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Conserved domains on  [gi|1171342959|ref|NP_001336891|]
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ectonucleoside triphosphate diphosphohydrolase 7 isoform 1 [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_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
84-533 0e+00

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: 821.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  84 LNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 163
Cdd:cd24045     1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPHELLDIKPLRDENGKPVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 164 KKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDA- 242
Cdd:cd24045    81 EKHKETPLYILATAGMRLLPESQQEAILEDLRTDIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFDHSEDDDPa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 243 ---EATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAkqeeAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGG 319
Cdd:cd24045   161 vvvVSDNKEAILRKRTVGILDMGGASTQIAFEVPKTVEFASP----VAKNLLAEFNLGCDAHDTEHVYRVYVTTFLGYGA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 320 NFARQRYEDLVLNETLNKNRLlgQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQ 399
Cdd:cd24045   237 NEARQRYEDSLVSSTKSTNRL--KQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGTGDFELCRQSLKPLLNKTNPCQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 400 ---ASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFsSHADEHRLK 476
Cdd:cd24045   315 kspCSLNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRMGGPYDYEKFTKAAKDYCATRWSLLEERFKKGLY-PKADEHRLK 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1171342959 477 YQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLR 533
Cdd:cd24045   394 TQCFKSAWMTSVLHDGFSFPKNYKNLKSAQLIYGKEVQWTLGALLYRTRFLPLRDIQ 450
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
84-533 0e+00

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: 821.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  84 LNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 163
Cdd:cd24045     1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPHELLDIKPLRDENGKPVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 164 KKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDA- 242
Cdd:cd24045    81 EKHKETPLYILATAGMRLLPESQQEAILEDLRTDIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFDHSEDDDPa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 243 ---EATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAkqeeAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGG 319
Cdd:cd24045   161 vvvVSDNKEAILRKRTVGILDMGGASTQIAFEVPKTVEFASP----VAKNLLAEFNLGCDAHDTEHVYRVYVTTFLGYGA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 320 NFARQRYEDLVLNETLNKNRLlgQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQ 399
Cdd:cd24045   237 NEARQRYEDSLVSSTKSTNRL--KQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGTGDFELCRQSLKPLLNKTNPCQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 400 ---ASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFsSHADEHRLK 476
Cdd:cd24045   315 kspCSLNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRMGGPYDYEKFTKAAKDYCATRWSLLEERFKKGLY-PKADEHRLK 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1171342959 477 YQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLR 533
Cdd:cd24045   394 TQCFKSAWMTSVLHDGFSFPKNYKNLKSAQLIYGKEVQWTLGALLYRTRFLPLRDIQ 450
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
79-529 1.21e-106

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 327.46  E-value: 1.21e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  79 TEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNphdLLDIKQMRDRnsqpvVKKIKPGISAMADTPEHASDYLRPLLSFAA 158
Cdd:pfam01150   3 ALPENVKYGIIIDAGSSGTRLHVYKWPDEKEG---LTPIVPLIEE-----FKKLEPGLSSFATKPDAAANYLTPLLEFAE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 159 AHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHED 238
Cdd:pfam01150  75 EHIPEEKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 239 ESdaeatqelaagrrrTVGILDMGGASLQIAYEvPTSTSVLPAKQEEAakillaefNLGCDVQHTEHVYRVYVTTFLGFG 318
Cdd:pfam01150 155 QS--------------TFGAIDLGGASTQIAFE-PSNESAINSTVEDI--------ELGLQFRLYDKDYTLYVHSFLGYG 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 319 GNFARQRYEDLVLNEtlnknrllgqktglSPDNPFLDPCLPVGLTDVVER---NSQVLHVRGRGDWVSCGAMLSPLL--- 392
Cdd:pfam01150 212 ANEALRKYLAKLIQN--------------LSNGILNDPCMPPGYNKTVEVstlEGKQFAIQGTGNWEQCRQSILELLnkn 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 393 ARSNTSQASLNGIYQSPIDfNNSEFYGFSEFFYCTEDVLRIGGRYHGP-TFAKAAQDYCGMAWSVLTQRFKNGLFSSHAD 471
Cdd:pfam01150 278 AHCPYEPCAFNGVHAPSIG-SLQKSFGASSYFYTVMDFFGLGGEYSSQeKFTDIARKFCSKNWNDIKAGFPKVLDKNISE 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1171342959 472 EHrlkyQCFKSAWMYQVLHEGFHFPyDYPNLRTAQLVYDREVQWTLGAILYKTRFLPL 529
Cdd:pfam01150 357 ET----YCFKGAYILSLLHDGFNFP-KTEEIQSVGKIAGKEAGWTLGAMLNLTSMIPL 409
 
Name Accession Description Interval E-value
ASKHA_NBD_NTPDase4-like cd24045
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 4 ...
84-533 0e+00

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: 821.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  84 LNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 163
Cdd:cd24045     1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPHELLDIKPLRDENGKPVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 164 KKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDA- 242
Cdd:cd24045    81 EKHKETPLYILATAGMRLLPESQQEAILEDLRTDIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFDHSEDDDPa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 243 ---EATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAkqeeAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGG 319
Cdd:cd24045   161 vvvVSDNKEAILRKRTVGILDMGGASTQIAFEVPKTVEFASP----VAKNLLAEFNLGCDAHDTEHVYRVYVTTFLGYGA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 320 NFARQRYEDLVLNETLNKNRLlgQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQ 399
Cdd:cd24045   237 NEARQRYEDSLVSSTKSTNRL--KQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGTGDFELCRQSLKPLLNKTNPCQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 400 ---ASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFsSHADEHRLK 476
Cdd:cd24045   315 kspCSLNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRMGGPYDYEKFTKAAKDYCATRWSLLEERFKKGLY-PKADEHRLK 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1171342959 477 YQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLR 533
Cdd:cd24045   394 TQCFKSAWMTSVLHDGFSFPKNYKNLKSAQLIYGKEVQWTLGALLYRTRFLPLRDIQ 450
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
79-529 1.21e-106

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 327.46  E-value: 1.21e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  79 TEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNphdLLDIKQMRDRnsqpvVKKIKPGISAMADTPEHASDYLRPLLSFAA 158
Cdd:pfam01150   3 ALPENVKYGIIIDAGSSGTRLHVYKWPDEKEG---LTPIVPLIEE-----FKKLEPGLSSFATKPDAAANYLTPLLEFAE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 159 AHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHED 238
Cdd:pfam01150  75 EHIPEEKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 239 ESdaeatqelaagrrrTVGILDMGGASLQIAYEvPTSTSVLPAKQEEAakillaefNLGCDVQHTEHVYRVYVTTFLGFG 318
Cdd:pfam01150 155 QS--------------TFGAIDLGGASTQIAFE-PSNESAINSTVEDI--------ELGLQFRLYDKDYTLYVHSFLGYG 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 319 GNFARQRYEDLVLNEtlnknrllgqktglSPDNPFLDPCLPVGLTDVVER---NSQVLHVRGRGDWVSCGAMLSPLL--- 392
Cdd:pfam01150 212 ANEALRKYLAKLIQN--------------LSNGILNDPCMPPGYNKTVEVstlEGKQFAIQGTGNWEQCRQSILELLnkn 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 393 ARSNTSQASLNGIYQSPIDfNNSEFYGFSEFFYCTEDVLRIGGRYHGP-TFAKAAQDYCGMAWSVLTQRFKNGLFSSHAD 471
Cdd:pfam01150 278 AHCPYEPCAFNGVHAPSIG-SLQKSFGASSYFYTVMDFFGLGGEYSSQeKFTDIARKFCSKNWNDIKAGFPKVLDKNISE 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1171342959 472 EHrlkyQCFKSAWMYQVLHEGFHFPyDYPNLRTAQLVYDREVQWTLGAILYKTRFLPL 529
Cdd:pfam01150 357 ET----YCFKGAYILSLLHDGFNFP-KTEEIQSVGKIAGKEAGWTLGAMLNLTSMIPL 409
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
85-522 3.02e-102

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: 314.68  E-value: 3.02e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  85 NYGLVVDCGSSGSRIFVYFW--PRHNGNPHDLLDIKQM-----RDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFA 157
Cdd:cd24039     2 KYGIVIDAGSSGSRVQIYSWkdPESATSKASLEELKSLphietGIGDGKDWTLKVEPGISSFADHPHVVGEHLKPLLDFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 158 AAHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLF--SQSQAEVISGKQEGVYAWIGINFVLGRFD 235
Cdd:cd24039    82 LNIIPPSVHSSTPIFLLATAGMRLLPQDQQNAILDAVCDYLRKNYPFLLpdCSEHVQVISGEEEGLYGWLAVNYLMGGFD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 236 HedesdaeATQELAAGRRRTVGILDMGGASLQIAYEVPTStsvlpAKQEEAAKILLAEFNLgcdVQHTEHVYRVYVTTFL 315
Cdd:cd24039   162 D-------APKHSIAHDHHTFGFLDMGGASTQIAFEPNAS-----AAKEHADDLKTVHLRT---LDGSQVEYPVFVTTWL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 316 GFGGNFARQRYEDLVLNE-TLNKNrllgQKTGLSPDNPFLDPCLPVGLtdvvernsqvlhvrgrgdwvscgamlspllar 394
Cdd:cd24039   227 GFGTNEARRRYVESLIEQaGSDTN----SKSNSSSELTLPDPCLPLGL-------------------------------- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 395 sntsqaslngiyqspidfNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFSSHADEHR 474
Cdd:cd24039   271 ------------------ENNHFVGVSEYWYTTQDVFGLGGAYDFVEFEKAAREFCSKPWESILHELEAGKAGNSVDENR 332
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1171342959 475 LKYQCFKSAWMYQVLHEGFHfpydypnlrTAQLVYDREVQWTLGAILY 522
Cdd:cd24039   333 LQMQCFKAAWIVNVLHEGFQ---------SVNKIDDTEVSWTLGKVLL 371
ASKHA_NBD_GDA1_CD39_NTPase cd24003
nucleotide-binding domain (NBD) of the GDA1/CD39 NTPase family; The GDA1/CD39 NTPase family ...
86-521 6.83e-98

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: 302.00  E-value: 6.83e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDikqmrdRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKK 165
Cdd:cd24003     1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIE------LVSSGKEKSGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 166 HKETPLYILCTAGMRLLPERKQLAILADLVKDLPlEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDaeat 245
Cdd:cd24003    75 RSSTPVYLLATAGMRLLPEEQQEAILDAVRTILR-NSGFGFDDGWVRVISGEEEGLYGWLSVNYLLGNLGSEPAKK---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 246 qelaagrrrTVGILDMGGASLQIAYEVPTSTsvlpakqeeaakilLAEFNLGCDVQHTEHVYRVYVTTFLGFGGNFARQR 325
Cdd:cd24003   150 ---------TVGVLDLGGASTQIAFEPPEDD--------------LSSLSNVYPLRLGGKTYDLYSHSFLGYGLNEARKR 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 326 YEDLVLNEtlnknrllgqktglSPDNPFLDPCLPVGLTDvvernsqvlhvrgrgdwvscgamlspllarsntsqaslngi 405
Cdd:cd24003   207 VLESLINN--------------SEGGNVTNPCLPKGYTG----------------------------------------- 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 406 yqspidfnnsEFYGFSEFFYCTEDVLRIGGRYHGP-TFAKAAQDYCGMAWSVLTQRFknglfsSHADEHRLKYQCFKSAW 484
Cdd:cd24003   232 ----------PFYAFSNFYYTAKFLGLVDSGTFTLeELEEAAREFCSLDWAELKAKY------PGVDDDFLPNLCFDAAY 295
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1171342959 485 MYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAIL 521
Cdd:cd24003   296 IYSLLEDGFGLDDDSPIIKFVDKINGVELSWTLGAAL 332
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
86-524 5.14e-64

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: 215.99  E-value: 5.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNgnphdlldikqmrdRNSQPVVKKI------KPGISAMADTPEHASDYLRPLLSFAAA 159
Cdd:cd24044     1 YGIVIDAGSSHTSLFVYKWPADK--------------ENGTGVVQQVstcrvkGGGISSYENNPSQAGESLEPCLDQAKK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 160 HVPVKKHKETPLYILCTAGMRLL----PERKQLAILA--DLVKDLPLEFDFlfsqSQAEVISGKQEGVYAWIGINFVLGR 233
Cdd:cd24044    67 KVPEDRRHSTPLYLGATAGMRLLnltnPSAADAILESvrDALKSSKFGFDF----RNARILSGEDEGLYGWITVNYLLGN 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 234 FDHEDESDAEATQELaagrrrTVGILDMGGASLQIAYEVptSTSVLPAKQEeaakillAEFNL-GcdvqhteHVYRVYVT 312
Cdd:cd24044   143 LGKYSISSIPRSRPE------TVGALDLGGASTQITFEP--AEPSLPADYT-------RKLRLyG-------KDYNVYTH 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 313 TFLGFGGNFARQRYEDLVLNETLNKNRL------LGQKTGLSPDNPFLDPC-LPVGLTDVVERNSQVlHVRGRGDWVSCG 385
Cdd:cd24044   201 SYLCYGKDEAERRYLASLVQESNYSSTVenpcapKGYSTNVTLAEIFSSPCtSKPLSPSGLNNNTNF-TFNGTSNPDQCR 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 386 AMLSPLLARSNT---SQASLNGIYQSPidfNNSEFYGFSEFFYcTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLtqrfk 462
Cdd:cd24044   280 ELVRKLFNFTSCcssGCCSFNGVFQPP---LNGNFYAFSGFYY-TADFLNLTSNGSLDEFREAVDDFCNKPWDEV----- 350
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1171342959 463 ngLFSSHADEHRLKYQCFKSAWMYQVLHEGFHFPY-DYPNLRTAQLVYDREVQWTLGAILYKT 524
Cdd:cd24044   351 --SELPPKGAKFLANYCFDANYILTLLTDGYGFTEeTWRNIHFVKKVNGTEVGWSLGYMLNAT 411
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
85-523 1.13e-54

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: 189.10  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  85 NYGLVVDCGSSGSRIFVYFWprHNGNPHDLLDIKQMRDrnsqpvvKKIKPGISAMadTPEHASDYLRPLLSfaaaHVPVK 164
Cdd:cd24038     2 SCTAVIDAGSSGSRLHLYQY--DTDDSNPPIHEIELKN-------NKIKPGLASV--NTTDVDAYLDPLFA----KLPIA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 165 KHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQsqAEVISGKQEGVYAWIGINFVLGRFdhedesdaea 244
Cdd:cd24038    67 KTSNIPVYFYATAGMRLLPPSEQKKLYQELKDWLAQQSKFQLVE--AKTITGHMEGLYDWIAVNYLLDTL---------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 245 tqelaAGRRRTVGILDMGGASLQIAYEVPTSTSvlpakqeeaaKILLAEFNLGcdvqhtEHVYRVYVTTFLGFGGNFARQ 324
Cdd:cd24038   135 -----KSSKKTVGVLDLGGASTQIAFAVPNNAS----------KDNTVEVKIG------NKTINLYSHSYLGLGQDQARH 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 325 RYEDlvlnetlnknrllgqktglSPDnpfldpCLPVGLTDVverNSQvlhvRGRGDWVSCGAMLSPLLarsnTSQASLNG 404
Cdd:cd24038   194 QFLN-------------------NPD------CFPKGYPLP---SGK----IGQGNFAACVEEISPLI----NSVHNVNS 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 405 IYQSPIDFNNsEFYGFSEFFY-CTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNglfsshaDEHRLKYqCFKSA 483
Cdd:cd24038   238 IILLALPPVK-DWYAIGGFSYlASSKPFENNELTSLSLLQQGGNQFCKQSWDELVQQYPD-------DPYLYAY-CLNSA 308
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1171342959 484 WMYQVLHEGFHFPYDypNLRTAQLVYDREVQWTLGAILYK 523
Cdd:cd24038   309 YIYALLVDGYGFPPN--QTTIHNIIDGQNIDWTLGVALYF 346
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
86-521 6.06e-54

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: 189.08  E-value: 6.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYfwpRHN--GNPHDLLDIKqmrdrnsqpVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 163
Cdd:cd24040     1 YALMIDAGSTGSRIHVY---RFNncQPPIPKLEDE---------VFEMTKPGLSSYADDPKGAAASLDPLLQVALQAVPK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 164 KKHKETPLYILCTAGMRLLPERKQLAILaDLVKDLpLE---FDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDhedes 240
Cdd:cd24040    69 ELHSCTPIAVKATAGLRLLGEDKSKEIL-DAVRHR-LEkeyPFVSVELDGVSIMDGKDEGVYAWITVNYLLGNIG----- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 241 daeatqelAAGRRRTVGILDMGGASLQIAYEvPTSTSVLPAKQEEaakiLLAEFNLGcDVQHTehvyrVYVTTFLGFGGN 320
Cdd:cd24040   142 --------GNEKLPTAAVLDLGGGSTQIVFE-PDFPSDEEDPEGD----HKYELTFG-GKDYV-----LYQHSYLGYGLM 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 321 FARQRYEDLVLNetlnkNRLLGQKTGLSPDNPFLD-PCLPVGLTDVV------ERNSQVLHVRGRGDWVSCGAmLSPLLA 393
Cdd:cd24040   203 EARKKIHKLVAE-----NASTGGSEGEATEGGLIAnPCLPPGYTKTVdlvqpeKSKKNVMVGGGKGSFEACRR-LVEKVL 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 394 RSNTSQASL----NGIYQSPI--DFNNSEFYGFSeFFYcteDVLRIGGrYHGPTF-----AKAAQDYC-GMA-WSVLTqr 460
Cdd:cd24040   277 NKDAECESKpcsfNGVHQPSLaeTFKDGPIYAFS-YFY---DRLNPLG-MEPSSFtlgelQKLAEQVCkGETsWDDFF-- 349
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1171342959 461 fknGLFSSHADEHRLKYQCFKSAWMYQVLHEGFHFPYDYPnLRTAQLVYDREVQWTLGAIL 521
Cdd:cd24040   350 ---GIDVLLDELKDNPEWCLDLTFMLSLLRTGYELPLDRE-LKIAKKIDGFELGWCLGASL 406
ASKHA_NBD_AtAPY3-like cd24042
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrases 3-6 (AtAPY3-6) and similar ...
86-521 7.99e-53

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: 185.73  E-value: 7.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNGNP---HDLLDIKQMrdrnsqpvvkKIKPGISAMADTPEHASDYLRPLLSFAAAHVP 162
Cdd:cd24042     1 YSVIIDAGSSGTRLHVFGYAAESGKPvfpFGEKDYASL----------KTTPGLSSFADNPSGASASLTELLEFAKERVP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 163 VKKHKETPLYILCTAGMRLLPERKQLAILaDLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGrfdhedesda 242
Cdd:cd24042    71 KGKRKETDIRLMATAGLRLLEVPVQEQIL-EVCRRVLRSSGFMFRDEWASVISGTDEGIYAWVAANYALG---------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 243 eatqELAAGRRRTVGILDMGGASLQIAYeVPtstSVLPAKqeeaakillaEFNLgcDVQHTEHVYRVYVTTFLGFGGNFA 322
Cdd:cd24042   140 ----SLGGDPLETTGIVELGGASAQVTF-VP---SEAVPP----------EFSR--TLVYGGVSYKLYSHSFLDFGQEAA 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 323 RQRYEDLVLNETLNKNRllgqktglspDNPFLDPCLPVGLtdVVERNSQ-------------VLHVRGRGDWVSCGAMLS 389
Cdd:cd24042   200 WDKLLESLLNGAAKSTR----------GGVVVDPCTPKGY--IPDTNSQkgeagaladksvaAGSLQAAGNFTECRSAAL 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 390 PLLARSNT----SQASLNGIYQSPID---FNNSEFYGFSEFFyctedvlRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFK 462
Cdd:cd24042   268 ALLQEGKDnclyKHCSIGSTFTPELRgkfLATENFFYTSEFF-------GLGETTWLSEMILAGERFCGEDWSKLKKKHP 340
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1171342959 463 nglfsSHADEHRLKYqCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAIL 521
Cdd:cd24042   341 -----GWEEEDLLKY-CFSAAYIVAMLHDGLGIALDDERIRYANKVGEIPLDWALGAFI 393
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
84-528 2.75e-49

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: 176.86  E-value: 2.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  84 LNYGLVVDCGSSGSRIFVYFWP--RHNG----NPHDLLDIKqmrdrnsqpvvkkiKPGISAMADTPEHASDYLRPLLSFA 157
Cdd:cd24111     2 LKYGIVLDAGSSHTSMFVYKWPadKENDtgivSQHSSCDVQ--------------GGGISSYANDPSKAGQSLVRCLEQA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 158 AAHVPVKKHKETPLYILCTAGMRLL------PERKQLAILADLVKDLPleFDFlfsqSQAEVISGKQEGVYAWIGINFVL 231
Cdd:cd24111    68 LRDVPRDRHASTPLYLGATAGMRLLnltspeASARVLEAVTQTLTSYP--FDF----RGARILSGQEEGVFGWVTANYLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 232 ---------GRFDHEdesdaeatqelaagRRRTVGILDMGGASLQIAYEvpTSTSVLPAKQEEAAKILlaefnlgcdvqh 302
Cdd:cd24111   142 enfikygwvGQWIRP--------------RKGTLGAMDLGGASTQITFE--TTSPSEDPGNEVHLRLY------------ 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 303 tEHVYRVYVTTFLGFGgnfarqryEDLVLNETLNKnRLLGQKTGLSPDNpfldPCLPVGLTDVV-------------ER- 368
Cdd:cd24111   194 -GQHYRVYTHSFLCYG--------RDQVLLRLLAS-ALQIQGYGAHRFH----PCWPKGYSTQVllqevyqspctmgQRp 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 369 ----NSQVLHVRGRGDWVSCGAMLSPL--LARSNTSQASLNGIYQSPIDFNnseFYGFSEFFYcTEDVLR--IGGRYHGP 440
Cdd:cd24111   260 rafnGSAIVSLSGTSNATLCRDLVSRLfnFSSCPFSQCSFNGVFQPPVTGN---FIAFSAFYY-TVDFLTtvMGLPVGTP 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 441 T-FAKAAQDYCGMAWSVLTQRfknglfsSHADEHRLKYQCFKSAWMYQVLHEGFHFPYD-YPNLRTAQLVYDREVQWTLG 518
Cdd:cd24111   336 KqLEEATEIICNQTWTELQAK-------VPGQETRLADYCAVAMFIHQLLSRGYHFDERsFREISFQKKAGDTAVGWALG 408
                         490
                  ....*....|
gi 1171342959 519 AILYKTRFLP 528
Cdd:cd24111   409 YMLNLTNLIP 418
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
83-528 4.00e-46

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: 168.05  E-value: 4.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  83 NLNYGLVVDCGSSGSRIFVYFWPRHNGNphDLLDIKQMRDRNsqpvVKKikPGISAMADTPEHASDYLRPLLSFAAAHVP 162
Cdd:cd24110     4 NVKYGIVLDAGSSHTSLYIYKWPAEKEN--DTGVVQQLEECK----VKG--PGISSYSQKTTKAGASLAECMKKAKEVIP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 163 VKKHKETPLYILCTAGMRLLP-ERKQLA--ILADLVKDLPLefdFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDE 239
Cdd:cd24110    76 ASQHHETPVYLGATAGMRLLRmESEQAAeeVLASVERSLKS---YPFDFQGARIITGQEEGAYGWITINYLLGNFKQDSG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 240 SDAEATQELAAGrrrTVGILDMGGASLQIAYeVPTSTSVlpakqeEAAKILLaEFNL-GCDvqhtehvYRVYVTTFLGFG 318
Cdd:cd24110   153 WFTQLSGGKPTE---TFGALDLGGASTQITF-VPLNSTI------ESPENSL-QFRLyGTD-------YTVYTHSFLCYG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 319 GNFARQryedlvlnetlnknRLLGQKTGLSPDNPFLDPCLPVGLTDVVERNS----------------QVLHVRGRGDWV 382
Cdd:cd24110   215 KDQALW--------------QKLAQDIQSTSGGILKDPCFHPGYKRVVNVSElygtpctkrfekklpfNQFQVQGTGNYE 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 383 SCGAMLSPLLARSNT--SQASLNGIYQSPIDfnnSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQR 460
Cdd:cd24110   281 QCHQSILKIFNNSHCpySQCSFNGVFLPPLQ---GSFGAFSAFYFVMDFLNLTANVSSLDKMKETIKNFCSKPWEEVKAS 357
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1171342959 461 FKNglfsshADEHRLKYQCFKSAWMYQVLHEGFHFPYD-YPNLRTAQLVYDREVQWTLGAILYKTRFLP 528
Cdd:cd24110   358 YPK------VKEKYLSEYCFSGTYILSLLEQGYNFTSDnWNDIHFMGKIKDSDAGWTLGYMLNLTNMIP 420
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
86-521 5.15e-46

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: 167.64  E-value: 5.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNGNphdlldikqmrdrNSQPVVKKIK-----PGISAMADTPEHASDYLRPLLSFAAAH 160
Cdd:cd24112     1 YGIVLDAGSSRTTVYVYQWPAEKEN-------------NTGVVSQTYKcnvkgPGISSYAHNPQKAARALEECMNKVKEI 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 161 VPVKKHKETPLYILCTAGMRLL------PERKQLAILADLVKDLPleFDFlfsqSQAEVISGKQEGVYAWIGINFVLGRF 234
Cdd:cd24112    68 IPSHLHNSTPVYLGATAGMRLLklqnetAANEVLSSIENYFKTLP--FDF----RGAHIITGQEEGVYGWITANYLMGNF 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 235 DHEDESDAEATQElaagRRRTVGILDMGGASLQIAYevptstsvLPAKQEEaakillaEFNLGCDVQHTEHVYRVYVTTF 314
Cdd:cd24112   142 LEKNLWNAWVHPH----GVETVGALDLGGASTQIAF--------IPEDSLE-------NLNDTVKVSLYGYKYNVYTHSF 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 315 LGFGGNFARQRYEDLVLNETLNKnrllgqktglspdNPFLDPCLPVGLTDVVERN------------------SQVLHVR 376
Cdd:cd24112   203 QCYGKDEAEKRFLANLAQASESK-------------SPVDNPCYPRGYNTSFSMKhifgslctasqrpanydpDDSITFT 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 377 GRGDWVSCGAMLSPLL---ARSNTSQASLNGIYQSPIdfnNSEFYGFSEFFYcTEDVLRIGGRYHGPTFAKAAQDYCGMA 453
Cdd:cd24112   270 GTGDPALCKEKVSLLFdfkSCQGKENCSFDGIYQPKV---KGKFVAFAGFYY-TASALNLTGSFTLTTFNSSMWSFCSQS 345
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1171342959 454 WSVLTQRFKNglfsshADEHRLKYQCFKSAWMYQVLHEGFHF-PYDYPNLRTAQLVYDREVQWTLGAIL 521
Cdd:cd24112   346 WAQLKVMLPK------FEERYARSYCFSANYIYTLLVRGYKFdPETWPQISFQKEVGNSSIAWSLGYML 408
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
86-522 1.20e-45

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: 165.76  E-value: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDikqmrdrnsQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKK 165
Cdd:cd24114     3 YGIMFDAGSTGTRIHIYTFVQKSPAELPELD---------GEIFESVKPGLSAYADQPEQGAETVRGLLDVAKKTIPSTQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 166 HKETPLYILCTAGMRLLPERKQLAILADlVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRfdhedesdaeat 245
Cdd:cd24114    74 WKKTPVVLKATAGLRLLPEEKAQALLSE-VKEIFEESPFLVPEGSVSIMNGTYEGILAWVTVNFLTGQ------------ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 246 qeLAAGRRRTVGILDMGGASLQIAYeVPTSTSVLpakqEEAAKILLAEFNLgcdvqhTEHVYRVYVTTFLGFGGNFARqr 325
Cdd:cd24114   141 --LYGQNQRTVGILDLGGASTQITF-LPRFEKTL----KQAPEDYLTSFEM------FNSTYKLYTHSYLGFGLKAAR-- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 326 yedLVLNETLNKNRLLGQKtglspdnpFLDPCLP---------VGLTDVVERNSQvlhvrGRGDWVSCGAMLSPLlarsn 396
Cdd:cd24114   206 ---LATLGALGTEDQEKQV--------FRSSCLPkglkaewkfGGVTYKYGGNKE-----GETGFKSCYSEVLKV----- 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 397 tsqasLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRI----GGRYHGPTFAKAAQDYCgmawSVLTQrfknglFSSHAde 472
Cdd:cd24114   265 -----VKGKLHQPEEMQHSSFYAFSYYYDRAVDTGLIdyeqGGVLEVKDFEKKAKEVC----ENLER------YSSGS-- 327
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1171342959 473 hrlKYQCFKSAWMYQVLHEGFHFpYDYPNLRTAQLVYDREVQWTLGAILY 522
Cdd:cd24114   328 ---PFLCMDLTYITALLKEGFGF-EDNTVLQLTKKVNNVETSWTLGAIFH 373
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
86-519 8.44e-45

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


Pssm-ID: 466896  Cd Length: 372  Bit Score: 163.11  E-value: 8.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVY-FWPRHNGNPHDLLDikqmrdrnsqPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVK 164
Cdd:cd24046     1 YAIVFDAGSTGSRVHVFkFSHSPSGGPLKLLD----------ELFEEVKPGLSSYADDPKEAADSLKPLLEKAKTRIPKE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 165 KHKETPLYILCTAGMRLLPERKQLAILA---DLVKDLPlefdFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHedesd 241
Cdd:cd24046    71 KWSSTPLALKATAGLRLLPEEKANAILDevrKLFKKSP----FLVGEDSVSIMDGTDEGIFSWFTVNFLLGRLGG----- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 242 aeatqelaaGRRRTVGILDMGGASLQIAYeVPTSTSVLPAkqeeaakillAEFNLGCDVQHTEHVYRVYVTTFLGFGGNF 321
Cdd:cd24046   142 ---------SASNTVAALDLGGGSTQITF-APSDKETLSA----------SPKGYLHKVSIFGKKIKLYTHSYLGLGLMA 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 322 ARqryedlvlnetlnKNRLLGQKTGLSPD-NPFLDPCLPVGLTDVVERNSQVLHVRGRG----DWVSCGAMLSPLLARSN 396
Cdd:cd24046   202 AR-------------LAILQGSSTNSNSGtTELKSPCFPPNFKGEWWFGGKKYTSSIGGsseySFDACYKLAKKVVDSSV 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 397 TSQaslngiyqsPIDFNNSEFYGFSEFFYCTEDVlRIGGRYHGPT-----FAKAAQDYCGMawsvltqrfknglfsshaD 471
Cdd:cd24046   269 IHK---------PEELKSREIYAFSYFYDRAVDA-GLIDEQEGGTvtvgdFKKAAKKACSN------------------P 320
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1171342959 472 EHRLKYQCFKSAWMYQVLHEGFHFPYDYPnLRTAQLVYDREVQWTLGA 519
Cdd:cd24046   321 NPEQPFLCLDLTYIYALLHDGYGLPDDKK-LTLVKKINGVEISWALGA 367
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
82-524 7.52e-44

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: 162.23  E-value: 7.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  82 PNLNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSqpvvkkikPGISAMADTPEHASDYLRPLLSFAAAHV 161
Cdd:cd24113    21 PGIKYGIVFDAGSSHTSLFLYQWPADKENGTGIVSQVLSCDVEG--------PGISSYAQNPAKAGESLKPCLDEALAAI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 162 PVKKHKETPLYILCTAGMRLLPERKQ------LAILADLVKDLPLEFdflfsqSQAEVISGKQEGVYAWIGINFVLGRF- 234
Cdd:cd24113    93 PAEQQKETPVYLGATAGMRLLRLQNStqsdeiLAEVSKTIGSYPFDF------QGARILTGMEEGAYGWITVNYLLETFi 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 235 DHEDESDAEATQElaagrRRTVGILDMGGASLQIAYeVPtSTSVLPAKQEeaAKILLAEFNlgcdvqhtehvYRVYVTTF 314
Cdd:cd24113   167 KYSFEGKWIHPKG-----GNILGALDLGGASTQITF-VP-GGPIEDKNTE--ANFRLYGYN-----------YTVYTHSY 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 315 LGFGGNFARQRyedlvLNETLNKNR-----------LLGQKTGLSPDNPFLDPCLPvglTDVVERNSQVLHVRGRGDWVS 383
Cdd:cd24113   227 LCYGKDQMLKR-----LLAALLQGRnlaalishpcyLKGYTTNLTLASIYDSPCVP---DPPPYSLAQNITVEGTGNPAE 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 384 CGAMLSPLL---ARSNTSQASLNGIYQSPIdfnNSEFYGFSEFFYcTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQR 460
Cdd:cd24113   299 CLSAIRNLFnftACGGSQTCAFNGVYQPPV---NGEFFAFSAFYY-TFDFLNLTSGQSLSTVNSTIWEFCSKPWTELEAS 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1171342959 461 FKNglfsshADEHRLKYQCFKSAWMYQVLHEGFHFPYD-YPNLRTAQLVYDREVQWTLGAILYKT 524
Cdd:cd24113   375 YPK------EKDKRLKDYCASGLYILTLLVDGYKFDSEtWNNIHFQKKAGNTDIGWTLGYMLNLT 433
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
86-522 2.00e-42

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: 158.00  E-value: 2.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNGNPH--DLLDI--KQMRDRNSQPVVKKIK-----PGISAMADTPEHASDYLRPLLSF 156
Cdd:cd24043     1 YAIVMDCGSTGTRVYVYSWARNPSKDSlpVMVDPptVASAALVKKPKKRAYKrvetePGLDKLADNETGLGAALGPLLDW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 157 AAAHVPVKKHKETPLYILCTAGMRLLPERKQlAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDH 236
Cdd:cd24043    81 AGKQIPRSQHPRTPVFLFATAGLRRLPPDDS-AWLLDKAWGVLEASPFRFERSWVRIISGTEEAYYGWIALNYLTGRLGQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 237 EDESDAeatqelaagrrrTVGILDMGGASLQIAYEvptsTSVLPAKqeeaakillaEFNLGCDVQHTEHvyRVYVTTFLG 316
Cdd:cd24043   160 GPGKGA------------TVGSLDLGGSSLEVTFE----PEAVPRG----------EYGVNLSVGSTEH--HLYAHSHAG 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 317 FGGNFARQRYEDLVLNETLNKNRLLGQKTGLSPDNPFLDP-----------CLPVGLTDVVERNSQV-LHVRGRGDWVSC 384
Cdd:cd24043   212 YGLNDAFDKSVALLLKDQNATPPVRLREGTLEVEHPCLHSgynrpykcshhAGAPPVRGLKAGPGGAsVQLVGAPNWGAC 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 385 GAMLSPLLARSNTSQASLN----GIYQSPIdfnNSEFYGFSEFFYC-----------TEDVLRiggryhgptfakAAQDY 449
Cdd:cd24043   292 QALAGRVVNTTASAECEFPpcalGKHQPRP---QGQFYALTGFFVVykffglsatasLDDLLA------------KGQEF 356
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1171342959 450 CGMAWSVLTqrfknglfSSHADEHRLKYQCFKSAWMYQVLHEGFHfpydypnLRTAQL-VYDREVQWTLGAILY 522
Cdd:cd24043   357 CGKPWQVAR--------ASVPPQPFIERYCFRAPYVVSLLREGLH-------LRDEQIqIGSGDVGWTLGAALA 415
ASKHA_NBD_AtAPY1-like cd24041
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 1 (AtAPY1), apyrase 2 (AtAPY2), ...
85-519 4.69e-41

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


Pssm-ID: 466891  Cd Length: 399  Bit Score: 153.63  E-value: 4.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  85 NYGLVVDCGSSGSRIFVYFWPRHNgnphDLLDIKqmrdrNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVK 164
Cdd:cd24041     1 RYAVVFDAGSTGSRVHVFKFDQNL----DLLHLG-----LDLELFEQIKPGLSSYADDPEQAAKSLRPLLDKALAVVPEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 165 KHKETPLYILCTAGMRLLPERKQLAILADlVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDEsdaea 244
Cdd:cd24041    72 LQSKTPVRLGATAGLRLLPGDASENILQE-VRDLLRNYSFKVQPDAVSIIDGTDEGSYQWVTVNYLLGNLGKPFT----- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 245 tqelaagrrRTVGILDMGGASLQIAYEVPTSTSVLPAKQEEAAKILLAEFNLGcdvqhtEHVYRVYVTTFLGFGGNFARQ 324
Cdd:cd24041   146 ---------KTVGVVDLGGGSVQMAYAVSDETAKNAPKPTDGEDGYIRKLVLK------GKTYDLYVHSYLGYGLMAARA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 325 ryedlvlnETLNknrlLGQKTGLSpdnpfldPCLPVGLTDVVERNSQVLHVRGR---GDWVSCGAMLSPLL---ARSNTS 398
Cdd:cd24041   211 --------EILK----LTEGTSAS-------PCIPAGFDGTYTYGGEEYKAVAGesgADFDKCKKLALKALkldEPCGYE 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 399 QASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIG-----GRYHGPTFAKAAQDYCGMAWSVLTQRFKnglfssHADEH 473
Cdd:cd24041   272 QCTFGGVWNGGGGGGQKKLFVASYFFDRASEVGIIDdqasqAVVRPSDFEKAAKKACKLNVEEIKSKYP------LVEEK 345
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1171342959 474 RLKYQCFKSAWMYQVLHEGFhfpyDYPNLRTAQLV-------YDREVQWTLGA 519
Cdd:cd24041   346 DAPFLCMDLTYQYTLLVDGF----GLDPDQEITLVkqieyqgALVEAAWPLGA 394
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
86-522 1.74e-30

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: 123.00  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959  86 YGLVVDCGSSGSRIFVYFWPRHNGNPHDLldikqmrdrnSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKK 165
Cdd:cd24115     3 YGIMFDAGSTGTRIHIFKFTRPPNEAPKL----------THETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 166 HKETPLYILCTAGMRLLPERKQlAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGrfdhedesdaeat 245
Cdd:cd24115    73 WKATPLVLKATAGLRLLPGEKA-QKLLDKVKEVFKASPFLVGDDSVSIMDGTDEGISAWITVNFLTG------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 246 qELAAGRRRTVGILDMGGASLQIAYeVPTSTSVLPAKQEEaakiLLAEFNLGcdvqhtEHVYRVYVTTFLGFGGNFARQr 325
Cdd:cd24115   139 -SLHGTGRSSVGMLDLGGGSTQITF-SPHSEGTLQTSPID----YITSFQMF------NRTYTLYSHSYLGLGLMSARL- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 326 yedlvlnetlnknRLLGQKTGLSPDNP--FLDPCLPVGLTDVVERNSQVLHVRGRGD----WVSCGAMLSPLLARSntsq 399
Cdd:cd24115   206 -------------AILGGVEGKPLKEGqeLVSPCLAPEYKGEWEHAEITYKIKGQKAeeplYESCYARVEKMLYKK---- 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 400 aslngiYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPT----FAKAAQDYCgmawsvltQRFKNGLFSShadehrl 475
Cdd:cd24115   269 ------VHKAEEVKNLDFYAFSYYYDRAVDVGLIDEEKGGSLkvgdFEIAAKKVC--------KTMESQPGEK------- 327
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1171342959 476 KYQCFKSAWMYQVLHEgFHFPYDyPNLRTAQLVYDREVQWTLGAILY 522
Cdd:cd24115   328 PFLCMDLTYISVLLQE-LGFPKD-KELKLARKIDNVETSWALGATFH 372
ASKHA_NBD_TgNTPase-like cd24037
nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) ...
170-281 5.81e-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: 46.01  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1171342959 170 PLYILCTAGMRLLPE--RKQLAILADLVKDLPL---EFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDhEDESDAEA 244
Cdd:cd24037   124 PVMLCSTAGVRDFHDwyRDALFVLLRHLINNPSpahGYKFFTNPFWTRPITGAEEGLFAFITLNHLSRRLG-EDPARCMI 202
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1171342959 245 TQELAAGRRRT-VGILDMGGASLQIAYEVPTSTsVLPA 281
Cdd:cd24037   203 DEYGVKQCRNDlAGVVEVGGASAQIVFPLQEGT-VLPS 239
 
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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