value: 1.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTF-VQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVL 127
Cdd:cd24044     1 YGIVIDAGSSHTSLFVYKWpADKENGTGVVQQVSTCRVKGGGISSYENNPSQAGESLEPCLDQAKKKVPEDRRHSTPLYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 128 KATAGLRLL----PEhKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQL--------HGHRQETV 195
Cdd:cd24044    81 GATAGMRLLnltnPS-AADAILESVRDALKSSKFGFDFRNARILSGEDEGLYGWITVNYLLGNLgkysissiPRSRPETV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 196 GTLDLGGASTQITFLPQfEKTLeqtPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPR 275
Cdd:cd24044   160 GALDLGGASTQITFEPA-EPSL---PADYTRKLRLYGKDYNVYTHSYLCYGKDEAERRYLASLVQESNYSSTVENPCAPK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 276 ----WLEAEWIFG---GVKYQYGGNQEGEVGF--------EPCYAEVLRVVRGKLHQPEE------VQ----RGSFYAFS 330
Cdd:cd24044   236 gystNVTLAEIFSspcTSKPLSPSGLNNNTNFtfngtsnpDQCRELVRKLFNFTSCCSSGccsfngVFqpplNGNFYAFS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 331 -YYYdravDTDMIDYEKGGILkvEDFERKAREVC----DNLENFT-SGSPFL---CMDLSYITALLKDGFGFADSTV--L 399
Cdd:cd24044   316 gFYY----TADFLNLTSNGSL--DEFREAVDDFCnkpwDEVSELPpKGAKFLanyCFDANYILTLLTDGYGFTEETWrnI 389
                         410
                  ....*....|....*.
gi 1013384490 400 QLTKKVNNIETGWALG 415
Cdd:cd24044   390 HFVKKVNGTEVGWSLG 405
ASKHA_NBD_AtAPY3-like cd24042
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar ...
49-416 4.81e-63

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: 208.07  E-value: 4.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVK--PGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVV 126
Cdd:cd24042     1 YSVIIDAGSSGTRLHVFGYAAESGKPVFPFGEKDYASLKttPGLSSFADNPSGASASLTELLEFAKERVPKGKRKETDIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 127 LKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQ 206
Cdd:cd24042    81 LMATAGLRLLEVPVQEQILEVCRRVLRSSGFMFRDEWASVISGTDEGIYAWVAANYALGSLGGDPLETTGIVELGGASAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 207 ITFLPQfektlEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGAL---ETEGTDGHTFRSACLPRwleaEWIF 283
Cdd:cd24042   161 VTFVPS-----EAVPPEFSRTLVYGGVSYKLYSHSFLDFGQEAAWDKLLESLlngAAKSTRGGVVVDPCTPK----GYIP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 284 GG--VKYQYGGNQEGEVG---------FEPCYAEVLRVVR-------------GKLHQPEevQRGSFYAF-SYYY----- 333
Cdd:cd24042   232 DTnsQKGEAGALADKSVAagslqaagnFTECRSAALALLQegkdnclykhcsiGSTFTPE--LRGKFLATeNFFYtseff 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 334 ---DRAVDTDMIDY------EKGGILKVedfERKAREVCDNLEnftsgspfLCMDLSYITALLKDGFGFA-DSTVLQLTK 403
Cdd:cd24042   310 glgETTWLSEMILAgerfcgEDWSKLKK---KHPGWEEEDLLK--------YCFSAAYIVAMLHDGLGIAlDDERIRYAN 378
                         410
                  ....*....|...
gi 1013384490 404 KVNNIETGWALGA 416
Cdd:cd24042   379 KVGEIPLDWALGA 391
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
49-419 7.64e-51

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: 177.50  E-value: 7.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKM--PGQLPILE------GE-VFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSH 119
Cdd:cd24045     3 YGVVIDCGSSGSRVFVYTWPRHSgnPHELLDIKplrdenGKpVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPREK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 120 WKKTPVVLKATAGLRLLPEHKAKALLFEVKE-IFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQL-HGH------- 190
Cdd:cd24045    83 HKETPLYILATAGMRLLPESQQEAILEDLRTdIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFdHSEdddpavv 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 191 ----------RQETVGTLDLGGASTQITF-LPQFEKTLEQTPRGYLTSFEMFNS------TYKLYTHSYLGFGLKAAR-- 251
Cdd:cd24045   163 vvsdnkeailRKRTVGILDMGGASTQIAFeVPKTVEFASPVAKNLLAEFNLGCDahdtehVYRVYVTTFLGYGANEARqr 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 252 ---------LATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNqeGEvgFEPCYAEVLRVV----------- 311
Cdd:cd24045   243 yedslvsstKSTNRLKQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGT--GD--FELCRQSLKPLLnktnpcqkspc 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 312 --RGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIdyekGGILKVEDFERKAREVC-----DNLENFTSG-SP--------F 375
Cdd:cd24045   319 slNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRM----GGPYDYEKFTKAAKDYCatrwsLLEERFKKGlYPkadehrlkT 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1013384490 376 LCMDLSYITALLKDGFGF-ADSTVLQLTKKVNNIETGWALGATFH 419
Cdd:cd24045   395 QCFKSAWMTSVLHDGFSFpKNYKNLKSAQLIYGKEVQWTLGALLY 439
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
49-416 6.64e-48

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: 167.92  E-value: 6.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTF----------VQKMPGQLPILEGEVFDS------VKPGLSAFVDQPKQGAETVQGLLEVAK 112
Cdd:cd24039     3 YGIVIDAGSSGSRVQIYSWkdpesatskaSLEELKSLPHIETGIGDGkdwtlkVEPGISSFADHPHVVGEHLKPLLDFAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 113 DSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRK-SPFLVPKGS--VSIMDGSDEGILAWVTVNFLTGQLH- 188
Cdd:cd24039    83 NIIPPSVHSSTPIFLLATAGMRLLPQDQQNAILDAVCDYLRKnYPFLLPDCSehVQVISGEEEGLYGWLAVNYLMGGFDd 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 189 ------GHRQETVGTLDLGGASTQITFLPqfEKTLEQTPRGYLTSFE--MFNST---YKLYTHSYLGFGLKAARLATLGA 257
Cdd:cd24039   163 apkhsiAHDHHTFGFLDMGGASTQIAFEP--NASAAKEHADDLKTVHlrTLDGSqveYPVFVTTWLGFGTNEARRRYVES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 258 L-ETEGTD---------GHTFRSACLPRWLEAEWiFGGVkyqyggnqegevgfepcyaevlrvvrgklhqpeevqrgSFY 327
Cdd:cd24039   241 LiEQAGSDtnsksnsssELTLPDPCLPLGLENNH-FVGV--------------------------------------SEY 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 328 AFSYYydravdtDMidYEKGGILKVEDFERKAREVC--------DNLENFTSGS-------PFLCMDLSYITALLKDGFg 392
Cdd:cd24039   282 WYTTQ-------DV--FGLGGAYDFVEFEKAAREFCskpwesilHELEAGKAGNsvdenrlQMQCFKAAWIVNVLHEGF- 351
                         410       420
                  ....*....|....*....|....
gi 1013384490 393 fadstvlQLTKKVNNIETGWALGA 416
Cdd:cd24039   352 -------QSVNKIDDTEVSWTLGK 368
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
49-416 1.06e-46

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: 165.70  E-value: 1.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFVQKMPGQ-LPILE--------GEVFDSVK---------PGLSAFVDQPKQGAETVQGLLEV 110
Cdd:cd24043     1 YAIVMDCGSTGTRVYVYSWARNPSKDsLPVMVdpptvasaALVKKPKKraykrvetePGLDKLADNETGLGAALGPLLDW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 111 AKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGH 190
Cdd:cd24043    81 AGKQIPRSQHPRTPVFLFATAGLRRLPPDDSAWLLDKAWGVLEASPFRFERSWVRIISGTEEAYYGWIALNYLTGRLGQG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 191 RQE--TVGTLDLGGASTQITFLPqfektlEQTPRG-YLTSFEMFNSTYKLYTHSYLGFGLKAA--RLATL---------- 255
Cdd:cd24043   161 PGKgaTVGSLDLGGSSLEVTFEP------EAVPRGeYGVNLSVGSTEHHLYAHSHAGYGLNDAfdKSVALllkdqnatpp 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 256 -----GALETE------GTDGHTFRSAC--LPRWLEAEWIFGGVKYQYggnqEGEVGFEPCYAEVLRVVR---------- 312
Cdd:cd24043   235 vrlreGTLEVEhpclhsGYNRPYKCSHHagAPPVRGLKAGPGGASVQL----VGAPNWGACQALAGRVVNttasaecefp 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 313 ----GKlHQPEevQRGSFYAFS-----YYYDRAVDTDMIDyekggilkveDFERKAREVCD----NLENFTSGSPFL--- 376
Cdd:cd24043   311 pcalGK-HQPR--PQGQFYALTgffvvYKFFGLSATASLD----------DLLAKGQEFCGkpwqVARASVPPQPFIery 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1013384490 377 CMDLSYITALLKDGFGFADSTVlqltkKVNNIETGWALGA 416
Cdd:cd24043   378 CFRAPYVVSLLREGLHLRDEQI-----QIGSGDVGWTLGA 412
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
49-415 1.79e-42

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: 154.16  E-value: 1.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFvqkmPGQLPILEGEVFDSVK-----PGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKT 123
Cdd:cd24112     1 YGIVLDAGSSRTTVYVYQW----PAEKENNTGVVSQTYKcnvkgPGISSYAHNPQKAARALEECMNKVKEIIPSHLHNST 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 124 PVVLKATAGLRLLP---EHKAKALLFEVKEIFRKSPFLVpkGSVSIMDGSDEGILAWVTVNFLTGQL----------HGH 190
Cdd:cd24112    77 PVYLGATAGMRLLKlqnETAANEVLSSIENYFKTLPFDF--RGAHIITGQEEGVYGWITANYLMGNFleknlwnawvHPH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 191 RQETVGTLDLGGASTQITFLPQ-----FEKTLEQTPRGYLtsfemfnstYKLYTHSYLGFGLKAARLATLGALETEGTDG 265
Cdd:cd24112   155 GVETVGALDLGGASTQIAFIPEdslenLNDTVKVSLYGYK---------YNVYTHSFQCYGKDEAEKRFLANLAQASESK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 266 HTFRSACLPR----WLEAEWIFGG------VKYQYGGNQE----GEVGFEPCYAEV-----LRVVRGK-------LHQPE 319
Cdd:cd24112   226 SPVDNPCYPRgyntSFSMKHIFGSlctasqRPANYDPDDSitftGTGDPALCKEKVsllfdFKSCQGKencsfdgIYQPK 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 320 evQRGSFYAFS--YYYDRAVDTDmidyekgGILKVEDFERKAREVCDN--------LENFT-SGSPFLCMDLSYITALLK 388
Cdd:cd24112   306 --VKGKFVAFAgfYYTASALNLT-------GSFTLTTFNSSMWSFCSQswaqlkvmLPKFEeRYARSYCFSANYIYTLLV 376
                         410       420
                  ....*....|....*....|....*....
gi 1013384490 389 DGFGFADSTVLQLT--KKVNNIETGWALG 415
Cdd:cd24112   377 RGYKFDPETWPQISfqKEVGNSSIAWSLG 405
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
45-415 6.11e-42

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: 153.37  E-value: 6.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  45 ASTLYGIMFDAGSTGTRIHVYTF-VQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKT 123
Cdd:cd24113    21 PGIKYGIVFDAGSSHTSLFLYQWpADKENGTGIVSQVLSCDVEGPGISSYAQNPAKAGESLKPCLDEALAAIPAEQQKET 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 124 PVVLKATAGLRLLPEH---KAKALLFEVKEIFRKSPFLVpkGSVSIMDGSDEGILAWVTVNFLTGQL----------HGH 190
Cdd:cd24113   101 PVYLGATAGMRLLRLQnstQSDEILAEVSKTIGSYPFDF--QGARILTGMEEGAYGWITVNYLLETFikysfegkwiHPK 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 191 RQETVGTLDLGGASTQITFLPQ---FEKTLEqtprgylTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHT 267
Cdd:cd24113   179 GGNILGALDLGGASTQITFVPGgpiEDKNTE-------ANFRLYGYNYTVYTHSYLCYGKDQMLKRLLAALLQGRNLAAL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 268 FRSACLPRWLEAEWIFGGV--------KYQYGGNQ----EGEVGFEPCYAEVLRVVR------------GKLHQPEevQR 323
Cdd:cd24113   252 ISHPCYLKGYTTNLTLASIydspcvpdPPPYSLAQnitvEGTGNPAECLSAIRNLFNftacggsqtcafNGVYQPP--VN 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 324 GSFYAFS-YYYdravDTDMIDYEKGGILK-----VEDF-ERKAREVcdnLENFTSGSPF----LCMDLSYITALLKDGFG 392
Cdd:cd24113   330 GEFFAFSaFYY----TFDFLNLTSGQSLStvnstIWEFcSKPWTEL---EASYPKEKDKrlkdYCASGLYILTLLVDGYK 402
                         410       420
                  ....*....|....*....|....*
gi 1013384490 393 FADSTVLQLT--KKVNNIETGWALG 415
Cdd:cd24113   403 FDSETWNNIHfqKKAGNTDIGWTLG 427
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
49-420 8.18e-42

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: 150.96  E-value: 8.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTFvQKMPGQLPILEGEVFDS-VKPGLSAfvdqpkQGAETVQGLLEVAKDSIPRSHWKKTPVVL 127
Cdd:cd24038     3 CTAVIDAGSSGSRLHLYQY-DTDDSNPPIHEIELKNNkIKPGLAS------VNTTDVDAYLDPLFAKLPIAKTSNIPVYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 128 KATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGsVSIMDGSDEGILAWVTVNFLTGQLhGHRQETVGTLDLGGASTQI 207
Cdd:cd24038    76 YATAGMRLLPPSEQKKLYQELKDWLAQQSKFQLVE-AKTITGHMEGLYDWIAVNYLLDTL-KSSKKTVGVLDLGGASTQI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 208 TFLPQfektlEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARlatlgaletegtdgHTF--RSACLPrwleaewifgg 285
Cdd:cd24038   154 AFAVP-----NNASKDNTVEVKIGNKTINLYSHSYLGLGQDQAR--------------HQFlnNPDCFP----------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 286 VKYQYGGNQEGEVGFEPCYAEV--LRVVRGKLHQPEEVQRGS---FYAFSYYYDRAvdtDMIDYEKGGILKVEDFERKAR 360
Cdd:cd24038   204 KGYPLPSGKIGQGNFAACVEEIspLINSVHNVNSIILLALPPvkdWYAIGGFSYLA---SSKPFENNELTSLSLLQQGGN 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013384490 361 EVC----DNLENFTSGSPFL---CMDLSYITALLKDGFGFADSTVlQLTKKVNNIETGWALGATFHL 420
Cdd:cd24038   281 QFCkqswDELVQQYPDDPYLyayCLNSAYIYALLVDGYGFPPNQT-TIHNIIDGQNIDWTLGVALYF 346
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
49-420 8.10e-37

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: 139.11  E-value: 8.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYTF-VQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVL 127
Cdd:cd24111     4 YGIVLDAGSSHTSMFVYKWpADKENDTGIVSQHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTPLYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 128 KATAGLRLL----PEHKAKALLfEVKEIFRKSPFLVpKGSvSIMDGSDEGILAWVTVNFL---------TGQLHGHRQET 194
Cdd:cd24111    84 GATAGMRLLnltsPEASARVLE-AVTQTLTSYPFDF-RGA-RILSGQEEGVFGWVTANYLlenfikygwVGQWIRPRKGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 195 VGTLDLGGASTQITFLPQfeKTLEQtpRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLG-ALETEGTDGHTFrSACL 273
Cdd:cd24111   161 LGAMDLGGASTQITFETT--SPSED--PGNEVHLRLYGQHYRVYTHSFLCYGRDQVLLRLLAsALQIQGYGAHRF-HPCW 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 274 PRWLEAEWIFGGVkYQ---------YGGNQEGEVGFEPC--YAEVLRVVRG---------------KLHQPEEVqrGSFY 327
Cdd:cd24111   236 PKGYSTQVLLQEV-YQspctmgqrpRAFNGSAIVSLSGTsnATLCRDLVSRlfnfsscpfsqcsfnGVFQPPVT--GNFI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 328 AFS--YYYDRAVDTDMidyeKGGILKVEDFERKAREVC-DNLENFTSGSPFL-------CMDLSYITALLKDGFGFADST 397
Cdd:cd24111   313 AFSafYYTVDFLTTVM----GLPVGTPKQLEEATEIICnQTWTELQAKVPGQetrladyCAVAMFIHQLLSRGYHFDERS 388
                         410       420
                  ....*....|....*....|....*
gi 1013384490 398 VLQLT--KKVNNIETGWALGATFHL 420
Cdd:cd24111   389 FREISfqKKAGDTAVGWALGYMLNL 413
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
49-420 8.15e-36

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: 136.46  E-value: 8.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490  49 YGIMFDAGSTGTRIHVYtfvqKMPGQLPILEGEVFD----SVK-PGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKT 123
Cdd:cd24110     7 YGIVLDAGSSHTSLYIY----KWPAEKENDTGVVQQleecKVKgPGISSYSQKTTKAGASLAECMKKAKEVIPASQHHET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 124 PVVLKATAGLRLL---PEHKAKALLFEVKEIFRKSPFLVpKGSvSIMDGSDEGILAWVTVNFLTGQL-----------HG 189
Cdd:cd24110    83 PVYLGATAGMRLLrmeSEQAAEEVLASVERSLKSYPFDF-QGA-RIITGQEEGAYGWITINYLLGNFkqdsgwftqlsGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 190 HRQETVGTLDLGGASTQITFLPQfEKTLEqTPRGYLtSFEMFNSTYKLYTHSYLGFGlKAARLATLGALETEGTDGHTFR 269
Cdd:cd24110   161 KPTETFGALDLGGASTQITFVPL-NSTIE-SPENSL-QFRLYGTDYTVYTHSFLCYG-KDQALWQKLAQDIQSTSGGILK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 270 SACL----PRWLEAEWIFGG-----VKYQYGGNQ---EGEVGFEPCYAEVLRVVRGK-----------LHQPeEVQrGSF 326
Cdd:cd24110   237 DPCFhpgyKRVVNVSELYGTpctkrFEKKLPFNQfqvQGTGNYEQCHQSILKIFNNShcpysqcsfngVFLP-PLQ-GSF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 327 YAFSYYYdravdtDMIDYekggiLKVEDFERKAREVCDNLENFTSGS-------------PFL---CMDLSYITALLKDG 390
Cdd:cd24110   315 GAFSAFY------FVMDF-----LNLTANVSSLDKMKETIKNFCSKPweevkasypkvkeKYLseyCFSGTYILSLLEQG 383
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1013384490 391 FGF-ADS-TVLQLTKKVNNIETGWALGATFHL 420
Cdd:cd24110   384 YNFtSDNwNDIHFMGKIKDSDAGWTLGYMLNL 415
ASKHA_NBD_TgNTPase-like cd24037
nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) ...
124-227 9.62e-06

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: 47.93  E-value: 9.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013384490 124 PVVLKATAGLRLLPEHKAKALLFEVKE-IFRKSP------FLVPKGSVSIMdGSDEGILAWVTVNFLTGQL--------- 187
Cdd:cd24037   124 PVMLCSTAGVRDFHDWYRDALFVLLRHlINNPSPahgykfFTNPFWTRPIT-GAEEGLFAFITLNHLSRRLgedparcmi 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1013384490 188 -----HGHRQETVGTLDLGGASTQITF-------LPQFEKTLEQTPRGYLTS 227
Cdd:cd24037   203 deygvKQCRNDLAGVVEVGGASAQIVFplqegtvLPSSVRAVNLQRERLLPE 254
 
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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