|
Name |
Accession |
Description |
Interval |
E-value |
| NUC |
smart00477 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
304-535 |
1.38e-81 |
|
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: 253.82 E-value: 1.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 304 QQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 382
Cdd:smart00477 1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 383 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 461
Cdd:smart00477 80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817478029 462 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 535
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
|
|
| NUC |
cd00091 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
286-545 |
2.38e-70 |
|
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: 225.71 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 286 PYGRPRILLKQhrvCLLQQQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKSNSKLS 364
Cdd:cd00091 2 QYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNvDRKYDQFKQDPRIPPLFSATNSDYKGSGSLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 365 YGFLTPPRLNRVSNHIYSEALLTSNIVPMYQ-SFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSleilKQ 443
Cdd:cd00091 79 RGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 444 NSRVIRSQEILIPTHFFIVLTSCKQLSEtplecsaLESSAYILPHRPDNIESCthgkrESSWVEELLTLHRARVTDvelI 523
Cdd:cd00091 155 STQVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---A 219
|
250 260
....*....|....*....|..
gi 817478029 524 TGLSFYQDRQESVSELLRLKTH 545
Cdd:cd00091 220 TGLSFFCNVPDSVSAVLELKKK 241
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
3-168 |
8.20e-41 |
|
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: 150.65 E-value: 8.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 3 EEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYLGDVNNVKVV-Y 81
Cdd:pfam01663 171 EEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYLREKGLLHLVdG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 82 GPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFYLDPQWQLALNP 154
Cdd:pfam01663 251 GPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGKD 328
|
170
....*....|....*
gi 817478029 155 SERKYC-GSGFHGSD 168
Cdd:pfam01663 329 GGDKEAaIHGTHGYD 343
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
3-208 |
1.01e-28 |
|
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: 114.99 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 3 EEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgdvnnvkvvyg 82
Cdd:cd16018 165 EEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM-------------------------- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 83 paarlrpTDVpetyysfnyealaknlscrepnqhfrpylkpflpkrlhfaksdriepltfyldpqwqlalnpserkycgs 162
Cdd:cd16018 219 -------TDV---------------------------------------------------------------------- 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 817478029 163 GFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLG 208
Cdd:cd16018 222 GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
4-209 |
9.75e-23 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 99.82 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 4 EPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKyLGDVNNVKVVYGP 83
Cdd:COG1524 192 DLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR-LRLAGLLAVRAGE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 84 AARLRPTDVpetyysfNYEALAKNLscrepNQHFRPYLKPFLpKRLHFAkSDRIEPLTFYLDPQWqlalnPSERKYCGSg 163
Cdd:COG1524 269 SAHLYLKDG-------ADAEVRALL-----GLPARVLTREEL-AAGHFG-PHRIGDLVLVAKPGW-----ALDAPLKGS- 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 817478029 164 fHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 209
Cdd:COG1524 329 -HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
|
|
| NUC1 |
COG1864 |
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism]; |
301-545 |
2.09e-13 |
|
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
Pssm-ID: 441469 Cd Length: 238 Bit Score: 69.93 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 301 LLQQQQFLTGYSLDLLMPLWASY----TFLSNDQFSRDDFsnclYQDLRIPLS-PVHKCSYykSNSKLSYGFLTP---PR 372
Cdd:COG1864 27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGyRATLADY--TGSGYDRGHLAPsadRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 373 LNRVSNhiySEALLTSNIVPMYQSF-QVIWHYLHDTLLQrYAHERNGINVVSGPVFDfdydgrydsleilKQNSRVIRSQ 451
Cdd:COG1864 101 FSKEAN---SETFLMTNISPQAPDFnQGIWARLENYVRD-LARKGGEVYVVTGPVFD-------------DGDLKTIGSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 452 EILIPTHFF-IVLTsckqlseTPLECSALESSAYILPHRPDniescthgkRESSWVEELLTlhrarVTDVELITGLSFYQ 530
Cdd:COG1864 164 GVAVPTAFWkVVVD-------PDKNTGTLRAIAFLLPNTAL---------SSGPLRTYQVS-----VDEIEKLTGLDFFP 222
|
250
....*....|....*
gi 817478029 531 DRQESVSELLRLKTH 545
Cdd:COG1864 223 NLPDDLEAALEAKVD 237
|
|
| Endonuclease_NS |
pfam01223 |
DNA/RNA non-specific endonuclease; |
303-528 |
2.01e-08 |
|
DNA/RNA non-specific endonuclease;
Pssm-ID: 460120 Cd Length: 220 Bit Score: 54.75 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 303 QQQQFLTGYSL----DLLMPLWASY-----TFLSNDQFSRDDFsnclYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPrl 373
Cdd:pfam01223 16 DVVLFYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPA-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 374 nrvSNHIYSEA--LLT---SNIVPMYQSF-QVIWHYLHDtLLQRYAHERNG-INVVSGPVFDFDYDGrydsleilkqnsr 446
Cdd:pfam01223 90 ---ADFKFSAGanAATfnfTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 447 virSQEILIPTHFFIVLtsckqLSETPLECSALESSAYILPHRPdniescthGKRESSWVEELLTlhrarVTDVELITGL 526
Cdd:pfam01223 153 ---KNKVAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPNKY--------ILDDGPLRTFQVP-----VDELERLTGL 211
|
..
gi 817478029 527 SF 528
Cdd:pfam01223 212 DF 213
|
|
| PTZ00259 |
PTZ00259 |
endonuclease G; Provisional |
246-531 |
9.89e-07 |
|
endonuclease G; Provisional
Pssm-ID: 240335 [Multi-domain] Cd Length: 434 Bit Score: 51.40 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 246 IKSTSNDLGCTCDPWIVPIKDFEKQLNLTTEDDDIYHMTVPYGRP---RILLKQHrvcllqqqqFLTGYSLDLLMPLWA- 321
Cdd:PTZ00259 62 VKSVVSGNALKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLPsteNLRLYEG---------YVSSLNYERRIPNWVa 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 322 ---SYTFLSNDQFSRD-DFSNC-LYQDLRIPLSPVHKCSYYKSnSKLSYGFLTPPRLNRVSNHIYSEA-LLTSNIVPmyQ 395
Cdd:PTZ00259 133 eyiPYRGISVEAGEKKaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP--Q 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 396 SF---QVIWHYLHD-TLLQRYAHErNGINVVSGPVFDFDYDGRYDSLEILKQNSR-------------------VIRSQE 452
Cdd:PTZ00259 210 DLtnnAGDWLRLENlTRKLAREYE-VGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDNN 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817478029 453 ILIPTHFFIVLtsckqLSETPLECSAlESSAYILPHRPdnIEScthgkresswvEELLTLHRARVTDVELITGLSFYQD 531
Cdd:PTZ00259 289 VAVPTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NUC |
smart00477 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
304-535 |
1.38e-81 |
|
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: 253.82 E-value: 1.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 304 QQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 382
Cdd:smart00477 1 RNQYVLGYNRSTRMPNWVAYHITGELLTSGaERKSDCFKPDTRIPEKFQAKLSDYK-GSGYDRGHLAPAADHKFSSEAMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 383 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQnsrVIRSQEILIPTHFFI 461
Cdd:smart00477 80 DTFYLSNIVPQYPDFnRGAWAYLEDYLRKLTASERNGVYVVSGPLFLPNYDGKGDKLEVKYQ---VIGSKNVAIPTHFFK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817478029 462 VLTSCKQLsetplecSALESSAYILPHRPDNIESCthgkresswveelLTLHRARVTDVELITGLSFYQDRQES 535
Cdd:smart00477 157 VITAEKAD-------SYLEVAAFILPNDPINDESP-------------LTNFRVPVDEIERLTGLDFFRNLDPA 210
|
|
| NUC |
cd00091 |
DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA ... |
286-545 |
2.38e-70 |
|
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: 225.71 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 286 PYGRPRILLKQhrvCLLQQQQFLTGYSLDLLMPLWASYTFLSNDQFSR-DDFSNCLYQDLRIPLSPVHKCSYYKSNSKLS 364
Cdd:cd00091 2 QYGRPGVLADT---EVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNvDRKYDQFKQDPRIPPLFSATNSDYKGSGSLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 365 YGFLTPPRLNRVSNHIYSEALLTSNIVPMYQ-SFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSleilKQ 443
Cdd:cd00091 79 RGHLAPAADPVWSQDAQDATFYLTNMAPQVQgFNQGNWAYLEDYLRDLAASEGKDVYVVTGPLFLPDLDGDGGS----YL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 444 NSRVIRSQEILIPTHFFIVLTSCKQLSEtplecsaLESSAYILPHRPDNIESCthgkrESSWVEELLTLHRARVTDvelI 523
Cdd:cd00091 155 STQVINNGKVAVPTHFWKVIIDEKAPGN-------LSVGAFVLPNNNPHDTLE-----FILCVEKTFQVPVASVEK---A 219
|
250 260
....*....|....*....|..
gi 817478029 524 TGLSFYQDRQESVSELLRLKTH 545
Cdd:cd00091 220 TGLSFFCNVPDSVSAVLELKKK 241
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
3-168 |
8.20e-41 |
|
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: 150.65 E-value: 8.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 3 EEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYLGDVNNVKVV-Y 81
Cdd:pfam01663 171 EEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYLREKGLLHLVdG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 82 GPAARLRP-----TDVPETYYSFNYEALAKNLSCR--EPNQHFRPYLKPFLPKRLHFakSDRIEPLTFYLDPQWQLALNP 154
Cdd:pfam01663 251 GPVVAIYPkarelGHVPPGEVEEVYAELKEKLLGLriQDGEHLAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGKD 328
|
170
....*....|....*
gi 817478029 155 SERKYC-GSGFHGSD 168
Cdd:pfam01663 329 GGDKEAaIHGTHGYD 343
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
3-208 |
1.01e-28 |
|
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: 114.99 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 3 EEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqgsckkyvylnkylgdvnnvkvvyg 82
Cdd:cd16018 165 EEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM-------------------------- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 83 paarlrpTDVpetyysfnyealaknlscrepnqhfrpylkpflpkrlhfaksdriepltfyldpqwqlalnpserkycgs 162
Cdd:cd16018 219 -------TDV---------------------------------------------------------------------- 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 817478029 163 GFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLG 208
Cdd:cd16018 222 GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
|
|
| Endonuclease_NS |
smart00892 |
DNA/RNA non-specific endonuclease; A family of bacterial and eukaryotic endonucleases share ... |
306-531 |
7.57e-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: 102.10 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 306 QFLTGYSLDLLMPLWASYTFL--SNDQFSRDDFSNCLYQD-LRIPLSPVHKCSYYKsNSKLSYGFLTPPRLNRVSNHIYS 382
Cdd:smart00892 3 HYALCYDERRRLPLWVAYHLTgsTRQGKNTGRKRPWFKPDgWHLPAIFQAVNSDYT-GSGYDRGHLAPAADHGVSQEAMA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 383 EALLTSNIVPMYQSF-QVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRydsleilkqnsrvirsqEILIPTHFFI 461
Cdd:smart00892 82 ATFYLTNIVPQTAGFnQGNWNRLENYVRKLLAKNKDTVYVVTGPIYLPTLPDN-----------------NVAVPSHFWK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 462 VLTSCKQLSEtplecsALESSAYILPHRPDNiescthgkresswVEELLTLHRARVTDVELITGLSFYQD 531
Cdd:smart00892 145 VILSEDGSNG------GLAAIAFNLPNAPIN-------------EDYPLCEFQVPVDNIERLTGLDFFCG 195
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
4-209 |
9.75e-23 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 99.82 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 4 EPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMeqGSCKKYVYLNKyLGDVNNVKVVYGP 83
Cdd:COG1524 192 DLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM--VDVPPDIDLNR-LRLAGLLAVRAGE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 84 AARLRPTDVpetyysfNYEALAKNLscrepNQHFRPYLKPFLpKRLHFAkSDRIEPLTFYLDPQWqlalnPSERKYCGSg 163
Cdd:COG1524 269 SAHLYLKDG-------ADAEVRALL-----GLPARVLTREEL-AAGHFG-PHRIGDLVLVAKPGW-----ALDAPLKGS- 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 817478029 164 fHGSDNlFSNMQALFIGYGPAFKHGaevdsFENIEVYNLMCDLLGL 209
Cdd:COG1524 329 -HGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
|
|
| NUC1 |
COG1864 |
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism]; |
301-545 |
2.09e-13 |
|
DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism];
Pssm-ID: 441469 Cd Length: 238 Bit Score: 69.93 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 301 LLQQQQFLTGYSLDLLMPLWASY----TFLSNDQFSRDDFsnclYQDLRIPLS-PVHKCSYykSNSKLSYGFLTP---PR 372
Cdd:COG1864 27 LLCYTGYSLSYNESRRTPNWVAYnldgSWLGKSLKRSDDF----RPDPRLPSGyRATLADY--TGSGYDRGHLAPsadRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 373 LNRVSNhiySEALLTSNIVPMYQSF-QVIWHYLHDTLLQrYAHERNGINVVSGPVFDfdydgrydsleilKQNSRVIRSQ 451
Cdd:COG1864 101 FSKEAN---SETFLMTNISPQAPDFnQGIWARLENYVRD-LARKGGEVYVVTGPVFD-------------DGDLKTIGSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 452 EILIPTHFF-IVLTsckqlseTPLECSALESSAYILPHRPDniescthgkRESSWVEELLTlhrarVTDVELITGLSFYQ 530
Cdd:COG1864 164 GVAVPTAFWkVVVD-------PDKNTGTLRAIAFLLPNTAL---------SSGPLRTYQVS-----VDEIEKLTGLDFFP 222
|
250
....*....|....*
gi 817478029 531 DRQESVSELLRLKTH 545
Cdd:COG1864 223 NLPDDLEAALEAKVD 237
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
4-95 |
1.48e-09 |
|
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: 58.59 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 4 EPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSC----KKYVYLNKYLGDVNNVKV 79
Cdd:cd00016 129 GPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHggdpKADGKADKSHTGMRVPFI 208
|
90
....*....|....*.
gi 817478029 80 VYGPAARLRPTDVPET 95
Cdd:cd00016 209 AYGPGVKKGGVKHELI 224
|
|
| Endonuclease_NS |
pfam01223 |
DNA/RNA non-specific endonuclease; |
303-528 |
2.01e-08 |
|
DNA/RNA non-specific endonuclease;
Pssm-ID: 460120 Cd Length: 220 Bit Score: 54.75 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 303 QQQQFLTGYSL----DLLMPLWASY-----TFLSNDQFSRDDFsnclYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPrl 373
Cdd:pfam01223 16 DVVLFYKYYSLcydrRTRRALWVAHhltgaSLAGSKGRRRPGF----KQDPRIPGAYFRTLYTDYTGSGFDRGHLAPA-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 374 nrvSNHIYSEA--LLT---SNIVPMYQSF-QVIWHYLHDtLLQRYAHERNG-INVVSGPVFDFDYDGrydsleilkqnsr 446
Cdd:pfam01223 90 ---ADFKFSAGanAATfnfTNIAPQWAGFnQGNWAYLEN-YVRDLAARHNNsVYVYTGPLYVPNLLD------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 447 virSQEILIPTHFFIVLtsckqLSETPLECSALESSAYILPHRPdniescthGKRESSWVEELLTlhrarVTDVELITGL 526
Cdd:pfam01223 153 ---KNKVAVPTHFWKVI-----LSEDGDGGGGLNAPAFVLPNKY--------ILDDGPLRTFQVP-----VDELERLTGL 211
|
..
gi 817478029 527 SF 528
Cdd:pfam01223 212 DF 213
|
|
| PTZ00259 |
PTZ00259 |
endonuclease G; Provisional |
246-531 |
9.89e-07 |
|
endonuclease G; Provisional
Pssm-ID: 240335 [Multi-domain] Cd Length: 434 Bit Score: 51.40 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 246 IKSTSNDLGCTCDPWIVPIKDFEKQLNLTTEDDDIYHMTVPYGRP---RILLKQHrvcllqqqqFLTGYSLDLLMPLWA- 321
Cdd:PTZ00259 62 VKSVVSGNALKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLPsteNLRLYEG---------YVSSLNYERRIPNWVa 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 322 ---SYTFLSNDQFSRD-DFSNC-LYQDLRIPLSPVHKCSYYKSnSKLSYGFLTPPRLNRVSNHIYSEA-LLTSNIVPmyQ 395
Cdd:PTZ00259 133 eyiPYRGISVEAGEKKaNRADCvFYADPTVPEAFRAENKDYTG-SGYSRGHLAAAGFHKASQTAMDDTfLLSANIVP--Q 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478029 396 SF---QVIWHYLHD-TLLQRYAHErNGINVVSGPVFDFDYDGRYDSLEILKQNSR-------------------VIRSQE 452
Cdd:PTZ00259 210 DLtnnAGDWLRLENlTRKLAREYE-VGVYVVSGPLFVPRYMREKLRKWRLAEPSEihkpdspadktpkkvvtyeVIGDNN 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817478029 453 ILIPTHFFIVLtsckqLSETPLECSAlESSAYILPHRPdnIEScthgkresswvEELLTLHRARVTDVELITGLSFYQD 531
Cdd:PTZ00259 289 VAVPTHLFKVI-----LAEKNDGPPH-EVAAFLMPNEP--ISK-----------EKPLTAYQVPLEEIEKLTGLQFFPK 348
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
6-60 |
1.21e-03 |
|
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: 41.04 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 817478029 6 DSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGM-EQGS 60
Cdd:cd16020 168 DTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMtDWGS 223
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
26-59 |
3.71e-03 |
|
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: 3.71e-03
10 20 30
....*....|....*....|....*....|....*.
gi 817478029 26 VDRLVGMLMDGLKDLGLDKclNLILI--SDHGMEQG 59
Cdd:COG3119 209 VDDQVGRLLDALEELGLAD--NTIVVftSDNGPSLG 242
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
26-55 |
6.15e-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: 39.09 E-value: 6.15e-03
10 20 30
....*....|....*....|....*....|..
gi 817478029 26 VDRLVGMLMDGLKDLGLDKclNLI--LISDHG 55
Cdd:cd16030 270 VDAQVGRVLDALEELGLAD--NTIvvLWSDHG 299
|
|
| |
