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Conserved domains on  [gi|392900592|ref|NP_001255511|]
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Inositol polyphosphate-related phosphatase domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 105-399 3.71e-100

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


:

Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 301.20  E-value: 3.71e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   105 RKLKVCTVTWNINE---KGVKILSHLAQKIaERGQEMDSDIFFISLQEIPSTAPtfheeaLRILEPVLNGHRLYLSHRAW 181
Cdd:smart00128   1 RDIKVLIGTWNVGGlesPKVDVTSWLFQKI-EVKQSEKPDIYVIGLQEVVGLAP------GVILETIAGKERLWSDLLES 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   182 SQM-----------------VIVFIRQKHLRYaIQPQVSFIASGAMAKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATP- 243
Cdd:smart00128  74 SLNgdgqynvlakvylvgilVLVFVKANHLVY-IKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASn 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   244 -QQRIQDYAKVVRTLRFPQLARFHahakdeIFGSDVVLWIGDLNFRVTVESNvdWRDPEKITEKTFRDVFETEELASHRK 322
Cdd:smart00128 153 vEQRNQDYKTILRALSFPERALLS------QFDHDVVFWFGDLNFRLDSPSY--EEVRRKISKKEFDDLLEKDQLNRQRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   323 KQLAFTDFKEAPIKFPPTHKFEP-DTDNYVP---KRIPSFTDRVLfWVRNSEwlQNIQ---YDCMRGTTPSDHKAVFATF 395
Cdd:smart00128 225 AGKVFKGFQEGPITFPPTYKYDSvGTETYDTsekKRVPAWCDRIL-YRSNGP--ELIQlseYHSGMEITTSDHKPVFATF 301


                   ....
gi 392900592   396 WLTV 399
Cdd:smart00128 302 RLKV 305
 
Name Accession Description Interval E-value
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 105-399 3.71e-100

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 301.20  E-value: 3.71e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   105 RKLKVCTVTWNINE---KGVKILSHLAQKIaERGQEMDSDIFFISLQEIPSTAPtfheeaLRILEPVLNGHRLYLSHRAW 181
Cdd:smart00128   1 RDIKVLIGTWNVGGlesPKVDVTSWLFQKI-EVKQSEKPDIYVIGLQEVVGLAP------GVILETIAGKERLWSDLLES 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   182 SQM-----------------VIVFIRQKHLRYaIQPQVSFIASGAMAKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATP- 243
Cdd:smart00128  74 SLNgdgqynvlakvylvgilVLVFVKANHLVY-IKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASn 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   244 -QQRIQDYAKVVRTLRFPQLARFHahakdeIFGSDVVLWIGDLNFRVTVESNvdWRDPEKITEKTFRDVFETEELASHRK 322
Cdd:smart00128 153 vEQRNQDYKTILRALSFPERALLS------QFDHDVVFWFGDLNFRLDSPSY--EEVRRKISKKEFDDLLEKDQLNRQRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   323 KQLAFTDFKEAPIKFPPTHKFEP-DTDNYVP---KRIPSFTDRVLfWVRNSEwlQNIQ---YDCMRGTTPSDHKAVFATF 395
Cdd:smart00128 225 AGKVFKGFQEGPITFPPTYKYDSvGTETYDTsekKRVPAWCDRIL-YRSNGP--ELIQlseYHSGMEITTSDHKPVFATF 301


                   ....
gi 392900592   396 WLTV 399
Cdd:smart00128 302 RLKV 305
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 107-395 4.82e-47

Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases.


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 163.66  E-value: 4.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 107 LKVCTVTWNINEKG-----VKILSHLAQkiaergqEMDSDIFFISLQEIPSTAPTFHEEALRI------------LEPVL 169
Cdd:cd09074    1 VKIFVVTWNVGGGIsppenLENWLSPKG-------TEAPDIYAVGVQEVDMSVQGFVGNDDSAkarewvdniqeaLNEKE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 170 NGHRLYlSHRAWSQMVIVFIRQKHLRYAIQPQVSFIASGAM-AKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATPQ--QR 246
Cdd:cd09074   74 NYVLLG-SAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGgGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEveRR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 247 IQDYAKVVRTLRFPQLARfhahAKDEIFGSDVVLWIGDLNFRVTVESnvdwrDPEK--ITEKTFRDVFETEELASHRKKQ 324
Cdd:cd09074  153 NQDYRDILSKLKFYRGDP----AIDSIFDHDVVFWFGDLNYRIDSTD-----DEVRklISQGDLDDLLEKDQLKKQKEKG 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392900592 325 LAFTDFKEAPIKFPPTHKFEPDTDNYV---PKRIPSFTDRVLFWVRNSEWLQNIQYDCMRGTTPSDHKAVFATF 395
Cdd:cd09074  224 KVFDGFQELPITFPPTYKFDPGTDEYDtsdKKRIPAWCDRILYKSKAGSEIQPLSYTSVPLYKTSDHKPVRATF 297
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
217-395 5.21e-24

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 103.71  E-value: 5.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 217 KGAIAVCLRlYQRF-IVLIGCHLS-HATP-QQRIQDYAKVVRTLRFPQLARfhahakdeIFGSDVVLWIGDLNFRVTVeS 293
Cdd:COG5411  153 KGAVAIRFN-YERTsFCFVNSHLAaGVNNiEERIFDYRSIASNICFSRGLR--------IYDHDTIFWLGDLNYRVTS-T 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 294 NVDWRDPEKITEKTFRDVFETEELASHRKKQLAFTDFKEAPIKFPPTHKFEPDTDNYVPK---RIPSFTDRVLFwvrNSE 370
Cdd:COG5411  223 NEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSdkgRIPSWTDRILY---KSE 299

                        170       180
                 ....*....|....*....|....*
gi 392900592 371 WLQNIQYDCMRGTTPSDHKAVFATF 395
Cdd:COG5411  300 QLTPHSYSSIPHLMISDHRPVYATF 324
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 183-414 2.01e-19

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 90.74  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 183 QMV----IVFIRQKHLRYAIQPQVSFIASGAMAKpVRTKGAIAVCLRLYQRFIVLIGCHLSHA----TPQQRIQDYAKVV 254
Cdd:PLN03191 371 QMVgiyvSVWVRKRLRRHINNLKVSPVGVGLMGY-MGNKGSVSISMSLFQSRLCFVCSHLTSGhkdgAEQRRNADVYEII 449

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 255 RTLRFPQLarFHAHAKDEIFGSDVVLWIGDLNFRVTVeSNVDWRdpEKITEKTFRDVFETEELASHRKKQLAFTDFKEAP 334
Cdd:PLN03191 450 RRTRFSSV--LDTDQPQTIPSHDQIFWFGDLNYRLNM-LDTEVR--KLVAQKRWDELINSDQLIKELRSGHVFDGWKEGP 524

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 335 IKFPPTHKFEPDTDNYV--------PKRIPSFTDRVLfwvrnseWL-QNIQYDCMRGTT--PSDHKAVFATFWLTVinkP 403
Cdd:PLN03191 525 IKFPPTYKYEINSDRYVgenpkegeKKRSPAWCDRIL-------WLgKGIKQLCYKRSEirLSDHRPVSSMFLVEV---E 594

                        250
                 ....*....|.
gi 392900592 404 VPEHYKQQKSL 414
Cdd:PLN03191 595 VFDHRKLQRAL 605
 
Name Accession Description Interval E-value
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 105-399 3.71e-100

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 301.20  E-value: 3.71e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   105 RKLKVCTVTWNINE---KGVKILSHLAQKIaERGQEMDSDIFFISLQEIPSTAPtfheeaLRILEPVLNGHRLYLSHRAW 181
Cdd:smart00128   1 RDIKVLIGTWNVGGlesPKVDVTSWLFQKI-EVKQSEKPDIYVIGLQEVVGLAP------GVILETIAGKERLWSDLLES 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   182 SQM-----------------VIVFIRQKHLRYaIQPQVSFIASGAMAKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATP- 243
Cdd:smart00128  74 SLNgdgqynvlakvylvgilVLVFVKANHLVY-IKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASn 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   244 -QQRIQDYAKVVRTLRFPQLARFHahakdeIFGSDVVLWIGDLNFRVTVESNvdWRDPEKITEKTFRDVFETEELASHRK 322
Cdd:smart00128 153 vEQRNQDYKTILRALSFPERALLS------QFDHDVVFWFGDLNFRLDSPSY--EEVRRKISKKEFDDLLEKDQLNRQRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592   323 KQLAFTDFKEAPIKFPPTHKFEP-DTDNYVP---KRIPSFTDRVLfWVRNSEwlQNIQ---YDCMRGTTPSDHKAVFATF 395
Cdd:smart00128 225 AGKVFKGFQEGPITFPPTYKYDSvGTETYDTsekKRVPAWCDRIL-YRSNGP--ELIQlseYHSGMEITTSDHKPVFATF 301


                   ....
gi 392900592   396 WLTV 399
Cdd:smart00128 302 RLKV 305
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 107-395 4.82e-47

Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases.


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 163.66  E-value: 4.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 107 LKVCTVTWNINEKG-----VKILSHLAQkiaergqEMDSDIFFISLQEIPSTAPTFHEEALRI------------LEPVL 169
Cdd:cd09074    1 VKIFVVTWNVGGGIsppenLENWLSPKG-------TEAPDIYAVGVQEVDMSVQGFVGNDDSAkarewvdniqeaLNEKE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 170 NGHRLYlSHRAWSQMVIVFIRQKHLRYAIQPQVSFIASGAM-AKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATPQ--QR 246
Cdd:cd09074   74 NYVLLG-SAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGgGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEveRR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 247 IQDYAKVVRTLRFPQLARfhahAKDEIFGSDVVLWIGDLNFRVTVESnvdwrDPEK--ITEKTFRDVFETEELASHRKKQ 324
Cdd:cd09074  153 NQDYRDILSKLKFYRGDP----AIDSIFDHDVVFWFGDLNYRIDSTD-----DEVRklISQGDLDDLLEKDQLKKQKEKG 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392900592 325 LAFTDFKEAPIKFPPTHKFEPDTDNYV---PKRIPSFTDRVLFWVRNSEWLQNIQYDCMRGTTPSDHKAVFATF 395
Cdd:cd09074  224 KVFDGFQELPITFPPTYKFDPGTDEYDtsdKKRIPAWCDRILYKSKAGSEIQPLSYTSVPLYKTSDHKPVRATF 297
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 107-395 2.62e-39

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate 5-phosphatase J and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase J (INPP5J), also known as PIB5PA or PIPP, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5J hydrolyzes PI(4,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4 at ruffling membranes. These proteins contain a C-terminal, SKIP carboxyl homology domain (SKICH), which may direct plasma membrane ruffle localization.


Pssm-ID: 197328  Cd Length: 300  Bit Score: 143.28  E-value: 2.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 107 LKVCTVTWNINEKGVKI-LSHLAQKIAErgqEMDSDIFFISLQEIpSTAPT-------FH----EEALRILEPvLNGHRL 174
Cdd:cd09094    1 LRVYVVTWNVATAPPPIdVRSLLGLQSP---EVAPDIYIIGLQEV-NSKPVqfvsdliFDdpwsDLFMDILSP-KGYVKV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 175 YlSHRAWSQMVIVFIRQKHLRYAIQPQVSFiasgamakpVRT--------KGAIAVCLRLYQRFIVLIGCHLS---HATp 243
Cdd:cd09094   76 S-SIRLQGLLLLVFVKIQHLPFIRDVQTNY---------TRTglggywgnKGAVTVRFSLYGHMICFLNCHLPahmEKW- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 244 QQRIQDYAKVVRTLRFPQlarfhaHAKDEIFGSDVVLWIGDLNFRVTVESNVDWRdpEKITEKTFRDVFETEELASHRKK 323
Cdd:cd09094  145 EQRIDDFETILSTQVFNE------CNTPSILDHDYVFWFGDLNFRIEDVSIEFVR--ELVNSKKYHLLLEKDQLNMAKRK 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 324 QLAFTDFKEAPIKFPPTHKFEPDTDNY---VPKRIPSFTDRVLFWV-----RNSEWLQNIQ--YDCMRGTTPSDHKAVFA 393
Cdd:cd09094  217 EEAFQGFQEGPLNFAPTYKFDLGTDEYdtsGKKRKPAWTDRILWKVnpdasTEEKFLSITQtsYKSHMEYGISDHKPVTA 296


                 ..
gi 392900592 394 TF 395
Cdd:cd09094  297 QF 298
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 113-395 2.44e-36

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins; This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain.


Pssm-ID: 197327  Cd Length: 292  Bit Score: 134.75  E-value: 2.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 113 TWNINEKGVKilSHLAQKIAErgQEMDSDIFFISLQEIPSTAPTF-------HEEALRILEPVLNGHRLY---LSHRAWS 182
Cdd:cd09093    7 TWNVNGQSPD--ESLRPWLSC--DEEPPDIYAIGFQELDLSAEAFlfndssrEQEWVKAVERGLHPDAKYkkvKLIRLVG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 183 QMVIVFIRQKHLRYAIQPQVSFIASGAMAKpVRTKGAIAVCLRLYQRFIVLIGCHLS-HATP-QQRIQDYAKVVRTLRFP 260
Cdd:cd09093   83 MMLLVFVKKEHRQHIKEVAAETVGTGIMGK-MGNKGGVAVRFQFHNTTFCFVNSHLAaHMEEvERRNQDYKDICARMKFE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 261 QLARFHAhakdEIFGSDVVLWIGDLNFRVTvESNVDWRdPEKITEKTFRDVFETEELASHRKKQLAFTDFKEAPIKFPPT 340
Cdd:cd09093  162 DPDGPPL----SISDHDVVFWLGDLNYRIQ-ELPTEEV-KELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINFIPT 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392900592 341 HKFEPDTDNY---VPKRIPSFTDRVLfwvrnseWL-QNIQYDCMRGTTP---SDHKAVFATF 395
Cdd:cd09093  236 YKYDPGTDNWdssEKCRAPAWCDRIL-------WRgTNIVQLSYRSHMElktSDHKPVSALF 290
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 104-395 3.40e-36

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol polyphosphate-5-phosphatase E and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase E (also called type IV or 72 kDa 5-phosphatase), rat pharbin, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5E hydrolyzes the 5-phosphate from PI(3,5)P2, PI(4,5)P2 and PI(3,4,5)P3, forming PI3P, PI4P, and PI(3,4)P2, respectively. It is a very potent PI(3,4,5)P3 5-phosphatase. Its intracellular localization is chiefly cytosolic, with pronounced perinuclear/Golgi localization. INPP5E also has an N-terminal proline rich domain (PRD) and a C-terminal CAAX motif. This protein is expressed in a variety of tissues, including the breast, brain, testis, and haemopoietic cells. It is differentially expressed in several cancers, for example, it is up-regulated in cervical cancer and down-regulated in stomach cancer. It is a candidate target for therapeutics of obesity and related disorders, as it is expressed in the hypothalamus, and following insulin stimulation, it undergoes tyrosine phosphorylation, associates with insulin receptor substrate-1, -2, and PI3-kinase, and become active as a 5-phosphatase. INPP5E may play a role, along with other 5-phosphatases SHIP2 and SKIP, in regulating glucose homoeostasis and energy metabolism. Mice deficient in INPPE5 develop a multi-organ disorder associated with structural defects of the primary cilium.


Pssm-ID: 197329  Cd Length: 298  Bit Score: 134.86  E-value: 3.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 104 DRKLKVCTVTWNIN-EKGVKilSHLAQKIAERGQEMDSDIFFISLQEIPSTAptfHEEALRILEPVLNGHRL--YLSHRA 180
Cdd:cd09095    2 DRNVGIFVATWNMQgQKELP--ENLDDFLLPTSADFAQDIYVIGVQEGCSDR---REWEIRLQETLGPSHVLlhSASHGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 181 WSQMVivFIRQKHLRYAIQPQVSFIASgAMAKPVRTKGAIAVCLRLYQRFIVLIGCHL--SHATPQQRIQDYAKVVRTLR 258
Cdd:cd09095   77 LHLAV--FIRRDLIWFCSEVESATVTT-RIVSQIKTKGALAISFTFFGTSFLFITSHFtsGDGKVKERVLDYNKIIQALN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 259 FPQLAR---FHAHAKDEIFGSDVVLWIGDLNFRVTVESNVDWRDPEKITEKTFRDVFETEELASHRKKQLAFTDFKEAPI 335
Cdd:cd09095  154 LPRNVPtnpYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPI 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392900592 336 KFPPTHKFEPDTDNY---VPKRIPSFTDRVLFWVRNSEWLQNIQYDCMRGTTPSDHKAVFATF 395
Cdd:cd09095  234 HFPPTYKFDIGSDVYdtsSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALF 296
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 113-395 1.05e-34

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae Inp51p, Inp52p, and Inp53p, and related proteins; This subfamily contains the INPP5c domain of three Saccharomyces cerevisiae synaptojanin-like inositol polyphosphate 5-phosphatases (INP51, INP52, and INP53), Schizosaccharomyces pombe synaptojanin (SPsynaptojanin), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, these proteins have an N-terminal catalytic Sac1-like domain (found in other proteins including the phophoinositide phosphatase Sac1p), and a C-terminal proline-rich domain (PRD). The Sac1 domain allows Inp52p and Inp53p to recognize and dephosphorylate a wider range of substrates including PI3P, PI4P, and PI(3,5)P2. The Sac1 domain of Inp51p is non-functional. Disruption of any two of INP51, INP52, and INP53, in S. cerevisiae leads to abnormal vacuolar and plasma membrane morphology. During hyperosmotic stress, Inp52p and Inp53p localize at actin patches, where they may facilitate the hydrolysis of PI(4,5)P2, and consequently promote actin rearrangement to regulate cell growth. SPsynaptojanin is also active against a range of soluble and lipid inositol phosphates, including I(1,4,5)P3, I(1,3,4,5)P4, I(1,4,5,6)P4, PI(4,5)P2, and PIP3. Transformation of S. cerevisiae with a plasmid expressing the SPsynaptojanin 5-phosphatase domain rescues inp51/inp52/inp53 triple-mutant strains.


Pssm-ID: 197324  Cd Length: 291  Bit Score: 130.54  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 113 TWNINEKGVKIlsHLAQKIAERGQEMDSDIFFISLQE--------IPSTAPTFHEEALRILEPVLNGHRL--YLshRAWS 182
Cdd:cd09090    7 TFNVNGKSYKD--DLSSWLFPEENDELPDIVVIGLQEvveltagqILNSDPSKSSFWEKKIKTTLNGRGGekYV--LLRS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 183 -QMV----IVFIRQKHLRYAIQPQVSFIASG--AMAKpvrTKGAIAVCLRLYQRFIVLIGCHLS--HATPQQRIQDYAKV 253
Cdd:cd09090   83 eQLVgtalLFFVKESQLPKVKNVEGSTKKTGlgGMSG---NKGAVAIRFDYGDTSFCFVTSHLAagLTNYEERNNDYKTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 254 VRTLRFPQLARFHAHakdeifgsDVVLWIGDLNFRVTVeSNVDWRDpeKITEKTFRDVFETEELASHRKKQLAFTDFKEA 333
Cdd:cd09090  160 ARGLRFSRGRTIKDH--------DHVIWLGDFNYRISL-TNEDVRR--FILNGKLDKLLEYDQLNQQMNAGEVFPGFSEG 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392900592 334 PIKFPPTHKFEPDTDNY---VPKRIPSFTDRVLFwvrNSEWLQNIQYDCMRGTTpSDHKAVFATF 395
Cdd:cd09090  229 PITFPPTYKYDKGTDNYdtsEKQRIPAWTDRILY---RGENLRQLSYNSAPLRF-SDHRPVYATF 289
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
217-395 5.21e-24

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 103.71  E-value: 5.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 217 KGAIAVCLRlYQRF-IVLIGCHLS-HATP-QQRIQDYAKVVRTLRFPQLARfhahakdeIFGSDVVLWIGDLNFRVTVeS 293
Cdd:COG5411  153 KGAVAIRFN-YERTsFCFVNSHLAaGVNNiEERIFDYRSIASNICFSRGLR--------IYDHDTIFWLGDLNYRVTS-T 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 294 NVDWRDPEKITEKTFRDVFETEELASHRKKQLAFTDFKEAPIKFPPTHKFEPDTDNYVPK---RIPSFTDRVLFwvrNSE 370
Cdd:COG5411  223 NEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSdkgRIPSWTDRILY---KSE 299

                        170       180
                 ....*....|....*....|....*
gi 392900592 371 WLQNIQYDCMRGTTPSDHKAVFATF 395
Cdd:COG5411  300 QLTPHSYSSIPHLMISDHRPVYATF 324
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 107-368 6.75e-21

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This subfamily contains the INPP5c domains of two human synaptojanins, synaptojanin 1 (Synj1) and synaptojanin 2 (Synj2), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs). They belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, Synjs contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25 (a mitochondrial outer membrane protein). Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197323 [Multi-domain]  Cd Length: 328  Bit Score: 92.84  E-value: 6.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 107 LKVCTVTWNIN------------EKGVKILSHLAQKIAERGQEMDS-----DIFFISLQE--------IPSTAPTFHEEA 161
Cdd:cd09089    1 LRVFVGTWNVNggkhfrsiafkhQSMTDWLLDNPKLAGQCSNDSEEdekpvDIFAIGFEEmvdlnasnIVSASTTNQKEW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 162 LRILEPVLNGHRLYLShRAWSQMV----IVFIRQKHLRYAIQPQVSFIASGaMAKPVRTKGAIAVCLRLYQRFIVLIGCH 237
Cdd:cd09089   81 GEELQKTISRDHKYVL-LTSEQLVgvclFVFVRPQHAPFIRDVAVDTVKTG-LGGAAGNKGAVAIRFLLHSTSLCFVCSH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 238 LSHATPQ--QRIQDYAKVVRTLRFPqLARfhahakdEIFGSDVVLWIGDLNFRVTVEsnvdwRDPEK--ITEKTFRDVFE 313
Cdd:cd09089  159 FAAGQSQvkERNEDFAEIARKLSFP-MGR-------TLDSHDYVFWCGDFNYRIDLP-----NDEVKelVRNGDWLKLLE 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392900592 314 TEELASHRKKQLAFTDFKEAPIKFPPTHK---FEPDTDNYVPKRIPSFTDRVLFWVRN 368
Cdd:cd09089  226 FDQLTKQKAAGNVFKGFLEGEINFAPTYKydlFSDDYDTSEKCRTPAWTDRVLWRRRK 283
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 141-395 1.02e-19

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and -2, and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D), and SHIP2 (also known as INPPL1). It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Both SHIP1 and -2 catalyze the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP1 also converts inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4] to inositol-1,3,4-polyphosphate [I(1,3,4)P3]. SHIP1 and SHIP2 have little overlap in their in vivo functions. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. SHIP2 is as an inhibitor of the insulin signaling pathway, and is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD), while SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif, and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate gene for conferring a predisposition for type 2 diabetes.


Pssm-ID: 197325  Cd Length: 307  Bit Score: 89.23  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 141 DIFFISLQEIPSTAPTFHEEALRILEPVLN-GHRLYLSHRAWSQMVIVFIRQKHLRYAIQPQVSFIASGaMAKPVRTKGA 219
Cdd:cd09091   42 DIYVIGTQEDPLGEKEWLDLLRHSLKELTSlDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTG-IANTLGNKGA 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 220 IAVCLRLYQRFIVLIGCHLSHATPQ--QRIQDYAKVVRTLRF--PQLARFH-AHAKDEIFgsdvvlWIGDLNFRVTVESN 294
Cdd:cd09091  121 VGVSFMFNGTSFGFVNSHLTSGSEKklRRNQNYLNILRFLSLgdKKLSAFNiTHRFTHLF------WLGDLNYRLDLPIQ 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 295 VDWRDPEKITEKTFRDVFETEELASHRKKQLAFTDFKEAPIKFPPTHKFEPDT-DNY---------VPKRIPSFTDRVLf 364
Cdd:cd09091  195 EAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFLRFSEEEITFPPTYRYERGSrDTYaytkqkatgVKYNLPSWCDRIL- 273

                        250       260       270
                 ....*....|....*....|....*....|....
gi 392900592 365 WvrNSEWLQNI---QYDCMRGTTPSDHKAVFATF 395
Cdd:cd09091  274 W--KSYPETHIicqSYGCTDDIVTSDHSPVFGTF 305
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 183-414 2.01e-19

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 90.74  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 183 QMV----IVFIRQKHLRYAIQPQVSFIASGAMAKpVRTKGAIAVCLRLYQRFIVLIGCHLSHA----TPQQRIQDYAKVV 254
Cdd:PLN03191 371 QMVgiyvSVWVRKRLRRHINNLKVSPVGVGLMGY-MGNKGSVSISMSLFQSRLCFVCSHLTSGhkdgAEQRRNADVYEII 449

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 255 RTLRFPQLarFHAHAKDEIFGSDVVLWIGDLNFRVTVeSNVDWRdpEKITEKTFRDVFETEELASHRKKQLAFTDFKEAP 334
Cdd:PLN03191 450 RRTRFSSV--LDTDQPQTIPSHDQIFWFGDLNYRLNM-LDTEVR--KLVAQKRWDELINSDQLIKELRSGHVFDGWKEGP 524

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 335 IKFPPTHKFEPDTDNYV--------PKRIPSFTDRVLfwvrnseWL-QNIQYDCMRGTT--PSDHKAVFATFWLTVinkP 403
Cdd:PLN03191 525 IKFPPTYKYEINSDRYVgenpkegeKKRSPAWCDRIL-------WLgKGIKQLCYKRSEirLSDHRPVSSMFLVEV---E 594

                        250
                 ....*....|.
gi 392900592 404 VPEHYKQQKSL 414
Cdd:PLN03191 595 VFDHRKLQRAL 605
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 141-395 1.84e-18

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP1's enzymic activity is restricted to phosphatidylinositol 3,4,5-trisphosphate [PI (3,4,5)P3] and inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4]. It converts these two phosphoinositides to phosphatidylinositol 3,4-bisphosphate [PI (3,4)P2] and inositol-1,3,4-polyphosphate [I(1,3,4)P3], respectively. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD). SHIP1's phosphorylated NPXY motifs interact with proteins with phosphotyrosine binding (PTB) domains, and facilitate the translocation of SHIP1 to the plasma membrane to hydrolyze PI(3,4,5)P3. SHIP1 generally acts to oppose the activity of phosphatidylinositol 3-kinase (PI3K). It acts as a negative signaling molecule, reducing the levels of PI(3,4,5)P3, thereby removing the latter as a membrane-targeting signal for PH domain-containing effector molecules. SHIP1 may also, in certain contexts, amplify PI3K signals. SHIP1 and SHIP2 have little overlap in their in vivo functions.


Pssm-ID: 197334  Cd Length: 307  Bit Score: 85.42  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 141 DIFFISLQEIPSTaptfHEEALRILEPVLNG-----HRLYLSHRAWSQMVIVFIRQKHlryaiQPQVSFIASGA----MA 211
Cdd:cd09100   42 DIYVIGTQEDPLG----EKEWLDTLKHSLREitsisFKVIAIQTLWNIRIVVLAKPEH-----ENRISHICTDSvktgIA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 212 KPVRTKGAIAVCLRLYQRFIVLIGCHLSHATPQQ--RIQDYAKVVRTLRF--PQLARFH-AHAKDEIFgsdvvlWIGDLN 286
Cdd:cd09100  113 NTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKlrRNQNYFNILRFLVLgdKKLSPFNiTHRFTHLF------WLGDLN 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 287 FRVTVESNVDWRDPEKITEKTFRDVFETEELASHRKKQLAFTDFKEAPIKFPPTHKFEPDT-DNYVPKR---------IP 356
Cdd:cd09100  187 YRVELPNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQFEEEEITFAPTYRFERGTrERYAYTKqkatgmkynLP 266

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 392900592 357 SFTDRVLfwvRNSEWLQNI---QYDCMRGTTPSDHKAVFATF 395
Cdd:cd09100  267 SWCDRVL---WKSYPLVHVvcqSYGCTDDITTSDHSPVFATF 305
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 181-395 4.44e-18

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol 5-phosphatase-2 and related proteins; This subfamily contains the INPP5c domain of SHIP2 (SH2 domain containing inositol 5-phosphatase-2, also called INPPL1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP2 catalyzes the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. SHIP2 is an inhibitor of the insulin signaling pathway. It is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. Its interacting partners include filamin/actin, p130Cas, Shc, Vinexin, Interesectin 1, and c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1). A large variety of extracellular stimuli appear to lead to the tyrosine phosphorylation of SHIP2, including epidermal growth factor (EGF), platelet-derived growth factor (PDGF), insulin, macrophage colony-stimulating factor (M-CSF) and hepatocyte growth factor (HGF). SHIP2 is localized to the cytosol in quiescent cells; following growth factor stimulation and /or cell adhesion, it relocalizes to membrane ruffles. In addition to this INPP5c domain, SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate for conferring a predisposition for type 2 diabetes; it has been suggested that suppression of SHIP2 may be of benefit in the treatment of obesity and thereby prevent type 2 diabetes. SHIP2 and SHIP1 have little overlap in their in vivo functions.


Pssm-ID: 197335  Cd Length: 304  Bit Score: 84.25  E-value: 4.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 181 WSQMVIVFIRQKHLRYAIQPQVSFIASGaMAKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATPQ--QRIQDYAKVVRTLR 258
Cdd:cd09101   83 WNIKMVVLVKPEHENRISHVHTSSVKTG-IANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKthRRNQNYLDILRSLS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 259 F--PQLARFhahakDEIFGSDVVLWIGDLNFRVtvesNVDWRDP-EKITEKTFRDVFETEELASHRKKQLAFTDFKEAPI 335
Cdd:cd09101  162 LgdKQLNAF-----DISLRFTHLFWFGDLNYRL----DMDIQEIlNYITRKEFDPLLAVDQLNLEREKNKVFLRFREEEI 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 336 KFPPTHKFEPDT-DNYVPKR---------IPSFTDRVLFWVRNSEWLQNIQYDCMRGTTPSDHKAVFATF 395
Cdd:cd09101  233 SFPPTYRYERGSrDTYMWQKqkttgmrtnVPSWCDRILWKSYPETHIVCNSYGCTDDIVTSDHSPVFGTF 302
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 107-371 1.17e-17

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This subfamily contains the INPP5c domains of human synaptojanin 1 (Synj1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro.


Pssm-ID: 197332  Cd Length: 336  Bit Score: 83.55  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 107 LKVCTVTWNINE----KGVKILSHL-------AQKIAERGQEMD-----SDIFFISLQEIPS-------TAPTFHEE--A 161
Cdd:cd09098    1 IRVCVGTWNVNGgkqfRSIAFKNQTltdwlldAPKKAGIPEFQDvrskpVDIFAIGFEEMVElnagnivSASTTNQKlwA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 162 LRILEPVLNGHRLYLshRAWSQMV----IVFIRQKHLRYAIQPQVSFIASGaMAKPVRTKGAIAVCLRLYQRFIVLIGCH 237
Cdd:cd09098   81 AELQKTISRDQKYVL--LASEQLVgvclFVFIRPQHAPFIRDVAVDTVKTG-MGGATGNKGAVAIRMLFHTTSLCFVCSH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 238 LSHATPQ--QRIQDYAKVVRTLRFPqLARFhahakdeIFGSDVVLWIGDLNFRVTVESNvdwRDPEKITEKTFRDVFETE 315
Cdd:cd09098  158 FAAGQSQvkERNEDFIEIARKLSFP-MGRM-------LFSHDYVFWCGDFNYRIDIPNE---EVKELIRQQNWDSLIAGD 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392900592 316 ELASHRKKQLAFTDFKEAPIKFPPTHKFEPDTDNYVPK---RIPSFTDRVLfWvRNSEW 371
Cdd:cd09098  227 QLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSekcRTPAWTDRVL-W-RRRKW 283
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 187-365 4.43e-17

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This subfamily contains the INPP5c domains of human synaptojanin 2 (Synj2) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25, a mitochondrial outer membrane protein. Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197333  Cd Length: 336  Bit Score: 81.99  E-value: 4.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 187 VFIRQKHLRYAIQPQVSFIASGaMAKPVRTKGAIAVCLRLYQRFIVLIGCHLSHATPQ--QRIQDYAKVVRTLRFPqlar 264
Cdd:cd09099  108 IFVRPYHVPFIRDVAIDTVKTG-MGGKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQvkERNEDYKEITQKLSFP---- 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 265 fhahAKDEIFGSDVVLWIGDLNFRV--TVESNVDWrdpekITEKTFRDVFETEELASHRKKQLAFTDFKEAPIKFPPTHK 342
Cdd:cd09099  183 ----MGRNVFSHDYVFWCGDFNYRIdlTYEEVFYF-----IKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTYK 253

                        170       180
                 ....*....|....*....|....*.
gi 392900592 343 FEPDTDNYVPK---RIPSFTDRVLFW 365
Cdd:cd09099  254 YDVGSEAYDTSdkcRTPAWTDRVLWW 279
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 214-397 4.87e-05

Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3.


Pssm-ID: 197326  Cd Length: 383  Bit Score: 45.15  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 214 VRTKGAIAVCLrlyqrfIVLIGCHLSH-----ATPQQRIQDYAKVV-RTLRFpQLARFHahakDEIFGSDVVLWIGDLNF 287
Cdd:cd09092  158 MRTRWKINNCV------FDLVNIHLFHdasnlAACESSPSVYSQNRhRALGY-VLERLT----DERFEKVPFFVFGDFNF 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 288 RVTVESNVDwRDPEKITEKTFRDVFETEE---------------LASHRKK-----QLAFTDFK---------------- 331
Cdd:cd09092  227 RLDTKSVVE-TLCAKATMQTVRKADSNIVvklefrekdndnkvvLQIEKKKfdyfnQDVFRDNNgkallkfdkelevfkd 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 332 ---EAPIKFPPTHKFEPDTDN---YVPKRIPSFTDRVLF-----WVRNSEWLQNIQYD------CMrgttpSDHKAVFAT 394
Cdd:cd09092  306 vlyELDISFPPSYPYSEDPEQgtqYMNTRCPAWCDRILMshsarELKSENEEKSVTYDmigpnvCM-----GDHKPVFLT 380


                 ...
gi 392900592 395 FWL 397
Cdd:cd09092  381 FRI 383
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 258-395 1.88e-03

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 39.63  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 258 RFPQLARFHAHAKDEIFGSDVVLwIGDLNFRvtvesnvDWRDPEKITEKTFRDVFEteelASHRKKQLAFT-DFKEAPIK 336
Cdd:cd09080  128 RTAQLEEIAKKLKKPPGAANVIL-GGDFNLR-------DKEDDTGGLPNGFVDAWE----ELGPPGEPGYTwDTQKNPML 195

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392900592 337 FPPTHKFepdtdnyvPKRIpsftDRVLFwvRNSEW-LQNIQY-------DCMRGTTPSDHKAVFATF 395
Cdd:cd09080  196 RKGEAGP--------RKRF----DRVLL--RGSDLkPKSIELigtepipGDEEGLFPSDHFGLLAEL 248
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 112-395 5.43e-03

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 38.10  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 112 VTWNINekGVKILSHLAQkIAERGQEMDSDIFFisLQEipstapTFHEEALRILEPVLNGHRLYLSHRAWSQM-VIVFIR 190
Cdd:cd09076    2 GTLNVR--GLRSPGKRAQ-LLEELKRKKLDILG--LQE------THWTGEGELKKKREGGTILYSGSDSGKSRgVAILLS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 191 QKHLRYAIQpqVSFIASGAMakpvrtkgaIAVCLRLYQRFIVLIGCHLSHATPQQRIQDYAKVVRTLRfpqlarfhahak 270
Cdd:cd09076   71 KTAANKLLE--YTKVVSGRI---------IMVRFKIKGKRLTIINVYAPTARDEEEKEEFYDQLQDVL------------ 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900592 271 DEIFGSDVVLWIGDLNFRVTVESNVDWRDpEKITEktfrdvfETEELASHRKKQLAFTDFKEapIKFPPTHKF---EPDT 347
Cdd:cd09076  128 DKVPRHDTLIIGGDFNAVLGPKDDGRKGL-DKRNE-------NGERALSALIEEHDLVDVWR--ENNPKTREYtwrSPDH 197

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 392900592 348 DNYvpKRIpsftDRVLFwvrNSEWLQNIqYDCMRGTTP-SDHKAVFATF 395
Cdd:cd09076  198 GSR--SRI----DRILV---SKRLRVKV-KKTKITPGAgSDHRLVTLKL 236
 
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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