|
Name |
Accession |
Description |
Interval |
E-value |
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
194-520 |
2.05e-112 |
|
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: 348.26 E-value: 2.05e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663 1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 274 SKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663 80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 424 GDVNNVKVV-YGPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
|
330 340
....*....|....*....|....*.
gi 817477963 496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
192-560 |
1.93e-109 |
|
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: 337.63 E-value: 1.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 192 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 271
Cdd:cd16018 1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 272 lKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPD------IYKVYNGSVPFEERILAVLEWLQLpshE 345
Cdd:cd16018 80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 346 RPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgd 425
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 426 vnnvkvvygpaarlrpTDVpetyysfnyealaknlscrepnqhfrpylkpflpkrlhfaksdriepltfyldpqwqlaln 505
Cdd:cd16018 219 ----------------TDV------------------------------------------------------------- 221
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 817477963 506 pserkycgsGFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLG 560
Cdd:cd16018 222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
|
|
| NUC |
smart00477 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
657-888 |
6.88e-80 |
|
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: 257.29 E-value: 6.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 657 QQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 735
Cdd:smart00477 1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 736 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 814
Cdd:smart00477 80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817477963 815 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 888
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
|
|
| NUC |
cd00091 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
639-898 |
1.14e-68 |
|
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: 228.41 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 639 PYGRPRILLKQhrvCLLQQQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKSNSKLS 717
Cdd:cd00091 2 QYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNvDRKYDQFKQDPRIPPLFSATNSDYKGSGSLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 718 YGFLTPPRLNRVSNHIYSEALLTSNIVPMYQ-SFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSleilKQ 796
Cdd:cd00091 79 RGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 797 NSRVIRSQEILIPTHFFIVLTSCKQLSEtplecsaLESSAYILPHRPDNIESCthgkrESSWVEELLTLHRARVTDvelI 876
Cdd:cd00091 155 STQVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---A 219
|
250 260
....*....|....*....|..
gi 817477963 877 TGLSFYQDRQESVSELLRLKTH 898
Cdd:cd00091 220 TGLSFFCNVPDSVSAVLELKKK 241
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
192-561 |
1.31e-66 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 227.32 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 192 PPTLLFSLDGFRAEYLHTwgGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP---KMNA 268
Cdd:COG1524 24 KKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPelgRVVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 269 SFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVE--IDGILPdiyKVYNGSVPF----EERILAVLEWLQLP 342
Cdd:COG1524 102 SLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAAAALELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 343 SHERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKy 422
Cdd:COG1524 179 REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 423 LGDVNNVKVVYGPAARLRPTDVpetyysfNYEALAKNLscrepNQHFRPYLKPFLpKRLHFAkSDRIEPLTFYLDPQWql 502
Cdd:COG1524 256 LRLAGLLAVRAGESAHLYLKDG-------ADAEVRALL-----GLPARVLTREEL-AAGHFG-PHRIGDLVLVAKPGW-- 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 817477963 503 alnPSERKYCGSgfHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 561
Cdd:COG1524 320 ---ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
|
|
| NUC1 |
COG1864 |
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism]; |
654-898 |
3.95e-13 |
|
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
Pssm-ID: 441469 Cd Length: 238 Bit Score: 69.93 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 654 LLQQQQFLTGYSLDLLMPLWASY----TFLSNDQFSRDDFsnclYQDLRIPLS-PVHKCSYykSNSKLSYGFLTP---PR 725
Cdd:COG1864 27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGyRATLADY--TGSGYDRGHLAPsadRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 726 LNRVSNhiySEALLTSNIVPMYQSF-QVIWHYLHDTLLQrYAHERNGINVVSGPVFDfdydgrydsleilKQNSRVIRSQ 804
Cdd:COG1864 101 FSKEAN---SETFLMTNISPQAPDFnQGIWARLENYVRD-LARKGGEVYVVTGPVFD-------------DGDLKTIGSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 805 EILIPTHFF-IVLTsckqlseTPLECSALESSAYILPHRPDniescthgkRESSWVEELLTlhrarVTDVELITGLSFYQ 883
Cdd:COG1864 164 GVAVPTAFWkVVVD-------PDKNTGTLRAIAFLLPNTAL---------SSGPLRTYQVS-----VDEIEKLTGLDFFP 222
|
250
....*....|....*
gi 817477963 884 DRQESVSELLRLKTH 898
Cdd:COG1864 223 NLPDDLEAALEAKVD 237
|
|
| Somatomedin_B |
pfam01033 |
Somatomedin B domain; |
129-169 |
1.37e-11 |
|
Somatomedin B domain;
Pssm-ID: 460034 Cd Length: 40 Bit Score: 59.62 E-value: 1.37e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 817477963 129 WTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDK 169
Cdd:pfam01033 1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
|
|
| SO |
smart00201 |
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ... |
86-126 |
1.48e-11 |
|
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: 59.69 E-value: 1.48e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 817477963 86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201 1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
|
|
| SO |
smart00201 |
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ... |
127-170 |
1.14e-10 |
|
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: 57.38 E-value: 1.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 817477963 127 HIWTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKK 170
Cdd:smart00201 1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
|
|
| Somatomedin_B |
pfam01033 |
Somatomedin B domain; |
89-125 |
2.87e-10 |
|
Somatomedin B domain;
Pssm-ID: 460034 Cd Length: 40 Bit Score: 56.16 E-value: 2.87e-10
10 20 30
....*....|....*....|....*....|....*....
gi 817477963 89 SCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEP 125
Cdd:pfam01033 2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
|
|
| Endonuclease_NS |
pfam01223 |
DNA/RNA non-specific endonuclease; |
656-881 |
3.71e-08 |
|
DNA/RNA non-specific endonuclease;
Pssm-ID: 460120 Cd Length: 220 Bit Score: 54.75 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 656 QQQQFLTGYSL----DLLMPLWASY-----TFLSNDQFSRDDFsnclYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPrl 726
Cdd:pfam01223 16 DVVLFYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPA-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 727 nrvSNHIYSEA--LLT---SNIVPMYQSF-QVIWHYLHDtLLQRYAHERNG-INVVSGPVFDFDYDGrydsleilkqnsr 799
Cdd:pfam01223 90 ---ADFKFSAGanAATfnfTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 800 virSQEILIPTHFFIVLtsckqLSETPLECSALESSAYILPHRPdniescthGKRESSWVEELLTlhrarVTDVELITGL 879
Cdd:pfam01223 153 ---KNKVAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPNKY--------ILDDGPLRTFQVP-----VDELERLTGL 211
|
..
gi 817477963 880 SF 881
Cdd:pfam01223 212 DF 213
|
|
| PTZ00259 |
PTZ00259 |
endonuclease G; Provisional |
598-884 |
2.70e-06 |
|
endonuclease G; Provisional
Pssm-ID: 240335 [Multi-domain] Cd Length: 434 Bit Score: 51.02 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 598 IKSTSNDLGCTCDPWIVPIKDFEkQLNLTTEDVDDIYHMTVPYGRP---RILLKQHrvcllqqqqFLTGYSLDLLMPLWA 674
Cdd:PTZ00259 62 VKSVVSGNALKKVTELPPPYPSE-QASTARADTLPFCKEYPSFGLPsteNLRLYEG---------YVSSLNYERRIPNWV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 675 ----SYTFLSNDQFSRD-DFSNC-LYQDLRIPLSPVHKCSYYKSnSKLSYGFLTPPRLNRVSNHIYSEA-LLTSNIVPmy 747
Cdd:PTZ00259 132 aeyiPYRGISVEAGEKKaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP-- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 748 QSF---QVIWHYLHD-TLLQRYAHErNGINVVSGPVFDFDYDGRYDSLEILKQNSR-------------------VIRSQ 804
Cdd:PTZ00259 209 QDLtnnAGDWLRLENlTRKLAREYE-VGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 805 EILIPTHFFIVLtsckqLSETPLECSAlESSAYILPHRPdnIEScthgkresswvEELLTLHRARVTDVELITGLSFYQD 884
Cdd:PTZ00259 288 NVAVPTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
194-520 |
2.05e-112 |
|
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: 348.26 E-value: 2.05e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 194 TLLFSLDGFRAEYLHTWGgLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLK 273
Cdd:pfam01663 1 LLVISLDGFRADYLDRFE-LTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 274 SKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEID---GILPDIYK-VYNGSVPFEERILAVL--EWLQLPS---- 343
Cdd:pfam01663 80 ISDPEDPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYStyyGTPPRYLKdDYNNSVPFEDRVDTAVlqTWLDLPFadva 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYL 423
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 424 GDVNNVKVV-YGPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFY 495
Cdd:pfam01663 240 REKGLLHLVdGGPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLV 317
|
330 340
....*....|....*....|....*.
gi 817477963 496 LDPQWQLALNPSERKYC-GSGFHGSD 520
Cdd:pfam01663 318 ADPGWYITGKDGGDKEAaIHGTHGYD 343
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
192-560 |
1.93e-109 |
|
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: 337.63 E-value: 1.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 192 PPTLLFSLDGFRAEYLhTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFS 271
Cdd:cd16018 1 PPLIVISIDGFRWDYL-DRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 272 lKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPD------IYKVYNGSVPFEERILAVLEWLQLpshE 345
Cdd:cd16018 80 -DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDL---E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 346 RPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgd 425
Cdd:cd16018 156 RPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM----------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 426 vnnvkvvygpaarlrpTDVpetyysfnyealaknlscrepnqhfrpylkpflpkrlhfaksdriepltfyldpqwqlaln 505
Cdd:cd16018 219 ----------------TDV------------------------------------------------------------- 221
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 817477963 506 pserkycgsGFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLG 560
Cdd:cd16018 222 ---------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
|
|
| NUC |
smart00477 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
657-888 |
6.88e-80 |
|
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: 257.29 E-value: 6.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 657 QQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 735
Cdd:smart00477 1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 736 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 814
Cdd:smart00477 80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817477963 815 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 888
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
|
|
| NUC |
cd00091 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
639-898 |
1.14e-68 |
|
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: 228.41 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 639 PYGRPRILLKQhrvCLLQQQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKSNSKLS 717
Cdd:cd00091 2 QYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNvDRKYDQFKQDPRIPPLFSATNSDYKGSGSLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 718 YGFLTPPRLNRVSNHIYSEALLTSNIVPMYQ-SFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSleilKQ 796
Cdd:cd00091 79 RGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 797 NSRVIRSQEILIPTHFFIVLTSCKQLSEtplecsaLESSAYILPHRPDNIESCthgkrESSWVEELLTLHRARVTDvelI 876
Cdd:cd00091 155 STQVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---A 219
|
250 260
....*....|....*....|..
gi 817477963 877 TGLSFYQDRQESVSELLRLKTH 898
Cdd:cd00091 220 TGLSFFCNVPDSVSAVLELKKK 241
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
192-561 |
1.31e-66 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 227.32 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 192 PPTLLFSLDGFRAEYLHTwgGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDP---KMNA 268
Cdd:COG1524 24 KKVVLILVDGLRADLLER--AHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPelgRVVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 269 SFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVE--IDGILPdiyKVYNGSVPF----EERILAVLEWLQLP 342
Cdd:COG1524 102 SLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSFEGSglIDAARP---YPYDGRKPLlgnpAADRWIAAAALELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 343 SHERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKy 422
Cdd:COG1524 179 REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 423 LGDVNNVKVVYGPAARLRPTDVpetyysfNYEALAKNLscrepNQHFRPYLKPFLpKRLHFAkSDRIEPLTFYLDPQWql 502
Cdd:COG1524 256 LRLAGLLAVRAGESAHLYLKDG-------ADAEVRALL-----GLPARVLTREEL-AAGHFG-PHRIGDLVLVAKPGW-- 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 817477963 503 alnPSERKYCGSgfHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 561
Cdd:COG1524 320 ---ALDAPLKGS--HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
192-447 |
1.25e-26 |
|
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: 109.43 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 192 PPTLLFSLDGFRAEYLHTWGG---LLPVISKLKNCGTYTkNMRPMYP-TKTFPNHYSIVTGLYPESHGIIDNKMYDPKMN 267
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNpapTTPNLKRLASEGATF-NFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 268 asfslkskEKFNPLWYKGQPIWVTANHQEVKSGTYFwpgsdveidgilpdiykvyngsvpfeerILAVLEWLQLpshERP 347
Cdd:cd00016 80 --------SRAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------LLKAIDETSK---EKP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 348 HFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSC----KKYVYLNKYL 423
Cdd:cd00016 121 FVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHggdpKADGKADKSH 200
|
250 260
....*....|....*....|....
gi 817477963 424 GDVNNVKVVYGPAARLRPTDVPET 447
Cdd:cd00016 201 TGMRVPFIAYGPGVKKGGVKHELI 224
|
|
| Endonuclease_NS |
smart00892 |
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ... |
659-884 |
9.95e-25 |
|
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: 102.49 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 659 QFLTGYSLDLLMPLWASYTFL--SNDQFSRDDFSNCLYQD-LRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 735
Cdd:smart00892 3 HYALCYDERRRLPLWVAYHLTgsTRQGKNTGRKRPWFKPDgWHLPAIFQAVNSDYT-GSGYDRGHLAPAADHGVSQEAMA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 736 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRydsleilkqnsrvirsqEILIPTHFFI 814
Cdd:smart00892 82 ATFYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPDN-----------------NVAVPSHFWK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 815 VLTSCKQLSEtplecsALESSAYILPHRPDNiescthgkresswVEELLTLHRARVTDVELITGLSFYQD 884
Cdd:smart00892 145 VILSEDGSNG------GLAAIAFNLPNAPIN-------------EDYPLCEFQVPVDNIERLTGLDFFCG 195
|
|
| NUC1 |
COG1864 |
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism]; |
654-898 |
3.95e-13 |
|
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
Pssm-ID: 441469 Cd Length: 238 Bit Score: 69.93 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 654 LLQQQQFLTGYSLDLLMPLWASY----TFLSNDQFSRDDFsnclYQDLRIPLS-PVHKCSYykSNSKLSYGFLTP---PR 725
Cdd:COG1864 27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGyRATLADY--TGSGYDRGHLAPsadRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 726 LNRVSNhiySEALLTSNIVPMYQSF-QVIWHYLHDTLLQrYAHERNGINVVSGPVFDfdydgrydsleilKQNSRVIRSQ 804
Cdd:COG1864 101 FSKEAN---SETFLMTNISPQAPDFnQGIWARLENYVRD-LARKGGEVYVVTGPVFD-------------DGDLKTIGSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 805 EILIPTHFF-IVLTsckqlseTPLECSALESSAYILPHRPDniescthgkRESSWVEELLTlhrarVTDVELITGLSFYQ 883
Cdd:COG1864 164 GVAVPTAFWkVVVD-------PDKNTGTLRAIAFLLPNTAL---------SSGPLRTYQVS-----VDEIEKLTGLDFFP 222
|
250
....*....|....*
gi 817477963 884 DRQESVSELLRLKTH 898
Cdd:COG1864 223 NLPDDLEAALEAKVD 237
|
|
| Somatomedin_B |
pfam01033 |
Somatomedin B domain; |
129-169 |
1.37e-11 |
|
Somatomedin B domain;
Pssm-ID: 460034 Cd Length: 40 Bit Score: 59.62 E-value: 1.37e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 817477963 129 WTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDK 169
Cdd:pfam01033 1 ESC-KGRCGESFDRGRLCQCDDDCVKYGDCCPDYESLCLGE 40
|
|
| SO |
smart00201 |
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ... |
86-126 |
1.48e-11 |
|
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: 59.69 E-value: 1.48e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 817477963 86 EVKSCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEPT 126
Cdd:smart00201 1 AIGSCKGRCGESFNEGnaCRCDALCLSYGDCCTDYESVCKKEV 43
|
|
| SO |
smart00201 |
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ... |
127-170 |
1.14e-10 |
|
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: 57.38 E-value: 1.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 817477963 127 HIWTCnKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKK 170
Cdd:smart00201 1 AIGSC-KGRCGESFNEGNACRCDALCLSYGDCCTDYESVCKKEV 43
|
|
| Somatomedin_B |
pfam01033 |
Somatomedin B domain; |
89-125 |
2.87e-10 |
|
Somatomedin B domain;
Pssm-ID: 460034 Cd Length: 40 Bit Score: 56.16 E-value: 2.87e-10
10 20 30
....*....|....*....|....*....|....*....
gi 817477963 89 SCKGRCFERTFSN--CRCDAACVSLGNCCLDFQETCVEP 125
Cdd:pfam01033 2 SCKGRCGESFDRGrlCQCDDDCVKYGDCCPDYESLCLGE 40
|
|
| Endonuclease_NS |
pfam01223 |
DNA/RNA non-specific endonuclease; |
656-881 |
3.71e-08 |
|
DNA/RNA non-specific endonuclease;
Pssm-ID: 460120 Cd Length: 220 Bit Score: 54.75 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 656 QQQQFLTGYSL----DLLMPLWASY-----TFLSNDQFSRDDFsnclYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPrl 726
Cdd:pfam01223 16 DVVLFYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPA-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 727 nrvSNHIYSEA--LLT---SNIVPMYQSF-QVIWHYLHDtLLQRYAHERNG-INVVSGPVFDFDYDGrydsleilkqnsr 799
Cdd:pfam01223 90 ---ADFKFSAGanAATfnfTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 800 virSQEILIPTHFFIVLtsckqLSETPLECSALESSAYILPHRPdniescthGKRESSWVEELLTlhrarVTDVELITGL 879
Cdd:pfam01223 153 ---KNKVAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPNKY--------ILDDGPLRTFQVP-----VDELERLTGL 211
|
..
gi 817477963 880 SF 881
Cdd:pfam01223 212 DF 213
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
192-411 |
3.88e-08 |
|
uncharacterized sulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 55.63 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 192 PPTLLFSLDGFRAEYLHTWGGLL---PVISKL-------KNCgtYTKNMRpmyptkTFPNHYSIVTGLYPESHGIIDNKM 261
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRvttPNLDRLaaegvvfDNH--YSGSNP------TLPSRFSLFTGLYPFYHGVWGGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 262 ydpkmnasfslkskEKFNPLWY-----KGqpiWVTA---NHQEVKSGTYFWPGSDVEIDGILPDIYKVYNGSVPFEERIL 333
Cdd:cd16148 73 --------------EPDDPTLAeilrkAG---YYTAavsSNPHLFGGPGFDRGFDTFEDFRGQEGDPGEEGDERAERVTD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 334 AVLEWLQLPSHERPHFYTLYLEEPdssghsHGP------VSsevikalqKVDRLVGMLMDGLKDLGL-DKCLnLILISDH 406
Cdd:cd16148 136 RALEWLDRNADDDPFFLFLHYFDP------HEPylydaeVR--------YVDEQIGRLLDKLKELGLlEDTL-VIVTSDH 200
|
....*
gi 817477963 407 GMEQG 411
Cdd:cd16148 201 GEEFG 205
|
|
| PTZ00259 |
PTZ00259 |
endonuclease G; Provisional |
598-884 |
2.70e-06 |
|
endonuclease G; Provisional
Pssm-ID: 240335 [Multi-domain] Cd Length: 434 Bit Score: 51.02 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 598 IKSTSNDLGCTCDPWIVPIKDFEkQLNLTTEDVDDIYHMTVPYGRP---RILLKQHrvcllqqqqFLTGYSLDLLMPLWA 674
Cdd:PTZ00259 62 VKSVVSGNALKKVTELPPPYPSE-QASTARADTLPFCKEYPSFGLPsteNLRLYEG---------YVSSLNYERRIPNWV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 675 ----SYTFLSNDQFSRD-DFSNC-LYQDLRIPLSPVHKCSYYKSnSKLSYGFLTPPRLNRVSNHIYSEA-LLTSNIVPmy 747
Cdd:PTZ00259 132 aeyiPYRGISVEAGEKKaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP-- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 748 QSF---QVIWHYLHD-TLLQRYAHErNGINVVSGPVFDFDYDGRYDSLEILKQNSR-------------------VIRSQ 804
Cdd:PTZ00259 209 QDLtnnAGDWLRLENlTRKLAREYE-VGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 805 EILIPTHFFIVLtsckqLSETPLECSAlESSAYILPHRPdnIEScthgkresswvEELLTLHRARVTDVELITGLSFYQD 884
Cdd:PTZ00259 288 NVAVPTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
200-265 |
3.78e-05 |
|
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: 47.14 E-value: 3.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817477963 200 DGFRAEYLH------TWGGLLpvisKLKNCGTYTKNMR-PMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPK 265
Cdd:cd16016 11 DQMRADYLYryrdrfGEGGFK----RLLNEGFVFENAHyNYAPTDTAPGHATIYTGTTPAIHGIIGNDWYDRE 79
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
344-412 |
3.29e-04 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; 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: 293744 Cd Length: 294 Bit Score: 43.73 E-value: 3.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817477963 344 HERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGM-EQGS 412
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMtDWGS 223
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| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
378-411 |
6.88e-03 |
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Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 39.86 E-value: 6.88e-03
10 20 30
....*....|....*....|....*....|....*.
gi 817477963 378 VDRLVGMLMDGLKDLGLDKclNLILI--SDHGMEQG 411
Cdd:COG3119 209 VDDQVGRLLDALEELGLAD--NTIVVftSDNGPSLG 242
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| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
378-407 |
9.49e-03 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 39.48 E-value: 9.49e-03
10 20 30
....*....|....*....|....*....|..
gi 817477963 378 VDRLVGMLMDGLKDLGLDKclNLI--LISDHG 407
Cdd:cd16030 270 VDAQVGRVLDALEELGLAD--NTIvvLWSDHG 299
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