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Conserved domains on  [gi|195947389|ref|NP_001124335|]
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autotaxin isoform 3 preproprotein [Homo sapiens]

Protein Classification

Enpp and NUC domain-containing protein( domain architecture ID 12193410)

protein containing domains SO, Enpp, and NUC

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 ...
166-478 1.79e-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: 332.46  E-value: 1.79e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  166 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 245
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  246 GREKFNHRWWGGQPLWITATKQGVKAGTFFW----------------------SVVIPHERRILTIL--QWLTLPD---- 297
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  298 HERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 377
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  378 TNVDDITLV-PGTLGRIRSKFSN-------NAKYDPKAIIANLTC--KKPDQHFKPYLKQHLPKRLHYanNRRIEDIHLL 447
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340       350
                  ....*....|....*....|....*....|.
gi 195947389  448 VERRWHVARKpldvyKKPSGKCFFQGDHGFD 478
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
640-870 4.50e-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: 4.50e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   640 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 718
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   719 YDAFLVTNMVPMYPAFKRV-WNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDkIKQYVEGS-SIPVPTHYYSI 796
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE-VKYQVIGSkNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195947389   797 ITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCnssedeskwveelMKMHTARVRDIEHLTSLDFFRKTSRS 870
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
55-98 2.83e-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: 2.83e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 195947389    55 ISGSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKTA 98
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
99-142 2.17e-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: 2.17e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 195947389    99 RGWECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGES 142
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
166-478 1.79e-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: 332.46  E-value: 1.79e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  166 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 245
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  246 GREKFNHRWWGGQPLWITATKQGVKAGTFFW----------------------SVVIPHERRILTIL--QWLTLPD---- 297
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  298 HERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 377
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  378 TNVDDITLV-PGTLGRIRSKFSN-------NAKYDPKAIIANLTC--KKPDQHFKPYLKQHLPKRLHYanNRRIEDIHLL 447
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340       350
                  ....*....|....*....|....*....|.
gi 195947389  448 VERRWHVARKpldvyKKPSGKCFFQGDHGFD 478
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
164-518 1.08e-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: 298.34  E-value: 1.08e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 164 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFH 243
Cdd:cd16018    1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 244 lRGREKFNHRWWGGQPLWITATKQGVKAGTFFW--SVV----------------------IPHERRILTILQWLTLpdhE 299
Cdd:cd16018   80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWpgSEVaiigynptpiplggywqpyndsFPFEERVDTILEWLDL---E 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 300 RPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVtcdrteflsnyltn 379
Cdd:cd16018  156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 380 vdditlvpgtlgrirskfsnnakydpkaiianltckkpdqhfkpylkqhlpkrlhyannrriedihllverrwhvarkpl 459
Cdd:cd16018      --------------------------------------------------------------------------------
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 195947389 460 dvykkpsgkcffqGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLG 518
Cdd:cd16018  222 -------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
640-870 4.50e-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: 4.50e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   640 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 718
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   719 YDAFLVTNMVPMYPAFKRV-WNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDkIKQYVEGS-SIPVPTHYYSI 796
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE-VKYQVIGSkNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195947389   797 ITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCnssedeskwveelMKMHTARVRDIEHLTSLDFFRKTSRS 870
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
622-880 5.22e-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: 223.40  E-value: 5.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 622 LLYGRPAVLYRTryDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVpDHLTSCVRPDVRVSPSFSQNCLAYKNDKQM 701
Cdd:cd00091    1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNV-DRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 702 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGlHDTEDKIK 779
Cdd:cd00091   78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDG-DGGSYLST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 780 QYVEGSSIPVPTHYYSIITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCNSSedeskWVEELMKMHtarVRDIEHLT 859
Cdd:cd00091  157 QVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPHDTLEFIL-----CVEKTFQVP---VASVEKAT 220
                        250       260
                 ....*....|....*....|.
gi 195947389 860 SLDFFRKTSRSYPEILTLKTY 880
Cdd:cd00091  221 GLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
154-520 3.72e-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: 3.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 154 AAECPAGFVRPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSM 233
Cdd:COG1524   14 AAAAAAAPPAKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 234 YDPVFDAT-FHLRGREKFNH--RWWGGQPLWITATKQGVKAGTFFWSV---------VIPH------------ERRILTI 289
Cdd:COG1524   92 YDPELGRVvNSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSfegsglidaARPYpydgrkpllgnpAADRWIA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 290 LQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTcdr 369
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP--- 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 370 TEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAkydpkAIIANLtckkpDQHFKPYLKQHLpKRLHYANNrRIEDIHLLVE 449
Cdd:COG1524  249 PDIDLNRLRLAGLLAVRAGESAHLYLKDGADA-----EVRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAK 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195947389 450 RRWHVARKPLdvykkpsgkcffqGDHGFDNKvNSMQTVFVGYGSTFKyktkvPPFENIELYNVMCDLLGLK 520
Cdd:COG1524  317 PGWALDAPLK-------------GSHGGLPD-EEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
619-864 1.13e-17

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 83.42  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 619 ERHLLYGRPAV---LYRTRYdILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDhlTSCVRPDVRVSPSFSqnclA- 694
Cdd:COG1864    7 PDFLLLGLPSLaraLSTNNY-LLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKR--SDDFRPDPRLPSGYR----At 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 695 ---YKN---DKqmsyGFLFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRVlVKKYASERNGVNVISGPIFDy 766
Cdd:COG1864   80 ladYTGsgyDR----GHLAPSAdRTFSKEANSETFLMTNISPQAPDFNQgIWARLENY-VRDLARKGGEVYVVTGPVFD- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 767 dydglhdtEDKIKQYVEGsSIPVPTHYYSIItscLDftqpADKCDGPLSVSSFILPHRPdneescNSSEDESKWVeelmk 846
Cdd:COG1864  154 --------DGDLKTIGSG-GVAVPTAFWKVV---VD----PDKNTGTLRAIAFLLPNTA------LSSGPLRTYQ----- 206
                        250
                 ....*....|....*...
gi 195947389 847 mhTArVRDIEHLTSLDFF 864
Cdd:COG1864  207 --VS-VDEIEKLTGLDFF 221
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
55-98 2.83e-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: 2.83e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 195947389    55 ISGSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKTA 98
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
99-142 2.17e-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: 2.17e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 195947389    99 RGWECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGES 142
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
101-141 1.26e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.01  E-value: 1.26e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 195947389  101 WECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGE 141
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
636-870 1.64e-11

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 64.76  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  636 DILYHTDFESGYSEIFLMPLWTSYTVSKQAevssvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGF----LFPPY- 710
Cdd:pfam01223  17 VVLFYKYYSLCYDRRTRRALWVAHHLTGAS-----LAGSKGRRRPGFKQDPRIPGAYFRTLYTDYTGSGFdrghLAPAAd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  711 LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRvLVKKYASERNG-VNVISGPIFDYDYDGLHdtedkikqyvegsSIP 788
Cdd:pfam01223  92 FKFSAGANAATFNFTNIAPQWAGFNQgNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLDKN-------------KVA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  789 VPTHYYSIITScldftqPADKCDGPLSVSSFILPhrpdnEESCNSSEDESKWVEElmkmhtarVRDIEHLTSLDFFRKTS 868
Cdd:pfam01223 158 VPTHFWKVILS------EDGDGGGGLNAPAFVLP-----NKYILDDGPLRTFQVP--------VDELERLTGLDFCCGVP 218

                  ..
gi 195947389  869 RS 870
Cdd:pfam01223 219 DA 220
Somatomedin_B pfam01033
Somatomedin B domain;
57-97 9.68e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 57.31  E-value: 9.68e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 195947389   57 GSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKT 97
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
166-478 1.79e-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: 332.46  E-value: 1.79e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  166 LIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLR 245
Cdd:pfam01663   1 LLVISLDGFRADYLDRF-ELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  246 GREKFNHRWWGGQPLWITATKQGVKAGTFFW----------------------SVVIPHERRILTIL--QWLTLPD---- 297
Cdd:pfam01663  80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWpgsevdystyygtpprylkddyNNSVPFEDRVDTAVlqTWLDLPFadva 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  298 HERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYL 377
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  378 TNVDDITLV-PGTLGRIRSKFSN-------NAKYDPKAIIANLTC--KKPDQHFKPYLKQHLPKRLHYanNRRIEDIHLL 447
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPKARElghvppgEVEEVYAELKEKLLGlrIQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
                         330       340       350
                  ....*....|....*....|....*....|.
gi 195947389  448 VERRWHVARKpldvyKKPSGKCFFQGDHGFD 478
Cdd:pfam01663 318 ADPGWYITGK-----DGGDKEAAIHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
164-518 1.08e-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: 298.34  E-value: 1.08e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 164 PPLIIFSVDGFRASYMKKGsKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFH 243
Cdd:cd16018    1 PPLIVISIDGFRWDYLDRA-GLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 244 lRGREKFNHRWWGGQPLWITATKQGVKAGTFFW--SVV----------------------IPHERRILTILQWLTLpdhE 299
Cdd:cd16018   80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWpgSEVaiigynptpiplggywqpyndsFPFEERVDTILEWLDL---E 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 300 RPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVtcdrteflsnyltn 379
Cdd:cd16018  156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV-------------- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 380 vdditlvpgtlgrirskfsnnakydpkaiianltckkpdqhfkpylkqhlpkrlhyannrriedihllverrwhvarkpl 459
Cdd:cd16018      --------------------------------------------------------------------------------
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 195947389 460 dvykkpsgkcffqGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLG 518
Cdd:cd16018  222 -------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
NUC smart00477
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
640-870 4.50e-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: 4.50e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   640 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKqMSYGFLFPPYL-SSSPEAK 718
Cdd:smart00477   1 RNQYVLGYNRSTRMPNWVAYHITGELLTSG-AERKSDCFKPDTRIPEKFQAKLSDYKGSG-YDRGHLAPAADhKFSSEAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   719 YDAFLVTNMVPMYPAFKRV-WNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDkIKQYVEGS-SIPVPTHYYSI 796
Cdd:smart00477  79 ADTFYLSNIVPQYPDFNRGaWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLE-VKYQVIGSkNVAIPTHFFKV 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195947389   797 ITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCnssedeskwveelMKMHTARVRDIEHLTSLDFFRKTSRS 870
Cdd:smart00477 158 ITAEKA--------DSYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
NUC cd00091
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ...
622-880 5.22e-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: 223.40  E-value: 5.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 622 LLYGRPAVLYRTryDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVpDHLTSCVRPDVRVSPSFSQNCLAYKNDKQM 701
Cdd:cd00091    1 LQYGRPGVLADT--EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNV-DRKYDQFKQDPRIPPLFSATNSDYKGSGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 702 SYGFLFPPYLSS-SPEAKYDAFLVTNMVPMYPAF-KRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGlHDTEDKIK 779
Cdd:cd00091   78 DRGHLAPAADPVwSQDAQDATFYLTNMAPQVQGFnQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDG-DGGSYLST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 780 QYVEGSSIPVPTHYYSIITSCLDftqpadkcDGPLSVSSFILPHRPDNEESCNSSedeskWVEELMKMHtarVRDIEHLT 859
Cdd:cd00091  157 QVINNGKVAVPTHFWKVIIDEKA--------PGNLSVGAFVLPNNNPHDTLEFIL-----CVEKTFQVP---VASVEKAT 220
                        250       260
                 ....*....|....*....|.
gi 195947389 860 SLDFFRKTSRSYPEILTLKTY 880
Cdd:cd00091  221 GLSFFCNVPDSVSAVLELKKK 241
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
154-520 3.72e-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: 3.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 154 AAECPAGFVRPPLIIFSVDGFRASYMKKGSkvMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSM 233
Cdd:COG1524   14 AAAAAAAPPAKKVVLILVDGLRADLLERAH--APNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 234 YDPVFDAT-FHLRGREKFNH--RWWGGQPLWITATKQGVKAGTFFWSV---------VIPH------------ERRILTI 289
Cdd:COG1524   92 YDPELGRVvNSLSWVEDGFGsnSLLPVPTIFERARAAGLTTAAVFWPSfegsglidaARPYpydgrkpllgnpAADRWIA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 290 LQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTcdr 369
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVP--- 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 370 TEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAkydpkAIIANLtckkpDQHFKPYLKQHLpKRLHYANNrRIEDIHLLVE 449
Cdd:COG1524  249 PDIDLNRLRLAGLLAVRAGESAHLYLKDGADA-----EVRALL-----GLPARVLTREEL-AAGHFGPH-RIGDLVLVAK 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195947389 450 RRWHVARKPLdvykkpsgkcffqGDHGFDNKvNSMQTVFVGYGSTFKyktkvPPFENIELYNVMCDLLGLK 520
Cdd:COG1524  317 PGWALDAPLK-------------GSHGGLPD-EEMRVPLLASGPGFR-----PGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
164-387 5.31e-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: 5.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 164 PPLIIFSVDGFRASYMKKGSKVM---PNIEKLRSCGTHSpYMRPVYP-TKTFPNLYTLATGLYPESHGIVGNSMYDPvfd 239
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPApttPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADP--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 240 atfhlRGREKFNHRWWGGQPLWITATKQGVKAGTFFwsvvipherrILTILQWLTLpdhERPSVYAFYSEQPDFSGHKYG 319
Cdd:cd00016   77 -----ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG----------LLKAIDETSK---EKPFVLFLHFDGPDGPGHAYG 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195947389 320 PFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVP 387
Cdd:cd00016  139 PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVP 206
Endonuclease_NS smart00892
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ...
640-869 1.32e-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: 1.32e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   640 HTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLS-SSPEAK 718
Cdd:smart00892   1 YKHYALCYDERRRLPLWVAYHLTGSTRQGKNTGRKRPWFKPDGWHLPAIFQAVNSDYTGSGYDRGHLAPAADHgVSQEAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389   719 YDAFLVTNMVPMYPAFKR-VWNYFQRVLVKKYASERNGVNVISGPIFDYDYDglhdtedkikqyveGSSIPVPTHYYSII 797
Cdd:smart00892  81 AATFYLTNIVPQTAGFNQgNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLP--------------DNNVAVPSHFWKVI 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195947389   798 TSCldftqpaDKCDGPLSVSSFILPHRPDNEescnssedeskwvEELMKMHTARVRDIEHLTSLDFFRKTSR 869
Cdd:smart00892 147 LSE-------DGSNGGLAAIAFNLPNAPINE-------------DYPLCEFQVPVDNIERLTGLDFFCGLPD 198
NUC1 COG1864
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
619-864 1.13e-17

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


Pssm-ID: 441469  Cd Length: 238  Bit Score: 83.42  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 619 ERHLLYGRPAV---LYRTRYdILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDhlTSCVRPDVRVSPSFSqnclA- 694
Cdd:COG1864    7 PDFLLLGLPSLaraLSTNNY-LLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKR--SDDFRPDPRLPSGYR----At 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 695 ---YKN---DKqmsyGFLFPPY-LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRVlVKKYASERNGVNVISGPIFDy 766
Cdd:COG1864   80 ladYTGsgyDR----GHLAPSAdRTFSKEANSETFLMTNISPQAPDFNQgIWARLENY-VRDLARKGGEVYVVTGPVFD- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 767 dydglhdtEDKIKQYVEGsSIPVPTHYYSIItscLDftqpADKCDGPLSVSSFILPHRPdneescNSSEDESKWVeelmk 846
Cdd:COG1864  154 --------DGDLKTIGSG-GVAVPTAFWKVV---VD----PDKNTGTLRAIAFLLPNTA------LSSGPLRTYQ----- 206
                        250
                 ....*....|....*...
gi 195947389 847 mhTArVRDIEHLTSLDFF 864
Cdd:COG1864  207 --VS-VDEIEKLTGLDFF 221
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
55-98 2.83e-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: 2.83e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 195947389    55 ISGSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKTA 98
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA-CRCDALCLSYGDCCTDYESVCKKEV 43
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
99-142 2.17e-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: 2.17e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 195947389    99 RGWECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGES 142
Cdd:smart00201   1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
Somatomedin_B pfam01033
Somatomedin B domain;
101-141 1.26e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 60.01  E-value: 1.26e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 195947389  101 WECtKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGE 141
Cdd:pfam01033   1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
Endonuclease_NS pfam01223
DNA/RNA non-specific endonuclease;
636-870 1.64e-11

DNA/RNA non-specific endonuclease;


Pssm-ID: 460120  Cd Length: 220  Bit Score: 64.76  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  636 DILYHTDFESGYSEIFLMPLWTSYTVSKQAevssvPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGF----LFPPY- 710
Cdd:pfam01223  17 VVLFYKYYSLCYDRRTRRALWVAHHLTGAS-----LAGSKGRRRPGFKQDPRIPGAYFRTLYTDYTGSGFdrghLAPAAd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  711 LSSSPEAKYDAFLVTNMVPMYPAFKR-VWNYFQRvLVKKYASERNG-VNVISGPIFDYDYDGLHdtedkikqyvegsSIP 788
Cdd:pfam01223  92 FKFSAGANAATFNFTNIAPQWAGFNQgNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLDKN-------------KVA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389  789 VPTHYYSIITScldftqPADKCDGPLSVSSFILPhrpdnEESCNSSEDESKWVEElmkmhtarVRDIEHLTSLDFFRKTS 868
Cdd:pfam01223 158 VPTHFWKVILS------EDGDGGGGLNAPAFVLP-----NKYILDDGPLRTFQVP--------VDELERLTGLDFCCGVP 218

                  ..
gi 195947389  869 RS 870
Cdd:pfam01223 219 DA 220
Somatomedin_B pfam01033
Somatomedin B domain;
57-97 9.68e-11

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 57.31  E-value: 9.68e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 195947389   57 GSCKGRCFELQEAGPPdCRCDNLCKSYTSCCHDFDELCLKT 97
Cdd:pfam01033   1 ESCKGRCGESFDRGRL-CQCDDDCVKYGDCCPDYESLCLGE 40
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
315-364 1.43e-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: 1.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 195947389 315 GHKYGPFGPEMTNPLREIDKIVGQLMDglkqlKLHRCVNVIFVGDHGMED 364
Cdd:cd16023  174 GHRYGPNHPEMARKLTQMDQFIRDIIE-----RLDDDTLLLVFGDHGMTE 218
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
315-364 4.84e-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: 4.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 195947389 315 GHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMED 364
Cdd:cd16024  159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMTD 208
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
163-236 4.86e-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: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195947389 163 RPPLIIF-SVDGFRASYM--------KKGSK-------VMPNieklrscgTHSPYMrpvyPTKTFPNLYTLATGLYPESH 226
Cdd:cd16016    1 RPKLVVGiVVDQMRADYLyryrdrfgEGGFKrllnegfVFEN--------AHYNYA----PTDTAPGHATIYTGTTPAIH 68
                         90
                 ....*....|
gi 195947389 227 GIVGNSMYDP 236
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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