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Conserved domains on  [gi|2027456844|ref|XP_040870017|]
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type I inositol polyphosphate 5-phosphatase 4 isoform X4 [Glycine max]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 662)

exonuclease/endonuclease/phosphatase (EEP) family protein may cleave phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 1-532 2.04e-158

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


The actual alignment was detected with superfamily member PLN03191:

Pssm-ID: 469791 [Multi-domain]  Cd Length: 621  Bit Score: 465.92  E-value: 2.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844   1 MRDENSKKSKLSWPKSLVKKWFNIKSKAEDFHADDVLSQ--GVDEECS-----SNYSEREACTIRKSKSE---------- 63
Cdd:PLN03191    1 MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTEteSEDDACSvkdvrVNVDEDHANRRQGNQSVfgnqisdggv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  64 RSSRWYSDRMRRGKNDLDEAQVTDVYNYRIFAATWNVAGKSPPSYLNLEDWLHTSPPADIYVLGFQEIVPLNAGNVLGTE 143
Cdd:PLN03191   81 SVSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADIYIIGFQEVVPLNAGNVLGAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 144 DNGPARKWLALIRRTLN--SLPGTSGGCHT--PSP-LPNPIV------ELDA-----------------DFEGSMRQKAT 195
Cdd:PLN03191  161 DSRPIPKWEAIIRRTLNksNKPESKHKSYSapPSPvLRTSIVadelaeEVDSlplemmnnefidaatgcPSLEPERNKNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 196 SFFQ----------------RRSFQSLSR---SMRIDNDMIKPQ---------------------ACLER--RLSVCDRV 233
Cdd:PLN03191  241 GWPEhsldatpqvvssnsklRRVFSSSARlgfKWPENPSLFSPQrfalnarglkrshrsfgnlglSWNEIkqRSEVPEVP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 234 MFGHRTSDYDPnyrWGSSDEENGTGGSPittqyspmSYGgCFTTEDSDRQTGHSRYSLVASKQMVGVFLTVWVKSDIRDD 313
Cdd:PLN03191  321 EVIDSLSDVSD---RSSEAEDDTFKEVP--------SYQ-LPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 314 VHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDELRRNSDVMEILRKTRFPPVHDIGdeySPQT 393
Cdd:PLN03191  389 INNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDTD---QPQT 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 394 ILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYAGDDR 473
Cdd:PLN03191  466 IPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYVGENP 545

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027456844 474 RSKQKRRTPAWCDRILWYGRGLHQLSYVRGESRFSDHRPVYSMFLAEVESVSCNQIKKS 532
Cdd:PLN03191  546 KEGEKKRSPAWCDRILWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRA 604
 
Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 1-532 2.04e-158

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 465.92  E-value: 2.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844   1 MRDENSKKSKLSWPKSLVKKWFNIKSKAEDFHADDVLSQ--GVDEECS-----SNYSEREACTIRKSKSE---------- 63
Cdd:PLN03191    1 MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTEteSEDDACSvkdvrVNVDEDHANRRQGNQSVfgnqisdggv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  64 RSSRWYSDRMRRGKNDLDEAQVTDVYNYRIFAATWNVAGKSPPSYLNLEDWLHTSPPADIYVLGFQEIVPLNAGNVLGTE 143
Cdd:PLN03191   81 SVSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADIYIIGFQEVVPLNAGNVLGAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 144 DNGPARKWLALIRRTLN--SLPGTSGGCHT--PSP-LPNPIV------ELDA-----------------DFEGSMRQKAT 195
Cdd:PLN03191  161 DSRPIPKWEAIIRRTLNksNKPESKHKSYSapPSPvLRTSIVadelaeEVDSlplemmnnefidaatgcPSLEPERNKNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 196 SFFQ----------------RRSFQSLSR---SMRIDNDMIKPQ---------------------ACLER--RLSVCDRV 233
Cdd:PLN03191  241 GWPEhsldatpqvvssnsklRRVFSSSARlgfKWPENPSLFSPQrfalnarglkrshrsfgnlglSWNEIkqRSEVPEVP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 234 MFGHRTSDYDPnyrWGSSDEENGTGGSPittqyspmSYGgCFTTEDSDRQTGHSRYSLVASKQMVGVFLTVWVKSDIRDD 313
Cdd:PLN03191  321 EVIDSLSDVSD---RSSEAEDDTFKEVP--------SYQ-LPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 314 VHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDELRRNSDVMEILRKTRFPPVHDIGdeySPQT 393
Cdd:PLN03191  389 INNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDTD---QPQT 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 394 ILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYAGDDR 473
Cdd:PLN03191  466 IPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYVGENP 545

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027456844 474 RSKQKRRTPAWCDRILWYGRGLHQLSYVRGESRFSDHRPVYSMFLAEVESVSCNQIKKS 532
Cdd:PLN03191  546 KEGEKKRSPAWCDRILWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRA 604
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 92-517 2.71e-77

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: 245.69  E-value: 2.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  92 RIFAATWNVAGKSPPSylNLEDWLHTSP-PADIYVLGFQEIvPLNAGNVLgTEDNGPARKWLALIRRTLNslpgtsggch 170
Cdd:cd09093     2 RIFVGTWNVNGQSPDE--SLRPWLSCDEePPDIYAIGFQEL-DLSAEAFL-FNDSSREQEWVKAVERGLH---------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 171 tpsplpnpiveldadfegsmrqkatsffqrrsfqslsrsmridndmikPQAclerrlsvcdrvmfghrtsdydpnyrwgs 250
Cdd:cd09093    68 ------------------------------------------------PDA----------------------------- 70

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 251 sdeengtggspittqyspmsyggcfttedsdrqtghsRYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYL 330
Cdd:cd09093    71 -------------------------------------KYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKM 113

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 331 GNKGSISISMSLHQTSFCFICSHLTSGQkdGDELRRNSDVMEILRKTRFppvhDIGDEySPQTILEHDRIIWLGDLNYRI 410
Cdd:cd09093   114 GNKGGVAVRFQFHNTTFCFVNSHLAAHM--EEVERRNQDYKDICARMKF----EDPDG-PPLSISDHDVVFWLGDLNYRI 186

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 411 A-LSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYagdDRRSKQkrRTPAWCDRIL 489
Cdd:cd09093   187 QeLPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINFIPTYKYDPGTDNW---DSSEKC--RAPAWCDRIL 261

                         410       420
                  ....*....|....*....|....*....
gi 2027456844 490 WYGRGLHQLSYVRGES-RFSDHRPVYSMF 517
Cdd:cd09093   262 WRGTNIVQLSYRSHMElKTSDHKPVSALF 290
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 274-521 1.37e-56

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 192.18  E-value: 1.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  274 CFTTEDSDRQTGHSRYSLVASKQMVGVFLTVWVKSD----IRDDVhnmkVSCVGRGLMGYLGNKGSISISMSLHQTSFCF 349
Cdd:smart00128  66 LWSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANhlvyIKDVE----TFTVKTGMGGLWGNKGAVAVRFKLSDTSFCF 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  350 ICSHLTSGQKDGDelRRNSDVMEILRKTRFPpvhdigdEYSPQTILEHDRIIWLGDLNYRIAL-SYRAAKALVEMHDWKT 428
Cdd:smart00128 142 VNSHLAAGASNVE--QRNQDYKTILRALSFP-------ERALLSQFDHDVVFWFGDLNFRLDSpSYEEVRRKISKKEFDD 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  429 LLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKY-SNNSDRYAgddrrSKQKRRTPAWCDRILW--YGRGLHQLS--YVRG 503
Cdd:smart00128 213 LLEKDQLNRQREAGKVFKGFQEGPITFPPTYKYdSVGTETYD-----TSEKKRVPAWCDRILYrsNGPELIQLSeyHSGM 287

                          250
                   ....*....|....*...
gi 2027456844  504 ESRFSDHRPVYSMFLAEV 521
Cdd:smart00128 288 EITTSDHKPVFATFRLKV 305
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
274-553 2.27e-46

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 168.81  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 274 CFTTEDSDRQtghsrYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSH 353
Cdd:COG5411    99 CLNGAQSDEK-----YSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSH 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 354 LTSGQKDGDElrRNSDVMEILRKTRFPpvhdigdeySPQTILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWK--TLLE 431
Cdd:COG5411   174 LAAGVNNIEE--RIFDYRSIASNICFS---------RGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGRldKLFE 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 432 NDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYAGDDrrskqKRRTPAWCDRILWYGRGLHQLSYVRGES-RFSDH 510
Cdd:COG5411   243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSD-----KGRIPSWTDRILYKSEQLTPHSYSSIPHlMISDH 317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2027456844 511 RPVYSMFLAEVESV----SCNQIKKSASSRIEVVELFPHSHCYSYTD 553
Cdd:COG5411   318 RPVYATFRAKIKVVdpskKEGLIEKLYAEYKTELGEAGDISCDNFTI 364
 
Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 1-532 2.04e-158

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 465.92  E-value: 2.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844   1 MRDENSKKSKLSWPKSLVKKWFNIKSKAEDFHADDVLSQ--GVDEECS-----SNYSEREACTIRKSKSE---------- 63
Cdd:PLN03191    1 MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTEteSEDDACSvkdvrVNVDEDHANRRQGNQSVfgnqisdggv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  64 RSSRWYSDRMRRGKNDLDEAQVTDVYNYRIFAATWNVAGKSPPSYLNLEDWLHTSPPADIYVLGFQEIVPLNAGNVLGTE 143
Cdd:PLN03191   81 SVSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADIYIIGFQEVVPLNAGNVLGAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 144 DNGPARKWLALIRRTLN--SLPGTSGGCHT--PSP-LPNPIV------ELDA-----------------DFEGSMRQKAT 195
Cdd:PLN03191  161 DSRPIPKWEAIIRRTLNksNKPESKHKSYSapPSPvLRTSIVadelaeEVDSlplemmnnefidaatgcPSLEPERNKNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 196 SFFQ----------------RRSFQSLSR---SMRIDNDMIKPQ---------------------ACLER--RLSVCDRV 233
Cdd:PLN03191  241 GWPEhsldatpqvvssnsklRRVFSSSARlgfKWPENPSLFSPQrfalnarglkrshrsfgnlglSWNEIkqRSEVPEVP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 234 MFGHRTSDYDPnyrWGSSDEENGTGGSPittqyspmSYGgCFTTEDSDRQTGHSRYSLVASKQMVGVFLTVWVKSDIRDD 313
Cdd:PLN03191  321 EVIDSLSDVSD---RSSEAEDDTFKEVP--------SYQ-LPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 314 VHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDELRRNSDVMEILRKTRFPPVHDIGdeySPQT 393
Cdd:PLN03191  389 INNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDTD---QPQT 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 394 ILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYAGDDR 473
Cdd:PLN03191  466 IPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYVGENP 545

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027456844 474 RSKQKRRTPAWCDRILWYGRGLHQLSYVRGESRFSDHRPVYSMFLAEVESVSCNQIKKS 532
Cdd:PLN03191  546 KEGEKKRSPAWCDRILWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRA 604
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 92-517 2.71e-77

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: 245.69  E-value: 2.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  92 RIFAATWNVAGKSPPSylNLEDWLHTSP-PADIYVLGFQEIvPLNAGNVLgTEDNGPARKWLALIRRTLNslpgtsggch 170
Cdd:cd09093     2 RIFVGTWNVNGQSPDE--SLRPWLSCDEePPDIYAIGFQEL-DLSAEAFL-FNDSSREQEWVKAVERGLH---------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 171 tpsplpnpiveldadfegsmrqkatsffqrrsfqslsrsmridndmikPQAclerrlsvcdrvmfghrtsdydpnyrwgs 250
Cdd:cd09093    68 ------------------------------------------------PDA----------------------------- 70

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 251 sdeengtggspittqyspmsyggcfttedsdrqtghsRYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYL 330
Cdd:cd09093    71 -------------------------------------KYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKM 113

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 331 GNKGSISISMSLHQTSFCFICSHLTSGQkdGDELRRNSDVMEILRKTRFppvhDIGDEySPQTILEHDRIIWLGDLNYRI 410
Cdd:cd09093   114 GNKGGVAVRFQFHNTTFCFVNSHLAAHM--EEVERRNQDYKDICARMKF----EDPDG-PPLSISDHDVVFWLGDLNYRI 186

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 411 A-LSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYagdDRRSKQkrRTPAWCDRIL 489
Cdd:cd09093   187 QeLPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINFIPTYKYDPGTDNW---DSSEKC--RAPAWCDRIL 261

                         410       420
                  ....*....|....*....|....*....
gi 2027456844 490 WYGRGLHQLSYVRGES-RFSDHRPVYSMF 517
Cdd:cd09093   262 WRGTNIVQLSYRSHMElKTSDHKPVSALF 290
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 92-517 2.75e-71

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: 230.30  E-value: 2.75e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  92 RIFAATWNVAG-KSPPSylNLEDWLH--TSPPADIYVLGFQEIVPLNAGNVlGTEDNGPARKWLALIRRTLNSLPGtsgg 168
Cdd:cd09074     2 KIFVVTWNVGGgISPPE--NLENWLSpkGTEAPDIYAVGVQEVDMSVQGFV-GNDDSAKAREWVDNIQEALNEKEN---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 169 chtpsplpnpiveldadfegsmrqkatsffqrrsfqslsrsmridndmikpqaclerrlsvcdrvmfghrtsdydpnyrw 248
Cdd:cd09074       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 249 gssdeengtggspittqyspmsyggcfttedsdrqtghsrYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSC--VGRGL 326
Cdd:cd09074    75 ----------------------------------------YVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEGvtVGTGG 114

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 327 MGYLGNKGSISISMSLHQTSFCFICSHLTSGQkdgDEL-RRNSDVMEILRKTRFPPvhdigDEYSPQTILEHDRIIWLGD 405
Cdd:cd09074   115 GGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQ---EEVeRRNQDYRDILSKLKFYR-----GDPAIDSIFDHDVVFWFGD 186

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 406 LNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYAgddrrSKQKRRTPAWC 485
Cdd:cd09074   187 LNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFPPTYKFDPGTDEYD-----TSDKKRIPAWC 261

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2027456844 486 DRILW---YGRGLHQLSYVR-GESRFSDHRPVYSMF 517
Cdd:cd09074   262 DRILYkskAGSEIQPLSYTSvPLYKTSDHKPVRATF 297
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 287-517 2.86e-69

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: 226.12  E-value: 2.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 287 SRYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDElrR 366
Cdd:cd09089    92 HKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQVKE--R 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 367 NSDVMEILRKTRFPpvhdigdeySPQTILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFE 446
Cdd:cd09089   170 NEDFAEIARKLSFP---------MGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFK 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 447 GWNEGKIYFPPTYKYSNNSDRYagdDRRSKQkrRTPAWCDRILWYGRGL--------------------HQLSYVRGESR 506
Cdd:cd09089   241 GFLEGEINFAPTYKYDLFSDDY---DTSEKC--RTPAWTDRVLWRRRKWpsdkteeslvetndptwnpgTLLYYGRAELK 315

                         250
                  ....*....|.
gi 2027456844 507 FSDHRPVYSMF 517
Cdd:cd09089   316 TSDHRPVVAII 326
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 92-519 3.70e-69

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: 224.53  E-value: 3.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  92 RIFAATWNVAGKSPPsyLNLEDWLHTS---PPADIYVLGFQEIVPLNAGNVLGTeDNGPARKWLALIRRTLNslpgtsgg 168
Cdd:cd09090     2 NIFVGTFNVNGKSYK--DDLSSWLFPEendELPDIVVIGLQEVVELTAGQILNS-DPSKSSFWEKKIKTTLN-------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 169 chtpsplpnpiveldadfegsmrqkatsffqrrsfqslsrsmridndmikpqaclerrlsvcdrvmfghrtsdydpnyrw 248
Cdd:cd09090       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 249 gssdeengtggspittqyspmsyggcfttedsdrQTGHSRYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMG 328
Cdd:cd09090    71 ----------------------------------GRGGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGG 116

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 329 YLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDElrRNSDVMEILRKTRFPpvhdigdeySPQTILEHDRIIWLGDLNY 408
Cdd:cd09090   117 MSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEE--RNNDYKTIARGLRFS---------RGRTIKDHDHVIWLGDFNY 185

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 409 RIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYagddrRSKQKRRTPAWCDRI 488
Cdd:cd09090   186 RISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITFPPTYKYDKGTDNY-----DTSEKQRIPAWTDRI 260

                         410       420       430
                  ....*....|....*....|....*....|.
gi 2027456844 489 LWYGRGLHQLSYVRGESRFSDHRPVYSMFLA 519
Cdd:cd09090   261 LYRGENLRQLSYNSAPLRFSDHRPVYATFEA 291
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 274-521 1.37e-56

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 192.18  E-value: 1.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  274 CFTTEDSDRQTGHSRYSLVASKQMVGVFLTVWVKSD----IRDDVhnmkVSCVGRGLMGYLGNKGSISISMSLHQTSFCF 349
Cdd:smart00128  66 LWSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANhlvyIKDVE----TFTVKTGMGGLWGNKGAVAVRFKLSDTSFCF 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  350 ICSHLTSGQKDGDelRRNSDVMEILRKTRFPpvhdigdEYSPQTILEHDRIIWLGDLNYRIAL-SYRAAKALVEMHDWKT 428
Cdd:smart00128 142 VNSHLAAGASNVE--QRNQDYKTILRALSFP-------ERALLSQFDHDVVFWFGDLNFRLDSpSYEEVRRKISKKEFDD 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844  429 LLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKY-SNNSDRYAgddrrSKQKRRTPAWCDRILW--YGRGLHQLS--YVRG 503
Cdd:smart00128 213 LLEKDQLNRQREAGKVFKGFQEGPITFPPTYKYdSVGTETYD-----TSEKKRVPAWCDRILYrsNGPELIQLSeyHSGM 287

                          250
                   ....*....|....*...
gi 2027456844  504 ESRFSDHRPVYSMFLAEV 521
Cdd:smart00128 288 EITTSDHKPVFATFRLKV 305
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 288-516 8.79e-55

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: 188.31  E-value: 8.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 288 RYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDElrRN 367
Cdd:cd09099    92 RYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQVKE--RN 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 368 SDVMEILRKTRFPpvhdigdeySPQTILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEG 447
Cdd:cd09099   170 EDYKEITQKLSFP---------MGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKD 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 448 WNEGKIYFPPTYKYSNNSDRYAGDDrrskqKRRTPAWCDRILWYGRGL-----------------------HQLS----- 499
Cdd:cd09099   241 FHEGTINFGPTYKYDVGSEAYDTSD-----KCRTPAWTDRVLWWRKKWpfektageinlldsdldfdtkirHTWTpgalm 315

                         250
                  ....*....|....*...
gi 2027456844 500 -YVRGESRFSDHRPVYSM 516
Cdd:cd09099   316 yYGRAELQASDHRPVLAI 333
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 288-516 5.57e-52

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: 180.62  E-value: 5.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 288 RYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDElrRN 367
Cdd:cd09098    92 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 368 SDVMEILRKTRFPpvhdIGdeyspQTILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEG 447
Cdd:cd09098   170 EDFIEIARKLSFP----MG-----RMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 448 WNEGKIYFPPTYKYSNNSDRYagddrRSKQKRRTPAWCDRILWYGR----------------GLHQ-------------L 498
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDY-----DTSEKCRTPAWTDRVLWRRRkwpfdrsaedldllnaSFPDnskeqytwspgtlL 315

                         250
                  ....*....|....*...
gi 2027456844 499 SYVRGESRFSDHRPVYSM 516
Cdd:cd09098   316 HYGRAELKTSDHRPVVAL 333
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 289-519 9.08e-48

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: 168.32  E-value: 9.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 289 YSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDElrRNS 368
Cdd:cd09094    72 YVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQ--RID 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 369 DVMEILRKTRFPpvhdigdEYSPQTILEHDRIIWLGDLNYRIA-LSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFEG 447
Cdd:cd09094   150 DFETILSTQVFN-------ECNTPSILDHDYVFWFGDLNFRIEdVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQG 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 448 WNEGKIYFPPTYKYSNNSDRYagdDRRSKQkrRTPAWCDRILWY----GRGLH------QLSYVRGES-RFSDHRPVYSM 516
Cdd:cd09094   223 FQEGPLNFAPTYKFDLGTDEY---DTSGKK--RKPAWTDRILWKvnpdASTEEkflsitQTSYKSHMEyGISDHKPVTAQ 297


                  ...
gi 2027456844 517 FLA 519
Cdd:cd09094   298 FRL 300
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
274-553 2.27e-46

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 168.81  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 274 CFTTEDSDRQtghsrYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSH 353
Cdd:COG5411    99 CLNGAQSDEK-----YSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSH 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 354 LTSGQKDGDElrRNSDVMEILRKTRFPpvhdigdeySPQTILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWK--TLLE 431
Cdd:COG5411   174 LAAGVNNIEE--RIFDYRSIASNICFS---------RGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGRldKLFE 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 432 NDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYAGDDrrskqKRRTPAWCDRILWYGRGLHQLSYVRGES-RFSDH 510
Cdd:COG5411   243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSD-----KGRIPSWTDRILYKSEQLTPHSYSSIPHlMISDH 317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2027456844 511 RPVYSMFLAEVESV----SCNQIKKSASSRIEVVELFPHSHCYSYTD 553
Cdd:COG5411   318 RPVYATFRAKIKVVdpskKEGLIEKLYAEYKTELGEAGDISCDNFTI 364
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 333-517 1.79e-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: 137.55  E-value: 1.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 333 KGSISISMSLHQTSFCFICSHLTSGqkDGDELRRNSDVMEILRKTRFPPV--HDIGDEYSPQTILEHDRIIWLGDLNYRI 410
Cdd:cd09095   110 KGALAISFTFFGTSFLFITSHFTSG--DGKVKERVLDYNKIIQALNLPRNvpTNPYKSESGDVTTRFDEVFWFGDFNFRL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 411 ALSYRAAKALVEM---HDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNSDRYagdDRRSKQkrRTPAWCDR 487
Cdd:cd09095   188 SGPRHLVDALINQgqeVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVY---DTSSKQ--RVPSYTDR 262

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2027456844 488 ILWYGRGLHQLSYVRGES----RFSDHRPVYSMF 517
Cdd:cd09095   263 ILYRSRQKGDVCCLKYNScpsiKTSDHRPVFALF 296
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 262-517 1.22e-34

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: 132.80  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 262 ITTQYSPMSYGGCFTT-EDSDRQTGHSRYSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISM 340
Cdd:cd09100    46 IGTQEDPLGEKEWLDTlKHSLREITSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 341 SLHQTSFCFICSHLTSGQKdgDELRRNSDVMEILRktrfppVHDIGD-EYSPQTILEH-DRIIWLGDLNYRIALSYRAAK 418
Cdd:cd09100   126 MFNGTSFGFVNSHLTSGSE--KKLRRNQNYFNILR------FLVLGDkKLSPFNITHRfTHLFWLGDLNYRVELPNTEAE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 419 ALVE---MHDWKTLLENDQLCIEQRQGRVFEGWNEGKIYFPPTYKYSNNS-DRYAGDDRRSK-QKRRTPAWCDRILWYGR 493
Cdd:cd09100   198 NIIQkikQQQYQELLPHDQLLIERKESKVFLQFEEEEITFAPTYRFERGTrERYAYTKQKATgMKYNLPSWCDRVLWKSY 277

                         250       260
                  ....*....|....*....|....*...
gi 2027456844 494 GL-HQLSYVRGESR---FSDHRPVYSMF 517
Cdd:cd09100   278 PLvHVVCQSYGCTDditTSDHSPVFATF 305
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 289-517 2.01e-34

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: 131.99  E-value: 2.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 289 YSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKdgDELRRNS 368
Cdd:cd09091    74 YKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSE--KKLRRNQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 369 DVMEILRktrfppVHDIGD-EYSPQTI-LEHDRIIWLGDLNYRIALSYRAAKALV---EMHDWKTLLENDQLCIEQRQGR 443
Cdd:cd09091   152 NYLNILR------FLSLGDkKLSAFNItHRFTHLFWLGDLNYRLDLPIQEAENIIqkiEQQQFEPLLRHDQLNLEREEHK 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 444 VFEGWNEGKIYFPPTYKYSNNS-DRYAGDDRRSK-QKRRTPAWCDRILWYGRGL-HQLSYVRGESR---FSDHRPVYSMF 517
Cdd:cd09091   226 VFLRFSEEEITFPPTYRYERGSrDTYAYTKQKATgVKYNLPSWCDRILWKSYPEtHIICQSYGCTDdivTSDHSPVFGTF 305
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 289-517 1.48e-30

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: 121.23  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 289 YSLVASKQMVGVFLTVWVKSDIRDDVHNMKVSCVGRGLMGYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDelRRNS 368
Cdd:cd09101    74 YQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTH--RRNQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 369 DVMEILRKTrfppvhDIGDEY--SPQTILEHDRIIWLGDLNYRIALSYRAAKALVEMHDWKTLLENDQLCIEQRQGRVFE 446
Cdd:cd09101   152 NYLDILRSL------SLGDKQlnAFDISLRFTHLFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFL 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027456844 447 GWNEGKIYFPPTYKYSNNS-DRYAGDDRRSKQKR-RTPAWCDRILWYGRGLHQL---SY-VRGESRFSDHRPVYSMF 517
Cdd:cd09101   226 RFREEEISFPPTYRYERGSrDTYMWQKQKTTGMRtNVPSWCDRILWKSYPETHIvcnSYgCTDDIVTSDHSPVFGTF 302
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 425-521 2.33e-04

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: 43.61  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 425 DWKTLLENDQLCIEQRQGRVFEGwnegKIYFPPTYKYSNnsdryagDDRRSKQ--KRRTPAWCDRILWYgrglHQLSYVR 502
Cdd:cd09092   288 NNGKALLKFDKELEVFKDVLYEL----DISFPPSYPYSE-------DPEQGTQymNTRCPAWCDRILMS----HSARELK 352

                          90
                  ....*....|....*....
gi 2027456844 503 GESrfSDHRPVYSMFLAEV 521
Cdd:cd09092   353 SEN--EEKSVTYDMIGPNV 369
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 328-514 5.05e-04

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 42.08  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 328 GYLGNKGSISISMSLHQTSFCFICSHLTSGQKDGDElrRNSDVMEILRKTRFPPVHdigdeyspqtilEHDRIIWLGDLN 407
Cdd:cd08372    91 GDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADV--RDAQLKEVLEFLKRLRQP------------NSAPVVICGDFN 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027456844 408 YRIALSYRaakalvemhdwktllENDQLCIEQRQGRVFEGWNEgKIYFPPTYKYsnnsdryagddrrskQKRRTPAWCDR 487
Cdd:cd08372   157 VRPSEVDS---------------ENPSSMLRLFVALNLVDSFE-TLPHAYTFDT---------------YMHNVKSRLDY 205

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2027456844 488 ILwyGRGLHQLSYVRGESRF--------SDHRPVY 514
Cdd:cd08372   206 IF--VSKSLLPSVKSSKILSdaararipSDHYPIE 238
 
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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