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Conserved domains on  [gi|1370512481|ref|XP_024302950|]
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autotaxin isoform X9 [Homo sapiens]

Protein Classification

DNA/RNA non-specific endonuclease( domain architecture ID 12193410)

DNA/RNA non-specific endonuclease catalyzes the cleavage of dsRNA, ssRNA, ssDNA, dsDNA, as well as RNA/DNA hybrids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
162-474 8.19e-106

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


:

Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 329.77  E-value: 8.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 162 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 241
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 242 GREKFNHRWWGGQPLWITATKQGVKAGTFFW----------------------SVVIPHERRILTIL--QWLTLPD---- 293
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 294 HERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 373
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 374 TNVDDITLV-PGTLGRIRSKFSN-------NAKYDPKAIIANLTC--KKPDQHFKPYLKQHLPKRLHYanNRRIEDIHLL 443
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1370512481 444 VERRWHVARKpldvyKKPSGKCFFQGDHGFD 474
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
607-837 2.37e-73

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases


:

Pssm-ID: 214683  Cd Length: 210  Bit Score: 238.80  E-value: 2.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  607 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 685
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  686 YDAFLVTNMVPMYPAFKRV-WNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDkIKQYVEGS-SIPVPTHYYSI 763
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE-VKYQVIGSkNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512481  764 ITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCnssedeskwveelMKMHTARVRDIEHLTSLDFFRKTSRS 837
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
51-94 2.49e-14

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


:

Pssm-ID: 197571  Cd Length: 43  Bit Score: 67.40  E-value: 2.49e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1370512481   51 ISGSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKTA 94
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
95-138 1.97e-13

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


:

Pssm-ID: 197571  Cd Length: 43  Bit Score: 65.09  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1370512481   95 RGWECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGES 138
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
162-474 8.19e-106

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 329.77  E-value: 8.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 162 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 241
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 242 GREKFNHRWWGGQPLWITATKQGVKAGTFFW----------------------SVVIPHERRILTIL--QWLTLPD---- 293
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 294 HERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 373
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 374 TNVDDITLV-PGTLGRIRSKFSN-------NAKYDPKAIIANLTC--KKPDQHFKPYLKQHLPKRLHYanNRRIEDIHLL 443
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1370512481 444 VERRWHVARKpldvyKKPSGKCFFQGDHGFD 474
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
160-514 2.98e-94

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 296.80  E-value: 2.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 160 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFH 239
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 240 lRGREKFNHRWWGGQPLWITATKQGVKAGTFFW--SVV----------------------IPHERRILTILQWLTLpdhE 295
Cdd:cd16018    80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWpgSEVaiigynptpiplggywqpyndsFPFEERVDTILEWLDL---E 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 296 RPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVtcdrteflsnyltn 375
Cdd:cd16018   156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 376 vdditlvpgtlgrirskfsnnakydpkaiianltckkpdqhfkpylkqhlpkrlhyannrriedihllverrwhvarkpl 455
Cdd:cd16018       --------------------------------------------------------------------------------
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370512481 456 dvykkpsgkcffqGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLG 514
Cdd:cd16018   222 -------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
607-837 2.37e-73

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases


Pssm-ID: 214683  Cd Length: 210  Bit Score: 238.80  E-value: 2.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  607 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 685
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  686 YDAFLVTNMVPMYPAFKRV-WNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDkIKQYVEGS-SIPVPTHYYSI 763
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE-VKYQVIGSkNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512481  764 ITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCnssedeskwveelMKMHTARVRDIEHLTSLDFFRKTSRS 837
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
589-847 5.25e-67

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases. They exists as monomers and homodimers.


Pssm-ID: 238043  Cd Length: 241  Bit Score: 223.02  E-value: 5.25e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 589 LLYGRPAVLYRTryDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVpDHLTSCVRPDVRVSPSFSQNCLAYKNDKQM 668
Cdd:cd00091     1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNV-DRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 669 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGlHDTEDKIK 746
Cdd:cd00091    78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDG-DGGSYLST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 747 QYVEGSSIPVPTHYYSIITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCNSSedeskWVEELMKMHtarVRDIEHLT 826
Cdd:cd00091   157 QVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPHDTLEFIL-----CVEKTFQVP---VASVEKAT 220
                         250       260
                  ....*....|....*....|.
gi 1370512481 827 SLDFFRKTSRSYPEILTLKTY 847
Cdd:cd00091   221 GLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
150-516 2.69e-61

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 211.92  E-value: 2.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 150 AAECPAGFVRPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSM 229
Cdd:COG1524    14 AAAAAAAPPAKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 230 YDPVFDAT-FHLRGREKFNH--RWWGGQPLWITATKQGVKAGTFFWSV---------VIPH------------ERRILTI 285
Cdd:COG1524    92 YDPELGRVvNSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSfegsglidaARPYpydgrkpllgnpAADRWIA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 286 LQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTcdr 365
Cdd:COG1524   172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP--- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 366 TEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAkydpkAIIANLtckkpDQHFKPYLKQHLpKRLHYANNrRIEDIHLLVE 445
Cdd:COG1524   249 PDIDLNRLRLAGLLAVRAGESAHLYLKDGADA-----EVRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAK 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370512481 446 RRWHVARKPLdvykkpsgkcffqGDHGFDNKvNSMQTVFVGYGSTFKyktkvPPFENIELYNVMCDLLGLK 516
Cdd:COG1524   317 PGWALDAPLK-------------GSHGGLPD-EEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
583-831 7.74e-18

DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];


Pssm-ID: 441469  Cd Length: 238  Bit Score: 83.80  E-value: 7.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 583 STEERHLLYGRPAV---LYRTRYdILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDhlTSCVRPDVRVSPSFSqnc 659
Cdd:COG1864     4 GYDPDFLLLGLPSLaraLSTNNY-LLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKR--SDDFRPDPRLPSGYR--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 660 lA----YKN---DKqmsyGFLFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRVlVKKYASERNGVNVISGPI 730
Cdd:COG1864    78 -AtladYTGsgyDR----GHLAPSAdRTFSKEANSETFLMTNISPQAPDFNQgIWARLENY-VRDLARKGGEVYVVTGPV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 731 FDydydglhdtEDKIKQYVEGsSIPVPTHYYSIItscLDftqpADKCDGPLSVSSFILPHRPdneescNSSEDESKWVee 810
Cdd:COG1864   152 FD---------DGDLKTIGSG-GVAVPTAFWKVV---VD----PDKNTGTLRAIAFLLPNTA------LSSGPLRTYQ-- 206
                         250       260
                  ....*....|....*....|.
gi 1370512481 811 lmkmhTArVRDIEHLTSLDFF 831
Cdd:COG1864   207 -----VS-VDEIEKLTGLDFF 221
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
51-94 2.49e-14

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 67.40  E-value: 2.49e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1370512481   51 ISGSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKTA 94
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
95-138 1.97e-13

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 65.09  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1370512481   95 RGWECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGES 138
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
97-137 1.21e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.01  E-value: 1.21e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370512481  97 WECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGE 137
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
603-837 1.54e-11

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 64.76  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 603 DILYHTDFESGYSEIFLMPLWTSYTVSKQAevssvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGF----LFPPY- 677
Cdd:pfam01223  17 VVLFYKYYSLCYDRRTRRALWVAHHLTGAS-----LAGSKGRRRPGFKQDPRIPGAYFRTLYTDYTGSGFdrghLAPAAd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 678 LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRvLVKKYASERNG-VNVISGPIFDYDYDGLHdtedkikqyvegsSIP 755
Cdd:pfam01223  92 FKFSAGANAATFNFTNIAPQWAGFNQgNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLDKN-------------KVA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 756 VPTHYYSIITScldftqPADKCDGPLSVSSFILPhrpdnEESCNSSEDESKWVEElmkmhtarVRDIEHLTSLDFFRKTS 835
Cdd:pfam01223 158 VPTHFWKVILS------EDGDGGGGLNAPAFVLP-----NKYILDDGPLRTFQVP--------VDELERLTGLDFCCGVP 218

                  ..
gi 1370512481 836 RS 837
Cdd:pfam01223 219 DA 220
Somatomedin_B pfam01033
Somatomedin B domain;
53-93 9.33e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 57.31  E-value: 9.33e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370512481  53 GSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKT 93
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
162-474 8.19e-106

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 329.77  E-value: 8.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 162 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 241
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 242 GREKFNHRWWGGQPLWITATKQGVKAGTFFW----------------------SVVIPHERRILTIL--QWLTLPD---- 293
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 294 HERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 373
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 374 TNVDDITLV-PGTLGRIRSKFSN-------NAKYDPKAIIANLTC--KKPDQHFKPYLKQHLPKRLHYanNRRIEDIHLL 443
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1370512481 444 VERRWHVARKpldvyKKPSGKCFFQGDHGFD 474
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
160-514 2.98e-94

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 296.80  E-value: 2.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 160 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFH 239
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 240 lRGREKFNHRWWGGQPLWITATKQGVKAGTFFW--SVV----------------------IPHERRILTILQWLTLpdhE 295
Cdd:cd16018    80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWpgSEVaiigynptpiplggywqpyndsFPFEERVDTILEWLDL---E 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 296 RPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVtcdrteflsnyltn 375
Cdd:cd16018   156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 376 vdditlvpgtlgrirskfsnnakydpkaiianltckkpdqhfkpylkqhlpkrlhyannrriedihllverrwhvarkpl 455
Cdd:cd16018       --------------------------------------------------------------------------------
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370512481 456 dvykkpsgkcffqGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLG 514
Cdd:cd16018   222 -------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
607-837 2.37e-73

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases


Pssm-ID: 214683  Cd Length: 210  Bit Score: 238.80  E-value: 2.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  607 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 685
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  686 YDAFLVTNMVPMYPAFKRV-WNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDkIKQYVEGS-SIPVPTHYYSI 763
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE-VKYQVIGSkNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512481  764 ITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCnssedeskwveelMKMHTARVRDIEHLTSLDFFRKTSRS 837
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
589-847 5.25e-67

DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases. They exists as monomers and homodimers.


Pssm-ID: 238043  Cd Length: 241  Bit Score: 223.02  E-value: 5.25e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 589 LLYGRPAVLYRTryDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVpDHLTSCVRPDVRVSPSFSQNCLAYKNDKQM 668
Cdd:cd00091     1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNV-DRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 669 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGlHDTEDKIK 746
Cdd:cd00091    78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDG-DGGSYLST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 747 QYVEGSSIPVPTHYYSIITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCNSSedeskWVEELMKMHtarVRDIEHLT 826
Cdd:cd00091   157 QVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPHDTLEFIL-----CVEKTFQVP---VASVEKAT 220
                         250       260
                  ....*....|....*....|.
gi 1370512481 827 SLDFFRKTSRSYPEILTLKTY 847
Cdd:cd00091   221 GLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
150-516 2.69e-61

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 211.92  E-value: 2.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 150 AAECPAGFVRPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSM 229
Cdd:COG1524    14 AAAAAAAPPAKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 230 YDPVFDAT-FHLRGREKFNH--RWWGGQPLWITATKQGVKAGTFFWSV---------VIPH------------ERRILTI 285
Cdd:COG1524    92 YDPELGRVvNSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSfegsglidaARPYpydgrkpllgnpAADRWIA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 286 LQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTcdr 365
Cdd:COG1524   172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP--- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 366 TEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAkydpkAIIANLtckkpDQHFKPYLKQHLpKRLHYANNrRIEDIHLLVE 445
Cdd:COG1524   249 PDIDLNRLRLAGLLAVRAGESAHLYLKDGADA-----EVRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAK 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370512481 446 RRWHVARKPLdvykkpsgkcffqGDHGFDNKvNSMQTVFVGYGSTFKyktkvPPFENIELYNVMCDLLGLK 516
Cdd:COG1524   317 PGWALDAPLK-------------GSHGGLPD-EEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
160-383 4.72e-46

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 164.90  E-value: 4.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 160 PPLIIFSVDGFRASYMKKGSKVM---PNIEKLRSCGTHSpYMRPVYP-TKTFPNLYTLATGLYPESHGIVGNSMYDPvfd 235
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPApttPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADP--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 236 atfhlRGREKFNHRWWGGQPLWITATKQGVKAGTFFwsvvipherrILTILQWLTLpdhERPSVYAFYSEQPDFSGHKYG 315
Cdd:cd00016    77 -----ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG----------LLKAIDETSK---EKPFVLFLHFDGPDGPGHAYG 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370512481 316 PFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVP 383
Cdd:cd00016   139 PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVP 206
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
607-836 1.22e-43

DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity. An histidine has been shown to be essential for the activity of the Serratia marcescens nuclease. This residue is located in a conserved region which also contains an aspartic acid residue that could be implicated in the binding of the divalent ion.


Pssm-ID: 214889 [Multi-domain]  Cd Length: 198  Bit Score: 156.80  E-value: 1.22e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  607 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLS-SSPEAK 685
Cdd:smart00892   1 YKHYALCYDERRRLPLWVAYHLTGSTRQGKNTGRKRPWFKPDGWHLPAIFQAVNSDYTGSGYDRGHLAPAADHgVSQEAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481  686 YDAFLVTNMVPMYPAFKR-VWNYFQRVLVKKYASERNGVNVISGPIFDYDYDglhdtedkikqyveGSSIPVPTHYYSII 764
Cdd:smart00892  81 AATFYLTNIVPQTAGFNQgNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLP--------------DNNVAVPSHFWKVI 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370512481  765 TSCldftqpaDKCDGPLSVSSFILPHRPDNEescnssedeskwvEELMKMHTARVRDIEHLTSLDFFRKTSR 836
Cdd:smart00892 147 LSE-------DGSNGGLAAIAFNLPNAPINE-------------DYPLCEFQVPVDNIERLTGLDFFCGLPD 198
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
583-831 7.74e-18

DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];


Pssm-ID: 441469  Cd Length: 238  Bit Score: 83.80  E-value: 7.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 583 STEERHLLYGRPAV---LYRTRYdILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDhlTSCVRPDVRVSPSFSqnc 659
Cdd:COG1864     4 GYDPDFLLLGLPSLaraLSTNNY-LLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKR--SDDFRPDPRLPSGYR--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 660 lA----YKN---DKqmsyGFLFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRVlVKKYASERNGVNVISGPI 730
Cdd:COG1864    78 -AtladYTGsgyDR----GHLAPSAdRTFSKEANSETFLMTNISPQAPDFNQgIWARLENY-VRDLARKGGEVYVVTGPV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 731 FDydydglhdtEDKIKQYVEGsSIPVPTHYYSIItscLDftqpADKCDGPLSVSSFILPHRPdneescNSSEDESKWVee 810
Cdd:COG1864   152 FD---------DGDLKTIGSG-GVAVPTAFWKVV---VD----PDKNTGTLRAIAFLLPNTA------LSSGPLRTYQ-- 206
                         250       260
                  ....*....|....*....|.
gi 1370512481 811 lmkmhTArVRDIEHLTSLDFF 831
Cdd:COG1864   207 -----VS-VDEIEKLTGLDFF 221
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
51-94 2.49e-14

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 67.40  E-value: 2.49e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1370512481   51 ISGSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKTA 94
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
95-138 1.97e-13

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 65.09  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1370512481   95 RGWECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGES 138
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
97-137 1.21e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.01  E-value: 1.21e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370512481  97 WECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGE 137
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
603-837 1.54e-11

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 64.76  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 603 DILYHTDFESGYSEIFLMPLWTSYTVSKQAevssvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGF----LFPPY- 677
Cdd:pfam01223  17 VVLFYKYYSLCYDRRTRRALWVAHHLTGAS-----LAGSKGRRRPGFKQDPRIPGAYFRTLYTDYTGSGFdrghLAPAAd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 678 LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRvLVKKYASERNG-VNVISGPIFDYDYDGLHdtedkikqyvegsSIP 755
Cdd:pfam01223  92 FKFSAGANAATFNFTNIAPQWAGFNQgNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLDKN-------------KVA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 756 VPTHYYSIITScldftqPADKCDGPLSVSSFILPhrpdnEESCNSSEDESKWVEElmkmhtarVRDIEHLTSLDFFRKTS 835
Cdd:pfam01223 158 VPTHFWKVILS------EDGDGGGGLNAPAFVLP-----NKYILDDGPLRTFQVP--------VDELERLTGLDFCCGVP 218

                  ..
gi 1370512481 836 RS 837
Cdd:pfam01223 219 DA 220
Somatomedin_B pfam01033
Somatomedin B domain;
53-93 9.33e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 57.31  E-value: 9.33e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370512481  53 GSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKT 93
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
311-360 1.45e-05

GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293747  Cd Length: 289  Bit Score: 47.94  E-value: 1.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370512481 311 GHKYGPFGPEMTNPLREIDKIVGQLMDglkqlKLHRCVNVIFVGDHGMED 360
Cdd:cd16023   174 GHRYGPNHPEMARKLTQMDQFIRDIIE-----RLDDDTLLLVFGDHGMTE 218
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
311-360 4.63e-05

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 46.02  E-value: 4.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370512481 311 GHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMED 360
Cdd:cd16024   159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMTD 208
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
159-232 4.65e-03

SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 40.21  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512481 159 RPPLIIF-SVDGFRASYM--------KKGSK-------VMPNieklrscgTHSPYMrpvyPTKTFPNLYTLATGLYPESH 222
Cdd:cd16016     1 RPKLVVGiVVDQMRADYLyryrdrfgEGGFKrllnegfVFEN--------AHYNYA----PTDTAPGHATIYTGTTPAIH 68
                          90
                  ....*....|
gi 1370512481 223 GIVGNSMYDP 232
Cdd:cd16016    69 GIIGNDWYDR 78
 
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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