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Conserved domains on  [gi|62078453|ref|NP_001013881|]
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inositol polyphosphate 5-phosphatase K [Rattus norvegicus]

Protein Classification

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 ...
 17-317 3.57e-149

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 cd09094:

Pssm-ID: 469791  Cd Length: 300  Bit Score: 426.02  E-value: 3.57e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNLDIYIIGLQEMNYGIISLLSDAAFEDPWSSFFMDMLSPLNLVKISQVRM 96
Cdd:cd09094   1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  97 QGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLTF 176
Cdd:cd09094  81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 177 EGYDVPNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPPTYKFDRHS 256
Cdd:cd09094 161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62078453 257 NNYDTSEKKRKPAWTDRILWRLKrqPAKANPSGFL-LTQKDYVSHMTYSISDHKPVTGTFDL 317
Cdd:cd09094 241 DEYDTSGKKRKPAWTDRILWKVN--PDASTEEKFLsITQTSYKSHMEYGISDHKPVTAQFRL 300
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 328-428 1.02e-38

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


:

Pssm-ID: 465482  Cd Length: 102  Bit Score: 135.45  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453   328 ITMMPEYLWT-KENDMLINYTSTPEFLSSPWDWIGLYKVGMRHINDYVSYVWVGDNQVSRGNNPNQVYINISAIP-DTEE 405
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPkEPEG 80

                          90       100
                  ....*....|....*....|...
gi 62078453   406 QFLLCYYSnNLHSIVGISQPFKI 428
Cdd:pfam17751  81 FYQFCYVS-NLGSVVGISTPFQF 102
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 17-317 3.57e-149

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: 426.02  E-value: 3.57e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNLDIYIIGLQEMNYGIISLLSDAAFEDPWSSFFMDMLSPLNLVKISQVRM 96
Cdd:cd09094   1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  97 QGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLTF 176
Cdd:cd09094  81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 177 EGYDVPNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPPTYKFDRHS 256
Cdd:cd09094 161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62078453 257 NNYDTSEKKRKPAWTDRILWRLKrqPAKANPSGFL-LTQKDYVSHMTYSISDHKPVTGTFDL 317
Cdd:cd09094 241 DEYDTSGKKRKPAWTDRILWKVN--PDASTEEKFLsITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 16-320 2.83e-119

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 350.50  E-value: 2.83e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453     16 MLSIHVVTWNVASAA-PTVDLSDLLQLN---NEDLNLDIYIIGLQEMNYGI--ISLLSDAAFEDPWSSFFMDMLSP-LNL 88
Cdd:smart00128   2 DIKVLIGTWNVGGLEsPKVDVTSWLFQKievKQSEKPDIYVIGLQEVVGLApgVILETIAGKERLWSDLLESSLNGdGQY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453     89 VKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFD 168
Cdd:smart00128  82 NVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDYK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453    169 RILESLTFEGYDVPNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPP 248
Cdd:smart00128 162 TILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFPP 241

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078453    249 TYKFDR-HSNNYDTSEKKRKPAWTDRILWRLKrqpakanpSGFLLTQKDYVSHMTYSISDHKPVTGTFDLELN 320
Cdd:smart00128 242 TYKYDSvGTETYDTSEKKRVPAWCDRILYRSN--------GPELIQLSEYHSGMEITTSDHKPVFATFRLKVT 306
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
17-317 7.05e-48

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 170.35  E-value: 7.05e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNL-DIYIIGLQE---MNYGIISLLSDAAFEDPWSSFFMDMLSPL----NL 88
Cdd:COG5411  30 VSIFVSTFNPPGKPPKASTKRWLFPEIEATELaDLYVVGLQEvveLTPGSILSADPYDRLRIWESKVLDCLNGAqsdeKY 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  89 VKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFD 168
Cdd:COG5411 110 SLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYR 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 169 RILESLTFEGYDvpNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRY-KELWEKDQLFIAKKQDQLLREFQEGPLLFP 247
Cdd:COG5411 190 SIASNICFSRGL--RIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGRlDKLFEYDQLLWEMEVGNVFPGFKEPVITFP 267

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 248 PTYKFDRHSNNYDTSEKKRKPAWTDRILWRlkrqpakanpsGFLLTQKDYVSHMTYSISDHKPVTGTFDL 317
Cdd:COG5411 268 PTYKFDYGTDEYDTSDKGRIPSWTDRILYK-----------SEQLTPHSYSSIPHLMISDHRPVYATFRA 326
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 328-428 1.02e-38

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


Pssm-ID: 465482  Cd Length: 102  Bit Score: 135.45  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453   328 ITMMPEYLWT-KENDMLINYTSTPEFLSSPWDWIGLYKVGMRHINDYVSYVWVGDNQVSRGNNPNQVYINISAIP-DTEE 405
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPkEPEG 80

                          90       100
                  ....*....|....*....|...
gi 62078453   406 QFLLCYYSnNLHSIVGISQPFKI 428
Cdd:pfam17751  81 FYQFCYVS-NLGSVVGISTPFQF 102
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 89-319 1.15e-26

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 112.69  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453   89 VKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQ------ 162
Cdd:PLN03191 365 VRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrrnad 444

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  163 -----RLEHFDRILESltfegyDVP-NILDHDLILWFGDMNFRIEDFGLLfVQECITKKRYKELWEKDQLFIAKKQDQLL 236
Cdd:PLN03191 445 vyeiiRRTRFSSVLDT------DQPqTIPSHDQIFWFGDLNYRLNMLDTE-VRKLVAQKRWDELINSDQLIKELRSGHVF 517

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  237 REFQEGPLLFPPTYKFDRHSNNY-----DTSEKKRKPAWTDRILWRLKRqpakanpsgflLTQKDYvSHMTYSISDHKPV 311
Cdd:PLN03191 518 DGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKG-----------IKQLCY-KRSEIRLSDHRPV 585


                 ....*...
gi 62078453  312 TGTFDLEL 319
Cdd:PLN03191 586 SSMFLVEV 593
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 17-317 3.57e-149

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: 426.02  E-value: 3.57e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNLDIYIIGLQEMNYGIISLLSDAAFEDPWSSFFMDMLSPLNLVKISQVRM 96
Cdd:cd09094   1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  97 QGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLTF 176
Cdd:cd09094  81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 177 EGYDVPNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPPTYKFDRHS 256
Cdd:cd09094 161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62078453 257 NNYDTSEKKRKPAWTDRILWRLKrqPAKANPSGFL-LTQKDYVSHMTYSISDHKPVTGTFDL 317
Cdd:cd09094 241 DEYDTSGKKRKPAWTDRILWKVN--PDASTEEKFLsITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 16-320 2.83e-119

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 350.50  E-value: 2.83e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453     16 MLSIHVVTWNVASAA-PTVDLSDLLQLN---NEDLNLDIYIIGLQEMNYGI--ISLLSDAAFEDPWSSFFMDMLSP-LNL 88
Cdd:smart00128   2 DIKVLIGTWNVGGLEsPKVDVTSWLFQKievKQSEKPDIYVIGLQEVVGLApgVILETIAGKERLWSDLLESSLNGdGQY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453     89 VKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFD 168
Cdd:smart00128  82 NVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDYK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453    169 RILESLTFEGYDVPNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPP 248
Cdd:smart00128 162 TILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFPP 241

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078453    249 TYKFDR-HSNNYDTSEKKRKPAWTDRILWRLKrqpakanpSGFLLTQKDYVSHMTYSISDHKPVTGTFDLELN 320
Cdd:smart00128 242 TYKYDSvGTETYDTSEKKRVPAWCDRILYRSN--------GPELIQLSEYHSGMEITTSDHKPVFATFRLKVT 306
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 17-317 9.29e-85

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: 261.88  E-value: 9.29e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASA-APTVDLSDLLQLNNEDLNlDIYIIGLQEM---NYGIISLLsDAAFEDPWSSFFMDMLSPL-NLVKI 91
Cdd:cd09074   1 VKIFVVTWNVGGGiSPPENLENWLSPKGTEAP-DIYAVGVQEVdmsVQGFVGND-DSAKAREWVDNIQEALNEKeNYVLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  92 SQVRMQGLLLLVFAKYQHLPYIQIISTKSIP--TGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDR 169
Cdd:cd09074  79 GSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTvgTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVERRNQDYRD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 170 ILESLTFEGYDVP--NILDHDLILWFGDMNFRIeDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFP 247
Cdd:cd09074 159 ILSKLKFYRGDPAidSIFDHDVVFWFGDLNYRI-DSTDDEVRKLISQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFP 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 248 PTYKFDRHSNNYDTSEKKRKPAWTDRILWRLKRqpakanpsGFLLTQKDYVSHMTYSISDHKPVTGTFDL 317
Cdd:cd09074 238 PTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKA--------GSEIQPLSYTSVPLYKTSDHKPVRATFRV 299
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 17-316 7.08e-83

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: 256.86  E-value: 7.08e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSdlLQLNNEDLNLDIYIIGLQEMNYGIISLL-SDAAFEDPWSSFFMDMLSPLN-LVKISQV 94
Cdd:cd09093   1 FRIFVGTWNVNGQSPDESLR--PWLSCDEEPPDIYAIGFQELDLSAEAFLfNDSSREQEWVKAVERGLHPDAkYKKVKLI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  95 RMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESL 174
Cdd:cd09093  79 RLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRNQDYKDICARM 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 175 TFEGYDVP--NILDHDLILWFGDMNFRIEDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPPTYKF 252
Cdd:cd09093 159 KFEDPDGPplSISDHDVVFWLGDLNYRIQELPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINFIPTYKY 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62078453 253 DRHSNNYDTSEKKRKPAWTDRILWRlkrqpakanpsGFLLTQKDYVSHMTYSISDHKPVTGTFD 316
Cdd:cd09093 239 DPGTDNWDSSEKCRAPAWCDRILWR-----------GTNIVQLSYRSHMELKTSDHKPVSALFD 291
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 17-315 4.95e-60

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: 197.56  E-value: 4.95e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNLDIYIIGLQE---MNYGIIsLLSDAAFEDPWSSFFMDMLSPLNLVKISQ 93
Cdd:cd09090   1 INIFVGTFNVNGKSYKDDLSSWLFPEENDELPDIVVIGLQEvveLTAGQI-LNSDPSKSSFWEKKIKTTLNGRGGEKYVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  94 VR---MQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRI 170
Cdd:cd09090  80 LRseqLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEERNNDYKTI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 171 LESLTF-EGYDVPnilDHDLILWFGDMNFRI----EDfgllfVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLL 245
Cdd:cd09090 160 ARGLRFsRGRTIK---DHDHVIWLGDFNYRIsltnED-----VRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPIT 231

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 246 FPPTYKFDRHSNNYDTSEKKRKPAWTDRILWRlkrqpakanpsGFLLTQKDYVSHMTYsISDHKPVTGTF 315
Cdd:cd09090 232 FPPTYKYDKGTDNYDTSEKQRIPAWTDRILYR-----------GENLRQLSYNSAPLR-FSDHRPVYATF 289
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 49-316 4.13e-53

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: 180.67  E-value: 4.13e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  49 DIYIIGLQEM---NYG-IISLLSDAAFEdpWSSFFMDMLSPLN-LVKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPT 123
Cdd:cd09089  52 DIFAIGFEEMvdlNASnIVSASTTNQKE--WGEELQKTISRDHkYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKT 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 124 GLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLTFE-GYdvpNILDHDLILWFGDMNFRIeD 202
Cdd:cd09089 130 GLGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQVKERNEDFAEIARKLSFPmGR---TLDSHDYVFWCGDFNYRI-D 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 203 FGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPPTYKFDRHSNNYDTSEKKRKPAWTDRILWRLKRQP 282
Cdd:cd09089 206 LPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWP 285

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62078453 283 AKANPSGFLLTQKDYVSHMT---Y-----SISDHKPVTGTFD 316
Cdd:cd09089 286 SDKTEESLVETNDPTWNPGTllyYgraelKTSDHRPVVAIID 327
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
17-317 7.05e-48

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 170.35  E-value: 7.05e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNL-DIYIIGLQE---MNYGIISLLSDAAFEDPWSSFFMDMLSPL----NL 88
Cdd:COG5411  30 VSIFVSTFNPPGKPPKASTKRWLFPEIEATELaDLYVVGLQEvveLTPGSILSADPYDRLRIWESKVLDCLNGAqsdeKY 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  89 VKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFD 168
Cdd:COG5411 110 SLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYR 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 169 RILESLTFEGYDvpNILDHDLILWFGDMNFRIEDFGLLFVQECITKKRY-KELWEKDQLFIAKKQDQLLREFQEGPLLFP 247
Cdd:COG5411 190 SIASNICFSRGL--RIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGRlDKLFEYDQLLWEMEVGNVFPGFKEPVITFP 267

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 248 PTYKFDRHSNNYDTSEKKRKPAWTDRILWRlkrqpakanpsGFLLTQKDYVSHMTYSISDHKPVTGTFDL 317
Cdd:COG5411 268 PTYKFDYGTDEYDTSDKGRIPSWTDRILYK-----------SEQLTPHSYSSIPHLMISDHRPVYATFRA 326
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 48-317 3.95e-41

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: 149.42  E-value: 3.95e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  48 LDIYIIGLQEM---NYGIISLLSDAAfEDPWSSFFMDMLSPLN-LVKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPT 123
Cdd:cd09098  50 VDIFAIGFEEMvelNAGNIVSASTTN-QKLWAAELQKTISRDQkYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKT 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 124 GLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLTFEGYDVpnILDHDLILWFGDMNFRIeDF 203
Cdd:cd09098 129 GMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRM--LFSHDYVFWCGDFNYRI-DI 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 204 GLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQEGPLLFPPTYKFDRHSNNYDTSEKKRKPAWTDRILWRLKRQP- 282
Cdd:cd09098 206 PNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPf 285

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62078453 283 ------AKANPSGFLLTQKD----------YVSHMTYSISDHKPVTGTFDL 317
Cdd:cd09098 286 drsaedLDLLNASFPDNSKEqytwspgtllHYGRAELKTSDHRPVVALIDI 336
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 23-311 1.51e-39

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: 145.16  E-value: 1.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  23 TWNV-------ASAAPTVDLSDLL----QL-------NNEDLNLDIYIIGLQEM---NYGIISLLSDAAfEDPWSSFFMD 81
Cdd:cd09099   7 TWNVnggkqfrSNILGTSELTDWLldspKLsgtpdfqDDESNPPDIFAVGFEEMvelSAGNIVNASTTN-RKMWGEQLQK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  82 MLSPLN-LVKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNN 160
Cdd:cd09099  86 AISRSHrYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQV 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 161 DQRLEHFDRILESLTFEGYDvpNILDHDLILWFGDMNFRIeDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREFQ 240
Cdd:cd09099 166 KERNEDYKEITQKLSFPMGR--NVFSHDYVFWCGDFNYRI-DLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKDFH 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 241 EGPLLFPPTYKFDRHSNNYDTSEKKRKPAWTDRILWRLKRQPAKANPSGFLLTQKD-----------------YVSHMTY 303
Cdd:cd09099 243 EGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWRKKWPFEKTAGEINLLDSDldfdtkirhtwtpgalmYYGRAEL 322


                ....*...
gi 62078453 304 SISDHKPV 311
Cdd:cd09099 323 QASDHRPV 330
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 328-428 1.02e-38

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


Pssm-ID: 465482  Cd Length: 102  Bit Score: 135.45  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453   328 ITMMPEYLWT-KENDMLINYTSTPEFLSSPWDWIGLYKVGMRHINDYVSYVWVGDNQVSRGNNPNQVYINISAIP-DTEE 405
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPkEPEG 80

                          90       100
                  ....*....|....*....|...
gi 62078453   406 QFLLCYYSnNLHSIVGISQPFKI 428
Cdd:pfam17751  81 FYQFCYVS-NLGSVVGISTPFQF 102
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 17-317 3.87e-37

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: 3.87e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVAS-AAPTVDLSDLLQLNNEDLNLDIYIIGLQEMnygiisllSDAAFEdpWSSFFMDMLSPlNLVKISQVR 95
Cdd:cd09095   5 VGIFVATWNMQGqKELPENLDDFLLPTSADFAQDIYVIGVQEG--------CSDRRE--WEIRLQETLGP-SHVLLHSAS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  96 MQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLT 175
Cdd:cd09095  74 HGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYNKIIQALN 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 176 FEG--------YDVPNILDH-DLILWFGDMNFRIEDFGLLFVQECITKKR--YKELWEKDQLFIAKKQDQLLREFQEGPL 244
Cdd:cd09095 154 LPRnvptnpykSESGDVTTRfDEVFWFGDFNFRLSGPRHLVDALINQGQEvdVSALLQHDQLTREMSKGSIFKGFQEAPI 233

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078453 245 LFPPTYKFDRHSNNYDTSEKKRKPAWTDRILWRlKRQPAKANPSgflltqkDYVSHMTYSISDHKPVTGTFDL 317
Cdd:cd09095 234 HFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYR-SRQKGDVCCL-------KYNSCPSIKTSDHRPVFALFRV 298
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 17-316 6.65e-33

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: 126.21  E-value: 6.65e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNLD---------IYIIGLQEmnygiisllsDAAFEDPWSSFFMDMLSPLN 87
Cdd:cd09091   1 ISIFIGTWNMGSAPPPKNITSWFTSKGQGKTRDdvadyiphdIYVIGTQE----------DPLGEKEWLDLLRHSLKELT 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  88 LVKISQVRMQGLL---LLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRL 164
Cdd:cd09091  71 SLDYKPIAMQTLWnirIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRN 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 165 EHFDRILESLTF-----EGYDVPNILDHdlILWFGDMNFRIEdfglLFVQEC---ITKKR---YKELWEKDQLFIAKKQD 233
Cdd:cd09091 151 QNYLNILRFLSLgdkklSAFNITHRFTH--LFWLGDLNYRLD----LPIQEAeniIQKIEqqqFEPLLRHDQLNLEREEH 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 234 QLLREFQEGPLLFPPTYKFDRHSNNYDTSEKKRK-------PAWTDRILWrlkrqpaKANPSGFLLTQKdYVSHMTYSIS 306
Cdd:cd09091 225 KVFLRFSEEEITFPPTYRYERGSRDTYAYTKQKAtgvkynlPSWCDRILW-------KSYPETHIICQS-YGCTDDIVTS 296

                       330
                ....*....|
gi 62078453 307 DHKPVTGTFD 316
Cdd:cd09091 297 DHSPVFGTFE 306
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 17-317 4.29e-32

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: 123.93  E-value: 4.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNEDLNLD---------IYIIGLQEMNYGiisllsdaafEDPWSSFFMDMLSPLN 87
Cdd:cd09101   1 ISIFIGTWNMGSVPPPKSLASWLTSRGLGKTLDettvtiphdIYVFGTQENSVG----------DREWVDFLRASLKELT 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  88 LVKISQVRMQGLL---LLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRL 164
Cdd:cd09101  71 DIDYQPIALQCLWnikMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTHRRN 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 165 EHFDRILESLTF-----EGYDVPNILDHdlILWFGDMNFRIeDFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLREF 239
Cdd:cd09101 151 QNYLDILRSLSLgdkqlNAFDISLRFTH--LFWFGDLNYRL-DMDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRF 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 240 QEGPLLFPPTYKFDRHSNNYDTSEKKRK-------PAWTDRILWrlkrqpaKANPSGFLLTQKdYVSHMTYSISDHKPVT 312
Cdd:cd09101 228 REEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILW-------KSYPETHIVCNS-YGCTDDIVTSDHSPVF 299


                ....*
gi 62078453 313 GTFDL 317
Cdd:cd09101 300 GTFEV 304
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 17-317 4.27e-31

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: 121.25  E-value: 4.27e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  17 LSIHVVTWNVASAAPTVDLSDLLQLNNED---------LNLDIYIIGLQEmnygiisllsDAAFEDPWSSFFMDMLSPLN 87
Cdd:cd09100   1 ITIFIGTWNMGNAPPPKKITSWFQCKGQGktrddtadyIPHDIYVIGTQE----------DPLGEKEWLDTLKHSLREIT 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  88 LVKISQVRMQGLL---LLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRL 164
Cdd:cd09100  71 SISFKVIAIQTLWnirIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRN 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 165 EHFDRILESLTF-----EGYDVPNILDHdlILWFGDMNFRIE--DFGLLFVQECITKKRYKELWEKDQLFIAKKQDQLLR 237
Cdd:cd09100 151 QNYFNILRFLVLgdkklSPFNITHRFTH--LFWLGDLNYRVElpNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFL 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 238 EFQEGPLLFPPTYKFDR-------HSNNYDTSEKKRKPAWTDRILWrlkrqpaKANPSGFLLTQKdYVSHMTYSISDHKP 310
Cdd:cd09100 229 QFEEEEITFAPTYRFERgtreryaYTKQKATGMKYNLPSWCDRVLW-------KSYPLVHVVCQS-YGCTDDITTSDHSP 300


                ....*..
gi 62078453 311 VTGTFDL 317
Cdd:cd09100 301 VFATFEV 307
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 89-319 1.15e-26

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 112.69  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453   89 VKISQVRMQGLLLLVFAKYQHLPYIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQ------ 162
Cdd:PLN03191 365 VRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrrnad 444

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  163 -----RLEHFDRILESltfegyDVP-NILDHDLILWFGDMNFRIEDFGLLfVQECITKKRYKELWEKDQLFIAKKQDQLL 236
Cdd:PLN03191 445 vyeiiRRTRFSSVLDT------DQPqTIPSHDQIFWFGDLNYRLNMLDTE-VRKLVAQKRWDELINSDQLIKELRSGHVF 517

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  237 REFQEGPLLFPPTYKFDRHSNNY-----DTSEKKRKPAWTDRILWRLKRqpakanpsgflLTQKDYvSHMTYSISDHKPV 311
Cdd:PLN03191 518 DGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKG-----------IKQLCY-KRSEIRLSDHRPV 585


                 ....*...
gi 62078453  312 TGTFDLEL 319
Cdd:PLN03191 586 SSMFLVEV 593
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 21-312 1.27e-08

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: 55.57  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453  21 VVTWNVASAAPTVDLSDLLQLNNEdlnLDIYIIGLQEMNYGIISLLSDAAFEDPWSSFFmdmLSPLNLVKISQvrmqGLL 100
Cdd:cd08372   1 VASYNVNGLNAATRASGIARWVRE---LDPDIVCLQEVKDSQYSAVALNQLLPEGYHQY---QSGPSRKEGYE----GVA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 101 LLVFAKyqhlpyIQIISTKSIPTGLYGYWGNKGGINICLKLYGYYVSIVNCHLPPHMYNNDQRLEHFDRILESLTFEGYD 180
Cdd:cd08372  71 ILSKTP------KFKIVEKHQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKRLRQP 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 181 VpnildHDLILWFGDMNFRIEDFGLLFVQECITKK---RYKELWEKdqlfiakkqdqllrefqegpLLFPPTYKFDRHsn 257
Cdd:cd08372 145 N-----SAPVVICGDFNVRPSEVDSENPSSMLRLFvalNLVDSFET--------------------LPHAYTFDTYMH-- 197

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62078453 258 nydtsekkRKPAWTDRILWRLKrqpAKANPSGFLLTQKDYVSHMtysISDHKPVT 312
Cdd:cd08372 198 --------NVKSRLDYIFVSKS---LLPSVKSSKILSDAARARI---PSDHYPIE 238
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 129-317 6.23e-06

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: 48.23  E-value: 6.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 129 WGNKGGINICLKLYGYYVSIVNCHL------------PPHMYNNDqRLEHFDRILESLTFEGYD-VPNILdhdlilwFGD 195
Cdd:cd09092 152 WSRKGFMRTRWKINNCVFDLVNIHLfhdasnlaacesSPSVYSQN-RHRALGYVLERLTDERFEkVPFFV-------FGD 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 196 MNFRIEDFGLL----------FVQECITKKRYKELWEKDQ------LFIAKK------QDQLL-----------REFQ-- 240
Cdd:cd09092 224 FNFRLDTKSVVetlcakatmqTVRKADSNIVVKLEFREKDndnkvvLQIEKKkfdyfnQDVFRdnngkallkfdKELEvf 303

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078453 241 -----EGPLLFPPTYKFDRHSNNYDTSEKKRKPAWTDRILwrlkrqpakANPSGFLLTQKDYVSHMTYS-------ISDH 308
Cdd:cd09092 304 kdvlyELDISFPPSYPYSEDPEQGTQYMNTRCPAWCDRIL---------MSHSARELKSENEEKSVTYDmigpnvcMGDH 374


                ....*....
gi 62078453 309 KPVTGTFDL 317
Cdd:cd09092 375 KPVFLTFRI 383
 
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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