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Conserved domains on  [gi|9966821|ref|NP_065087|]
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ectonucleoside triphosphate diphosphohydrolase 7 isoform 2 [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 ...
82-531 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 9966821   82 LNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 161
Cdd:cd24045   1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPHELLDIKPLRDENGKPVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  162 KKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDA- 240
Cdd:cd24045  81 EKHKETPLYILATAGMRLLPESQQEAILEDLRTDIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFDHSEDDDPa 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  241 ---EATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAkqeeAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGG 317
Cdd:cd24045 161 vvvVSDNKEAILRKRTVGILDMGGASTQIAFEVPKTVEFASP----VAKNLLAEFNLGCDAHDTEHVYRVYVTTFLGYGA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  318 NFARQRYEDLVLNETLNKNRLlgQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQ 397
Cdd:cd24045 237 NEARQRYEDSLVSSTKSTNRL--KQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGTGDFELCRQSLKPLLNKTNPCQ 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  398 ---ASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFsSHADEHRLK 474
Cdd:cd24045 315 kspCSLNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRMGGPYDYEKFTKAAKDYCATRWSLLEERFKKGLY-PKADEHRLK 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966821  475 YQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLR 531
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 ...
82-531 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 9966821   82 LNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 161
Cdd:cd24045   1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPHELLDIKPLRDENGKPVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  162 KKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDA- 240
Cdd:cd24045  81 EKHKETPLYILATAGMRLLPESQQEAILEDLRTDIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFDHSEDDDPa 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  241 ---EATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAkqeeAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGG 317
Cdd:cd24045 161 vvvVSDNKEAILRKRTVGILDMGGASTQIAFEVPKTVEFASP----VAKNLLAEFNLGCDAHDTEHVYRVYVTTFLGYGA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  318 NFARQRYEDLVLNETLNKNRLlgQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQ 397
Cdd:cd24045 237 NEARQRYEDSLVSSTKSTNRL--KQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGTGDFELCRQSLKPLLNKTNPCQ 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  398 ---ASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFsSHADEHRLK 474
Cdd:cd24045 315 kspCSLNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRMGGPYDYEKFTKAAKDYCATRWSLLEERFKKGLY-PKADEHRLK 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966821  475 YQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLR 531
Cdd:cd24045 394 TQCFKSAWMTSVLHDGFSFPKNYKNLKSAQLIYGKEVQWTLGALLYRTRFLPLRDIQ 450
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
77-527 1.14e-106

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 327.46  E-value: 1.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821     77 TEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNphdLLDIKQMRDRnsqpvVKKIKPGISAMADTPEHASDYLRPLLSFAA 156
Cdd:pfam01150   3 ALPENVKYGIIIDAGSSGTRLHVYKWPDEKEG---LTPIVPLIEE-----FKKLEPGLSSFATKPDAAANYLTPLLEFAE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    157 AHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHED 236
Cdd:pfam01150  75 EHIPEEKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    237 ESdaeatqelaagrrrTVGILDMGGASLQIAYEvPTSTSVLPAKQEEAakillaefNLGCDVQHTEHVYRVYVTTFLGFG 316
Cdd:pfam01150 155 QS--------------TFGAIDLGGASTQIAFE-PSNESAINSTVEDI--------ELGLQFRLYDKDYTLYVHSFLGYG 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    317 GNFARQRYEDLVLNEtlnknrllgqktglSPDNPFLDPCLPVGLTDVVER---NSQVLHVRGRGDWVSCGAMLSPLL--- 390
Cdd:pfam01150 212 ANEALRKYLAKLIQN--------------LSNGILNDPCMPPGYNKTVEVstlEGKQFAIQGTGNWEQCRQSILELLnkn 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    391 ARSNTSQASLNGIYQSPIDfNNSEFYGFSEFFYCTEDVLRIGGRYHGP-TFAKAAQDYCGMAWSVLTQRFKNGLFSSHAD 469
Cdd:pfam01150 278 AHCPYEPCAFNGVHAPSIG-SLQKSFGASSYFYTVMDFFGLGGEYSSQeKFTDIARKFCSKNWNDIKAGFPKVLDKNISE 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966821    470 EHrlkyQCFKSAWMYQVLHEGFHFPyDYPNLRTAQLVYDREVQWTLGAILYKTRFLPL 527
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 ...
82-531 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 9966821   82 LNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 161
Cdd:cd24045   1 LHYGVVIDCGSSGSRVFVYTWPRHSGNPHELLDIKPLRDENGKPVVKKIKPGLSSFADKPEKASDYLRPLLDFAAEHIPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  162 KKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDA- 240
Cdd:cd24045  81 EKHKETPLYILATAGMRLLPESQQEAILEDLRTDIPKHFNFLFSDSHAEVISGKQEGVYAWIAINYVLGRFDHSEDDDPa 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  241 ---EATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAkqeeAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGG 317
Cdd:cd24045 161 vvvVSDNKEAILRKRTVGILDMGGASTQIAFEVPKTVEFASP----VAKNLLAEFNLGCDAHDTEHVYRVYVTTFLGYGA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  318 NFARQRYEDLVLNETLNKNRLlgQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQ 397
Cdd:cd24045 237 NEARQRYEDSLVSSTKSTNRL--KQQGLTPDTPILDPCLPLDLSDTITQNGGTIHLRGTGDFELCRQSLKPLLNKTNPCQ 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  398 ---ASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFsSHADEHRLK 474
Cdd:cd24045 315 kspCSLNGVYQPPIDFSNSEFYGFSEFWYTTEDVLRMGGPYDYEKFTKAAKDYCATRWSLLEERFKKGLY-PKADEHRLK 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966821  475 YQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLR 531
Cdd:cd24045 394 TQCFKSAWMTSVLHDGFSFPKNYKNLKSAQLIYGKEVQWTLGALLYRTRFLPLRDIQ 450
GDA1_CD39 pfam01150
GDA1/CD39 (nucleoside phosphatase) family;
77-527 1.14e-106

GDA1/CD39 (nucleoside phosphatase) family;


Pssm-ID: 426082  Cd Length: 416  Bit Score: 327.46  E-value: 1.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821     77 TEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNphdLLDIKQMRDRnsqpvVKKIKPGISAMADTPEHASDYLRPLLSFAA 156
Cdd:pfam01150   3 ALPENVKYGIIIDAGSSGTRLHVYKWPDEKEG---LTPIVPLIEE-----FKKLEPGLSSFATKPDAAANYLTPLLEFAE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    157 AHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHED 236
Cdd:pfam01150  75 EHIPEEKRSETPVFLGATAGMRLLPDESKESILKALRNGLKSLTSFPVDDQGIRIIDGQEEGAYGWIAINYLLGNFGKPK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    237 ESdaeatqelaagrrrTVGILDMGGASLQIAYEvPTSTSVLPAKQEEAakillaefNLGCDVQHTEHVYRVYVTTFLGFG 316
Cdd:pfam01150 155 QS--------------TFGAIDLGGASTQIAFE-PSNESAINSTVEDI--------ELGLQFRLYDKDYTLYVHSFLGYG 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    317 GNFARQRYEDLVLNEtlnknrllgqktglSPDNPFLDPCLPVGLTDVVER---NSQVLHVRGRGDWVSCGAMLSPLL--- 390
Cdd:pfam01150 212 ANEALRKYLAKLIQN--------------LSNGILNDPCMPPGYNKTVEVstlEGKQFAIQGTGNWEQCRQSILELLnkn 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821    391 ARSNTSQASLNGIYQSPIDfNNSEFYGFSEFFYCTEDVLRIGGRYHGP-TFAKAAQDYCGMAWSVLTQRFKNGLFSSHAD 469
Cdd:pfam01150 278 AHCPYEPCAFNGVHAPSIG-SLQKSFGASSYFYTVMDFFGLGGEYSSQeKFTDIARKFCSKNWNDIKAGFPKVLDKNISE 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966821    470 EHrlkyQCFKSAWMYQVLHEGFHFPyDYPNLRTAQLVYDREVQWTLGAILYKTRFLPL 527
Cdd:pfam01150 357 ET----YCFKGAYILSLLHDGFNFP-KTEEIQSVGKIAGKEAGWTLGAMLNLTSMIPL 409
ASKHA_NBD_YND1-like cd24039
nucleotide-binding domain (NBD) of yeast nucleoside diphosphatase 1 (YND1) and similar ...
83-520 3.11e-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: 3.11e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   83 NYGLVVDCGSSGSRIFVYFW--PRHNGNPHDLLDIKQM-----RDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFA 155
Cdd:cd24039   2 KYGIVIDAGSSGSRVQIYSWkdPESATSKASLEELKSLphietGIGDGKDWTLKVEPGISSFADHPHVVGEHLKPLLDFA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  156 AAHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLF--SQSQAEVISGKQEGVYAWIGINFVLGRFD 233
Cdd:cd24039  82 LNIIPPSVHSSTPIFLLATAGMRLLPQDQQNAILDAVCDYLRKNYPFLLpdCSEHVQVISGEEEGLYGWLAVNYLMGGFD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  234 HedesdaeATQELAAGRRRTVGILDMGGASLQIAYEVPTStsvlpAKQEEAAKILLAEFNLgcdVQHTEHVYRVYVTTFL 313
Cdd:cd24039 162 D-------APKHSIAHDHHTFGFLDMGGASTQIAFEPNAS-----AAKEHADDLKTVHLRT---LDGSQVEYPVFVTTWL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  314 GFGGNFARQRYEDLVLNE-TLNKNrllgQKTGLSPDNPFLDPCLPVGLtdvvernsqvlhvrgrgdwvscgamlspllar 392
Cdd:cd24039 227 GFGTNEARRRYVESLIEQaGSDTN----SKSNSSSELTLPDPCLPLGL-------------------------------- 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  393 sntsqaslngiyqspidfNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFSSHADEHR 472
Cdd:cd24039 271 ------------------ENNHFVGVSEYWYTTQDVFGLGGAYDFVEFEKAAREFCSKPWESILHELEAGKAGNSVDENR 332
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 9966821  473 LKYQCFKSAWMYQVLHEGFHfpydypnlrTAQLVYDREVQWTLGAILY 520
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 ...
84-519 7.51e-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: 7.51e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDikqmrdRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKK 163
Cdd:cd24003   1 YGVVIDAGSSGTRLHVYKWKARSDDLPSIIE------LVSSGKEKSGKISSSSYADDPDEAKKYLQPLLEFAKAVVPEDR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  164 HKETPLYILCTAGMRLLPERKQLAILADLVKDLPlEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDaeat 243
Cdd:cd24003  75 RSSTPVYLLATAGMRLLPEEQQEAILDAVRTILR-NSGFGFDDGWVRVISGEEEGLYGWLSVNYLLGNLGSEPAKK---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  244 qelaagrrrTVGILDMGGASLQIAYEVPTSTsvlpakqeeaakilLAEFNLGCDVQHTEHVYRVYVTTFLGFGGNFARQR 323
Cdd:cd24003 150 ---------TVGVLDLGGASTQIAFEPPEDD--------------LSSLSNVYPLRLGGKTYDLYSHSFLGYGLNEARKR 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  324 YEDLVLNEtlnknrllgqktglSPDNPFLDPCLPVGLTDvvernsqvlhvrgrgdwvscgamlspllarsntsqaslngi 403
Cdd:cd24003 207 VLESLINN--------------SEGGNVTNPCLPKGYTG----------------------------------------- 231
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  404 yqspidfnnsEFYGFSEFFYCTEDVLRIGGRYHGP-TFAKAAQDYCGMAWSVLTQRFknglfsSHADEHRLKYQCFKSAW 482
Cdd:cd24003 232 ----------PFYAFSNFYYTAKFLGLVDSGTFTLeELEEAAREFCSLDWAELKAKY------PGVDDDFLPNLCFDAAY 295
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 9966821  483 MYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAIL 519
Cdd:cd24003 296 IYSLLEDGFGLDDDSPIIKFVDKINGVELSWTLGAAL 332
ASKHA_NBD_NTPDase1-like cd24044
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 1 ...
84-522 4.93e-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: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNgnphdlldikqmrdRNSQPVVKKI------KPGISAMADTPEHASDYLRPLLSFAAA 157
Cdd:cd24044   1 YGIVIDAGSSHTSLFVYKWPADK--------------ENGTGVVQQVstcrvkGGGISSYENNPSQAGESLEPCLDQAKK 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  158 HVPVKKHKETPLYILCTAGMRLL----PERKQLAILA--DLVKDLPLEFDFlfsqSQAEVISGKQEGVYAWIGINFVLGR 231
Cdd:cd24044  67 KVPEDRRHSTPLYLGATAGMRLLnltnPSAADAILESvrDALKSSKFGFDF----RNARILSGEDEGLYGWITVNYLLGN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  232 FDHEDESDAEATQELaagrrrTVGILDMGGASLQIAYEVptSTSVLPAKQEeaakillAEFNL-GcdvqhteHVYRVYVT 310
Cdd:cd24044 143 LGKYSISSIPRSRPE------TVGALDLGGASTQITFEP--AEPSLPADYT-------RKLRLyG-------KDYNVYTH 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  311 TFLGFGGNFARQRYEDLVLNETLNKNRL------LGQKTGLSPDNPFLDPC-LPVGLTDVVERNSQVlHVRGRGDWVSCG 383
Cdd:cd24044 201 SYLCYGKDEAERRYLASLVQESNYSSTVenpcapKGYSTNVTLAEIFSSPCtSKPLSPSGLNNNTNF-TFNGTSNPDQCR 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  384 AMLSPLLARSNT---SQASLNGIYQSPidfNNSEFYGFSEFFYcTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLtqrfk 460
Cdd:cd24044 280 ELVRKLFNFTSCcssGCCSFNGVFQPP---LNGNFYAFSGFYY-TADFLNLTSNGSLDEFREAVDDFCNKPWDEV----- 350
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9966821  461 ngLFSSHADEHRLKYQCFKSAWMYQVLHEGFHFPY-DYPNLRTAQLVYDREVQWTLGAILYKT 522
Cdd:cd24044 351 --SELPPKGAKFLANYCFDANYILTLLTDGYGFTEeTWRNIHFVKKVNGTEVGWSLGYMLNAT 411
ASKHA_NBD_Lp1NTPDase-like cd24038
nucleotide-binding domain (NBD) of Legionella pneumophila ectonucleoside triphosphate ...
83-521 1.09e-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: 1.09e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   83 NYGLVVDCGSSGSRIFVYFWprHNGNPHDLLDIKQMRDrnsqpvvKKIKPGISAMadTPEHASDYLRPLLSfaaaHVPVK 162
Cdd:cd24038   2 SCTAVIDAGSSGSRLHLYQY--DTDDSNPPIHEIELKN-------NKIKPGLASV--NTTDVDAYLDPLFA----KLPIA 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  163 KHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQsqAEVISGKQEGVYAWIGINFVLGRFdhedesdaea 242
Cdd:cd24038  67 KTSNIPVYFYATAGMRLLPPSEQKKLYQELKDWLAQQSKFQLVE--AKTITGHMEGLYDWIAVNYLLDTL---------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  243 tqelaAGRRRTVGILDMGGASLQIAYEVPTSTSvlpakqeeaaKILLAEFNLGcdvqhtEHVYRVYVTTFLGFGGNFARQ 322
Cdd:cd24038 135 -----KSSKKTVGVLDLGGASTQIAFAVPNNAS----------KDNTVEVKIG------NKTINLYSHSYLGLGQDQARH 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  323 RYEDlvlnetlnknrllgqktglSPDnpfldpCLPVGLTDVverNSQvlhvRGRGDWVSCGAMLSPLLarsnTSQASLNG 402
Cdd:cd24038 194 QFLN-------------------NPD------CFPKGYPLP---SGK----IGQGNFAACVEEISPLI----NSVHNVNS 237
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  403 IYQSPIDFNNsEFYGFSEFFY-CTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNglfsshaDEHRLKYqCFKSA 481
Cdd:cd24038 238 IILLALPPVK-DWYAIGGFSYlASSKPFENNELTSLSLLQQGGNQFCKQSWDELVQQYPD-------DPYLYAY-CLNSA 308
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 9966821  482 WMYQVLHEGFHFPYDypNLRTAQLVYDREVQWTLGAILYK 521
Cdd:cd24038 309 YIYALLVDGYGFPPN--QTTIHNIIDGQNIDWTLGVALYF 346
ASKHA_NBD_GDA1 cd24040
nucleotide-binding domain (NBD) of yeast guanosine-diphosphatase (GDA1) and similar proteins; ...
84-519 5.92e-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: 5.92e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYfwpRHN--GNPHDLLDIKqmrdrnsqpVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPV 161
Cdd:cd24040   1 YALMIDAGSTGSRIHVY---RFNncQPPIPKLEDE---------VFEMTKPGLSSYADDPKGAAASLDPLLQVALQAVPK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  162 KKHKETPLYILCTAGMRLLPERKQLAILaDLVKDLpLE---FDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDhedes 238
Cdd:cd24040  69 ELHSCTPIAVKATAGLRLLGEDKSKEIL-DAVRHR-LEkeyPFVSVELDGVSIMDGKDEGVYAWITVNYLLGNIG----- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  239 daeatqelAAGRRRTVGILDMGGASLQIAYEvPTSTSVLPAKQEEaakiLLAEFNLGcDVQHTehvyrVYVTTFLGFGGN 318
Cdd:cd24040 142 --------GNEKLPTAAVLDLGGGSTQIVFE-PDFPSDEEDPEGD----HKYELTFG-GKDYV-----LYQHSYLGYGLM 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  319 FARQRYEDLVLNetlnkNRLLGQKTGLSPDNPFLD-PCLPVGLTDVV------ERNSQVLHVRGRGDWVSCGAmLSPLLA 391
Cdd:cd24040 203 EARKKIHKLVAE-----NASTGGSEGEATEGGLIAnPCLPPGYTKTVdlvqpeKSKKNVMVGGGKGSFEACRR-LVEKVL 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  392 RSNTSQASL----NGIYQSPI--DFNNSEFYGFSeFFYcteDVLRIGGrYHGPTF-----AKAAQDYC-GMA-WSVLTqr 458
Cdd:cd24040 277 NKDAECESKpcsfNGVHQPSLaeTFKDGPIYAFS-YFY---DRLNPLG-MEPSSFtlgelQKLAEQVCkGETsWDDFF-- 349
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9966821  459 fknGLFSSHADEHRLKYQCFKSAWMYQVLHEGFHFPYDYPnLRTAQLVYDREVQWTLGAIL 519
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 ...
84-519 7.73e-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: 7.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNGNP---HDLLDIKQMrdrnsqpvvkKIKPGISAMADTPEHASDYLRPLLSFAAAHVP 160
Cdd:cd24042   1 YSVIIDAGSSGTRLHVFGYAAESGKPvfpFGEKDYASL----------KTTPGLSSFADNPSGASASLTELLEFAKERVP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  161 VKKHKETPLYILCTAGMRLLPERKQLAILaDLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGrfdhedesda 240
Cdd:cd24042  71 KGKRKETDIRLMATAGLRLLEVPVQEQIL-EVCRRVLRSSGFMFRDEWASVISGTDEGIYAWVAANYALG---------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  241 eatqELAAGRRRTVGILDMGGASLQIAYeVPtstSVLPAKqeeaakillaEFNLgcDVQHTEHVYRVYVTTFLGFGGNFA 320
Cdd:cd24042 140 ----SLGGDPLETTGIVELGGASAQVTF-VP---SEAVPP----------EFSR--TLVYGGVSYKLYSHSFLDFGQEAA 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  321 RQRYEDLVLNETLNKNRllgqktglspDNPFLDPCLPVGLtdVVERNSQ-------------VLHVRGRGDWVSCGAMLS 387
Cdd:cd24042 200 WDKLLESLLNGAAKSTR----------GGVVVDPCTPKGY--IPDTNSQkgeagaladksvaAGSLQAAGNFTECRSAAL 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  388 PLLARSNT----SQASLNGIYQSPID---FNNSEFYGFSEFFyctedvlRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFK 460
Cdd:cd24042 268 ALLQEGKDnclyKHCSIGSTFTPELRgkfLATENFFYTSEFF-------GLGETTWLSEMILAGERFCGEDWSKLKKKHP 340
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9966821  461 nglfsSHADEHRLKYqCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAIL 519
Cdd:cd24042 341 -----GWEEEDLLKY-CFSAAYIVAMLHDGLGIALDDERIRYANKVGEIPLDWALGAFI 393
ASKHA_NBD_NTPDase2 cd24111
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) ...
82-526 2.67e-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: 2.67e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   82 LNYGLVVDCGSSGSRIFVYFWP--RHNG----NPHDLLDIKqmrdrnsqpvvkkiKPGISAMADTPEHASDYLRPLLSFA 155
Cdd:cd24111   2 LKYGIVLDAGSSHTSMFVYKWPadKENDtgivSQHSSCDVQ--------------GGGISSYANDPSKAGQSLVRCLEQA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  156 AAHVPVKKHKETPLYILCTAGMRLL------PERKQLAILADLVKDLPleFDFlfsqSQAEVISGKQEGVYAWIGINFVL 229
Cdd:cd24111  68 LRDVPRDRHASTPLYLGATAGMRLLnltspeASARVLEAVTQTLTSYP--FDF----RGARILSGQEEGVFGWVTANYLL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  230 ---------GRFDHEdesdaeatqelaagRRRTVGILDMGGASLQIAYEvpTSTSVLPAKQEEAAKILlaefnlgcdvqh 300
Cdd:cd24111 142 enfikygwvGQWIRP--------------RKGTLGAMDLGGASTQITFE--TTSPSEDPGNEVHLRLY------------ 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  301 tEHVYRVYVTTFLGFGgnfarqryEDLVLNETLNKnRLLGQKTGLSPDNpfldPCLPVGLTDVV-------------ER- 366
Cdd:cd24111 194 -GQHYRVYTHSFLCYG--------RDQVLLRLLAS-ALQIQGYGAHRFH----PCWPKGYSTQVllqevyqspctmgQRp 259
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  367 ----NSQVLHVRGRGDWVSCGAMLSPL--LARSNTSQASLNGIYQSPIDFNnseFYGFSEFFYcTEDVLR--IGGRYHGP 438
Cdd:cd24111 260 rafnGSAIVSLSGTSNATLCRDLVSRLfnFSSCPFSQCSFNGVFQPPVTGN---FIAFSAFYY-TVDFLTtvMGLPVGTP 335
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  439 T-FAKAAQDYCGMAWSVLTQRfknglfsSHADEHRLKYQCFKSAWMYQVLHEGFHFPYD-YPNLRTAQLVYDREVQWTLG 516
Cdd:cd24111 336 KqLEEATEIICNQTWTELQAK-------VPGQETRLADYCAVAMFIHQLLSRGYHFDERsFREISFQKKAGDTAVGWALG 408
                       490
                ....*....|
gi 9966821  517 AILYKTRFLP 526
Cdd:cd24111 409 YMLNLTNLIP 418
ASKHA_NBD_NTPDase1 cd24110
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase1) ...
81-526 3.27e-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: 168.43  E-value: 3.27e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   81 NLNYGLVVDCGSSGSRIFVYFWPRHNGNphDLLDIKQMRDRNsqpvVKKikPGISAMADTPEHASDYLRPLLSFAAAHVP 160
Cdd:cd24110   4 NVKYGIVLDAGSSHTSLYIYKWPAEKEN--DTGVVQQLEECK----VKG--PGISSYSQKTTKAGASLAECMKKAKEVIP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  161 VKKHKETPLYILCTAGMRLLP-ERKQLA--ILADLVKDLPLefdFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDE 237
Cdd:cd24110  76 ASQHHETPVYLGATAGMRLLRmESEQAAeeVLASVERSLKS---YPFDFQGARIITGQEEGAYGWITINYLLGNFKQDSG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  238 SDAEATQELAAGrrrTVGILDMGGASLQIAYeVPTSTSVlpakqeEAAKILLaEFNL-GCDvqhtehvYRVYVTTFLGFG 316
Cdd:cd24110 153 WFTQLSGGKPTE---TFGALDLGGASTQITF-VPLNSTI------ESPENSL-QFRLyGTD-------YTVYTHSFLCYG 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  317 GNFARQryedlvlnetlnknRLLGQKTGLSPDNPFLDPCLPVGLTDVVERNS----------------QVLHVRGRGDWV 380
Cdd:cd24110 215 KDQALW--------------QKLAQDIQSTSGGILKDPCFHPGYKRVVNVSElygtpctkrfekklpfNQFQVQGTGNYE 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  381 SCGAMLSPLLARSNT--SQASLNGIYQSPIDfnnSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQR 458
Cdd:cd24110 281 QCHQSILKIFNNSHCpySQCSFNGVFLPPLQ---GSFGAFSAFYFVMDFLNLTANVSSLDKMKETIKNFCSKPWEEVKAS 357
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9966821  459 FKNglfsshADEHRLKYQCFKSAWMYQVLHEGFHFPYD-YPNLRTAQLVYDREVQWTLGAILYKTRFLP 526
Cdd:cd24110 358 YPK------VKEKYLSEYCFSGTYILSLLEQGYNFTSDnWNDIHFMGKIKDSDAGWTLGYMLNLTNMIP 420
ASKHA_NBD_NTPDase3 cd24112
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase3) ...
84-519 3.81e-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: 168.02  E-value: 3.81e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNGNphdlldikqmrdrNSQPVVKKIK-----PGISAMADTPEHASDYLRPLLSFAAAH 158
Cdd:cd24112   1 YGIVLDAGSSRTTVYVYQWPAEKEN-------------NTGVVSQTYKcnvkgPGISSYAHNPQKAARALEECMNKVKEI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  159 VPVKKHKETPLYILCTAGMRLL------PERKQLAILADLVKDLPleFDFlfsqSQAEVISGKQEGVYAWIGINFVLGRF 232
Cdd:cd24112  68 IPSHLHNSTPVYLGATAGMRLLklqnetAANEVLSSIENYFKTLP--FDF----RGAHIITGQEEGVYGWITANYLMGNF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  233 DHEDESDAEATQElaagRRRTVGILDMGGASLQIAYevptstsvLPAKQEEaakillaEFNLGCDVQHTEHVYRVYVTTF 312
Cdd:cd24112 142 LEKNLWNAWVHPH----GVETVGALDLGGASTQIAF--------IPEDSLE-------NLNDTVKVSLYGYKYNVYTHSF 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  313 LGFGGNFARQRYEDLVLNETLNKnrllgqktglspdNPFLDPCLPVGLTDVVERN------------------SQVLHVR 374
Cdd:cd24112 203 QCYGKDEAEKRFLANLAQASESK-------------SPVDNPCYPRGYNTSFSMKhifgslctasqrpanydpDDSITFT 269
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  375 GRGDWVSCGAMLSPLL---ARSNTSQASLNGIYQSPIdfnNSEFYGFSEFFYcTEDVLRIGGRYHGPTFAKAAQDYCGMA 451
Cdd:cd24112 270 GTGDPALCKEKVSLLFdfkSCQGKENCSFDGIYQPKV---KGKFVAFAGFYY-TASALNLTGSFTLTTFNSSMWSFCSQS 345
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9966821  452 WSVLTQRFKNglfsshADEHRLKYQCFKSAWMYQVLHEGFHF-PYDYPNLRTAQLVYDREVQWTLGAIL 519
Cdd:cd24112 346 WAQLKVMLPK------FEERYARSYCFSANYIYTLLVRGYKFdPETWPQISFQKEVGNSSIAWSLGYML 408
ASKHA_NBD_NTPDase5 cd24114
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase5) ...
84-520 1.17e-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: 1.17e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDikqmrdrnsQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKK 163
Cdd:cd24114   3 YGIMFDAGSTGTRIHIYTFVQKSPAELPELD---------GEIFESVKPGLSAYADQPEQGAETVRGLLDVAKKTIPSTQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  164 HKETPLYILCTAGMRLLPERKQLAILADlVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRfdhedesdaeat 243
Cdd:cd24114  74 WKKTPVVLKATAGLRLLPEEKAQALLSE-VKEIFEESPFLVPEGSVSIMNGTYEGILAWVTVNFLTGQ------------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  244 qeLAAGRRRTVGILDMGGASLQIAYeVPTSTSVLpakqEEAAKILLAEFNLgcdvqhTEHVYRVYVTTFLGFGGNFARqr 323
Cdd:cd24114 141 --LYGQNQRTVGILDLGGASTQITF-LPRFEKTL----KQAPEDYLTSFEM------FNSTYKLYTHSYLGFGLKAAR-- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  324 yedLVLNETLNKNRLLGQKtglspdnpFLDPCLP---------VGLTDVVERNSQvlhvrGRGDWVSCGAMLSPLlarsn 394
Cdd:cd24114 206 ---LATLGALGTEDQEKQV--------FRSSCLPkglkaewkfGGVTYKYGGNKE-----GETGFKSCYSEVLKV----- 264
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  395 tsqasLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRI----GGRYHGPTFAKAAQDYCgmawSVLTQrfknglFSSHAde 470
Cdd:cd24114 265 -----VKGKLHQPEEMQHSSFYAFSYYYDRAVDTGLIdyeqGGVLEVKDFEKKAKEVC----ENLER------YSSGS-- 327
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 9966821  471 hrlKYQCFKSAWMYQVLHEGFHFpYDYPNLRTAQLVYDREVQWTLGAILY 520
Cdd:cd24114 328 ---PFLCMDLTYITALLKEGFGF-EDNTVLQLTKKVNNVETSWTLGAIFH 373
ASKHA_NBD_NTPDase5-like cd24046
nucleotide-binding domain (NBD) of the ectonucleoside triphosphate diphosphohydrolase 5 ...
84-517 8.55e-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: 8.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVY-FWPRHNGNPHDLLDikqmrdrnsqPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVK 162
Cdd:cd24046   1 YAIVFDAGSTGSRVHVFkFSHSPSGGPLKLLD----------ELFEEVKPGLSSYADDPKEAADSLKPLLEKAKTRIPKE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  163 KHKETPLYILCTAGMRLLPERKQLAILA---DLVKDLPlefdFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHedesd 239
Cdd:cd24046  71 KWSSTPLALKATAGLRLLPEEKANAILDevrKLFKKSP----FLVGEDSVSIMDGTDEGIFSWFTVNFLLGRLGG----- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  240 aeatqelaaGRRRTVGILDMGGASLQIAYeVPTSTSVLPAkqeeaakillAEFNLGCDVQHTEHVYRVYVTTFLGFGGNF 319
Cdd:cd24046 142 ---------SASNTVAALDLGGGSTQITF-APSDKETLSA----------SPKGYLHKVSIFGKKIKLYTHSYLGLGLMA 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  320 ARqryedlvlnetlnKNRLLGQKTGLSPD-NPFLDPCLPVGLTDVVERNSQVLHVRGRG----DWVSCGAMLSPLLARSN 394
Cdd:cd24046 202 AR-------------LAILQGSSTNSNSGtTELKSPCFPPNFKGEWWFGGKKYTSSIGGsseySFDACYKLAKKVVDSSV 268
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  395 TSQaslngiyqsPIDFNNSEFYGFSEFFYCTEDVlRIGGRYHGPT-----FAKAAQDYCGMawsvltqrfknglfsshaD 469
Cdd:cd24046 269 IHK---------PEELKSREIYAFSYFYDRAVDA-GLIDEQEGGTvtvgdFKKAAKKACSN------------------P 320
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 9966821  470 EHRLKYQCFKSAWMYQVLHEGFHFPYDYPnLRTAQLVYDREVQWTLGA 517
Cdd:cd24046 321 NPEQPFLCLDLTYIYALLHDGYGLPDDKK-LTLVKKINGVEISWALGA 367
ASKHA_NBD_NTPDase8 cd24113
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 8 (NTPDase8) ...
80-522 7.32e-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: 7.32e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   80 PNLNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSqpvvkkikPGISAMADTPEHASDYLRPLLSFAAAHV 159
Cdd:cd24113  21 PGIKYGIVFDAGSSHTSLFLYQWPADKENGTGIVSQVLSCDVEG--------PGISSYAQNPAKAGESLKPCLDEALAAI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  160 PVKKHKETPLYILCTAGMRLLPERKQ------LAILADLVKDLPLEFdflfsqSQAEVISGKQEGVYAWIGINFVLGRF- 232
Cdd:cd24113  93 PAEQQKETPVYLGATAGMRLLRLQNStqsdeiLAEVSKTIGSYPFDF------QGARILTGMEEGAYGWITVNYLLETFi 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  233 DHEDESDAEATQElaagrRRTVGILDMGGASLQIAYeVPtSTSVLPAKQEeaAKILLAEFNlgcdvqhtehvYRVYVTTF 312
Cdd:cd24113 167 KYSFEGKWIHPKG-----GNILGALDLGGASTQITF-VP-GGPIEDKNTE--ANFRLYGYN-----------YTVYTHSY 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  313 LGFGGNFARQRyedlvLNETLNKNR-----------LLGQKTGLSPDNPFLDPCLPvglTDVVERNSQVLHVRGRGDWVS 381
Cdd:cd24113 227 LCYGKDQMLKR-----LLAALLQGRnlaalishpcyLKGYTTNLTLASIYDSPCVP---DPPPYSLAQNITVEGTGNPAE 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  382 CGAMLSPLL---ARSNTSQASLNGIYQSPIdfnNSEFYGFSEFFYcTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQR 458
Cdd:cd24113 299 CLSAIRNLFnftACGGSQTCAFNGVYQPPV---NGEFFAFSAFYY-TFDFLNLTSGQSLSTVNSTIWEFCSKPWTELEAS 374
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9966821  459 FKNglfsshADEHRLKYQCFKSAWMYQVLHEGFHFPYD-YPNLRTAQLVYDREVQWTLGAILYKT 522
Cdd:cd24113 375 YPK------EKDKRLKDYCASGLYILTLLVDGYKFDSEtWNNIHFQKKAGNTDIGWTLGYMLNLT 433
ASKHA_NBD_AtAPY7-like cd24043
nucleotide-binding domain (NBD) of Arabidopsis thaliana apyrase 7 (AtAPY7) and similar ...
84-520 2.34e-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: 157.61  E-value: 2.34e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNGNPH--DLLDI--KQMRDRNSQPVVKKIK-----PGISAMADTPEHASDYLRPLLSF 154
Cdd:cd24043   1 YAIVMDCGSTGTRVYVYSWARNPSKDSlpVMVDPptVASAALVKKPKKRAYKrvetePGLDKLADNETGLGAALGPLLDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  155 AAAHVPVKKHKETPLYILCTAGMRLLPERKQlAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDH 234
Cdd:cd24043  81 AGKQIPRSQHPRTPVFLFATAGLRRLPPDDS-AWLLDKAWGVLEASPFRFERSWVRIISGTEEAYYGWIALNYLTGRLGQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  235 EDESDAeatqelaagrrrTVGILDMGGASLQIAYEvptsTSVLPAKqeeaakillaEFNLGCDVQHTEHvyRVYVTTFLG 314
Cdd:cd24043 160 GPGKGA------------TVGSLDLGGSSLEVTFE----PEAVPRG----------EYGVNLSVGSTEH--HLYAHSHAG 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  315 FGGNFARQRYEDLVLNETLNKNRLLGQKTGLSPDNPFLDP-----------CLPVGLTDVVERNSQV-LHVRGRGDWVSC 382
Cdd:cd24043 212 YGLNDAFDKSVALLLKDQNATPPVRLREGTLEVEHPCLHSgynrpykcshhAGAPPVRGLKAGPGGAsVQLVGAPNWGAC 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  383 GAMLSPLLARSNTSQASLN----GIYQSPIdfnNSEFYGFSEFFYC-----------TEDVLRiggryhgptfakAAQDY 447
Cdd:cd24043 292 QALAGRVVNTTASAECEFPpcalGKHQPRP---QGQFYALTGFFVVykffglsatasLDDLLA------------KGQEF 356
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9966821  448 CGMAWSVLTqrfknglfSSHADEHRLKYQCFKSAWMYQVLHEGFHfpydypnLRTAQL-VYDREVQWTLGAILY 520
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), ...
83-517 4.58e-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: 4.58e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   83 NYGLVVDCGSSGSRIFVYFWPRHNgnphDLLDIKqmrdrNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVK 162
Cdd:cd24041   1 RYAVVFDAGSTGSRVHVFKFDQNL----DLLHLG-----LDLELFEQIKPGLSSYADDPEQAAKSLRPLLDKALAVVPEE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  163 KHKETPLYILCTAGMRLLPERKQLAILADlVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDEsdaea 242
Cdd:cd24041  72 LQSKTPVRLGATAGLRLLPGDASENILQE-VRDLLRNYSFKVQPDAVSIIDGTDEGSYQWVTVNYLLGNLGKPFT----- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  243 tqelaagrrRTVGILDMGGASLQIAYEVPTSTSVLPAKQEEAAKILLAEFNLGcdvqhtEHVYRVYVTTFLGFGGNFARQ 322
Cdd:cd24041 146 ---------KTVGVVDLGGGSVQMAYAVSDETAKNAPKPTDGEDGYIRKLVLK------GKTYDLYVHSYLGYGLMAARA 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  323 ryedlvlnETLNknrlLGQKTGLSpdnpfldPCLPVGLTDVVERNSQVLHVRGR---GDWVSCGAMLSPLL---ARSNTS 396
Cdd:cd24041 211 --------EILK----LTEGTSAS-------PCIPAGFDGTYTYGGEEYKAVAGesgADFDKCKKLALKALkldEPCGYE 271
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  397 QASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIG-----GRYHGPTFAKAAQDYCGMAWSVLTQRFKnglfssHADEH 471
Cdd:cd24041 272 QCTFGGVWNGGGGGGQKKLFVASYFFDRASEVGIIDdqasqAVVRPSDFEKAAKKACKLNVEEIKSKYP------LVEEK 345
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 9966821  472 RLKYQCFKSAWMYQVLHEGFhfpyDYPNLRTAQLV-------YDREVQWTLGA 517
Cdd:cd24041 346 DAPFLCMDLTYQYTLLVDGF----GLDPDQEITLVkqieyqgALVEAAWPLGA 394
ASKHA_NBD_NTPDase6 cd24115
nucleotide-binding domain (NBD) of ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase6) ...
84-520 1.72e-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: 1.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821   84 YGLVVDCGSSGSRIFVYFWPRHNGNPHDLldikqmrdrnSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKK 163
Cdd:cd24115   3 YGIMFDAGSTGTRIHIFKFTRPPNEAPKL----------THETFKALKPGLSAYADEPEKCAEGIQELLDVAKQDIPSDF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  164 HKETPLYILCTAGMRLLPERKQlAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGrfdhedesdaeat 243
Cdd:cd24115  73 WKATPLVLKATAGLRLLPGEKA-QKLLDKVKEVFKASPFLVGDDSVSIMDGTDEGISAWITVNFLTG------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  244 qELAAGRRRTVGILDMGGASLQIAYeVPTSTSVLPAKQEEaakiLLAEFNLGcdvqhtEHVYRVYVTTFLGFGGNFARQr 323
Cdd:cd24115 139 -SLHGTGRSSVGMLDLGGGSTQITF-SPHSEGTLQTSPID----YITSFQMF------NRTYTLYSHSYLGLGLMSARL- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  324 yedlvlnetlnknRLLGQKTGLSPDNP--FLDPCLPVGLTDVVERNSQVLHVRGRGD----WVSCGAMLSPLLARSntsq 397
Cdd:cd24115 206 -------------AILGGVEGKPLKEGqeLVSPCLAPEYKGEWEHAEITYKIKGQKAeeplYESCYARVEKMLYKK---- 268
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  398 aslngiYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPT----FAKAAQDYCgmawsvltQRFKNGLFSShadehrl 473
Cdd:cd24115 269 ------VHKAEEVKNLDFYAFSYYYDRAVDVGLIDEEKGGSLkvgdFEIAAKKVC--------KTMESQPGEK------- 327
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 9966821  474 KYQCFKSAWMYQVLHEgFHFPYDyPNLRTAQLVYDREVQWTLGAILY 520
Cdd:cd24115 328 PFLCMDLTYISVLLQE-LGFPKD-KELKLARKIDNVETSWALGATFH 372
ASKHA_NBD_TgNTPase-like cd24037
nucleotide-binding domain (NBD) of Toxoplasma gondii nucleoside triphosphate hydrolase (NTPase) ...
168-279 5.78e-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: 5.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966821  168 PLYILCTAGMRLLPE--RKQLAILADLVKDLPL---EFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDhEDESDAEA 242
Cdd:cd24037 124 PVMLCSTAGVRDFHDwyRDALFVLLRHLINNPSpahGYKFFTNPFWTRPITGAEEGLFAFITLNHLSRRLG-EDPARCMI 202
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 9966821  243 TQELAAGRRRT-VGILDMGGASLQIAYEVPTSTsVLPA 279
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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