NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|50726960|ref|NP_001002837|]
View 

phosphatidylinositol 4,5-bisphosphate 5-phosphatase A isoform c [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 56-362 0e+00

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: 545.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGadMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVR 135
Cdd:cd09094   2 RVYVVTWNVATAPPPIDVRSLLGLQSPEVAPD--IYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 136 MQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQ 215
Cdd:cd09094  80 LQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 216 FQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVG 295
Cdd:cd09094 160 FNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLG 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50726960 296 TNKYDTSAKKRKPAWTDRILWKVKAPGGGPspsgrkSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLL 362
Cdd:cd09094 240 TDEYDTSGKKRKPAWTDRILWKVNPDASTE------EKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 373-471 2.04e-35

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: 128.90  E-value: 2.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960   373 VRLEVADEW-VRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDG--NTYQVTFSEESLPK-GHG 448
Cdd:pfam17751   1 VVFQNVGEWyPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGsnSVRQVLFKASYLPKePEG 80

                          90       100
                  ....*....|....*....|...
gi 50726960   449 DFILGYYSHNHSIlIGITEPFQI 471
Cdd:pfam17751  81 FYQFCYVSNLGSV-VGISTPFQF 102
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 56-362 0e+00

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: 545.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGadMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVR 135
Cdd:cd09094   2 RVYVVTWNVATAPPPIDVRSLLGLQSPEVAPD--IYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 136 MQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQ 215
Cdd:cd09094  80 LQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 216 FQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVG 295
Cdd:cd09094 160 FNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLG 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50726960 296 TNKYDTSAKKRKPAWTDRILWKVKAPGGGPspsgrkSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLL 362
Cdd:cd09094 240 TDEYDTSGKKRKPAWTDRILWKVNPDASTE------EKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 56-360 3.30e-89

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 279.62  E-value: 3.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960     56 RITVVTWNVGTAMPPD-DVTSLLHLGGGDDSDGAD-MIAIGLQEVNSM--LNKRLKDALFTDQWSELFMDAL-GPFNFVL 130
Cdd:smart00128   4 KVLIGTWNVGGLESPKvDVTSWLFQKIEVKQSEKPdIYVIGLQEVVGLapGVILETIAGKERLWSDLLESSLnGDGQYNV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960    131 VSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTI 210
Cdd:smart00128  84 LAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDYKTI 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960    211 LSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTF 290
Cdd:smart00128 164 LRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFPPTY 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50726960    291 KFDV-GTNKYDTSAKKRKPAWTDRILWKVKAPgggpspsgrkshrlQVTQHS-YRSHMEYTVSDHKPVAAQF 360
Cdd:smart00128 244 KYDSvGTETYDTSEKKRVPAWCDRILYRSNGP--------------ELIQLSeYHSGMEITTSDHKPVFATF 301
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
93-375 3.39e-45

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 167.27  E-value: 3.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  93 IGLQEV-----NSMLNKRLKDALftDQWSELFMD----ALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRT 163
Cdd:COG5411  67 VGLQEVveltpGSILSADPYDRL--RIWESKVLDclngAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKT 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 164 GLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIES- 242
Cdd:COG5411 145 GFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICF--SRGLRIYDHDTIFWLGDLNYRVTSt 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 243 YDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILwkvkapg 322
Cdd:COG5411 223 NEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRIL------- 295

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 50726960 323 ggpspsGRKShrlQVTQHSYRSHMEYTVSDHKPVAAQFLLQFAFRDDMPLVRL 375
Cdd:COG5411 296 ------YKSE---QLTPHSYSSIPHLMISDHRPVYATFRAKIKVVDPSKKEGL 339
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 373-471 2.04e-35

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: 128.90  E-value: 2.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960   373 VRLEVADEW-VRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDG--NTYQVTFSEESLPK-GHG 448
Cdd:pfam17751   1 VVFQNVGEWyPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGsnSVRQVLFKASYLPKePEG 80

                          90       100
                  ....*....|....*....|...
gi 50726960   449 DFILGYYSHNHSIlIGITEPFQI 471
Cdd:pfam17751  81 FYQFCYVSNLGSV-VGISTPFQF 102
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 164-387 5.29e-34

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 137.35  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  164 GLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPA-HMDKAEQRKD----------NFQTILSLQQfqgpgAQGILDHDLVFW 232
Cdd:PLN03191 400 GLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRRNadvyeiirrtRFSSVLDTDQ-----PQTIPSHDQIFW 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  233 FGDLNFRIESYDLHFVKFaIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKY-----DTSAKKRK 307
Cdd:PLN03191 475 FGDLNYRLNMLDTEVRKL-VAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRS 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  308 PAWTDRILWKVKApgggpspsgrkshrlqVTQHSYRsHMEYTVSDHKPVAAQFLLQFAFRDDMPLVR-LEV---ADEWVR 383
Cdd:PLN03191 554 PAWCDRILWLGKG----------------IKQLCYK-RSEIRLSDHRPVSSMFLVEVEVFDHRKLQRaLNVnsaAASAVH 616


                 ....
gi 50726960  384 PEQA 387
Cdd:PLN03191 617 PEPS 620
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 56-362 0e+00

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: 545.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGadMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVR 135
Cdd:cd09094   2 RVYVVTWNVATAPPPIDVRSLLGLQSPEVAPD--IYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 136 MQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQ 215
Cdd:cd09094  80 LQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 216 FQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVG 295
Cdd:cd09094 160 FNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLG 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50726960 296 TNKYDTSAKKRKPAWTDRILWKVKAPGGGPspsgrkSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLL 362
Cdd:cd09094 240 TDEYDTSGKKRKPAWTDRILWKVNPDASTE------EKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 56-362 5.44e-123

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: 366.27  E-value: 5.44e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNVGTAM-PPDDVTSLLHLGGGDDSDgadMIAIGLQEVNSMLN--KRLKDALFTDQWSELFMDALGP-FNFVLV 131
Cdd:cd09074   2 KIFVVTWNVGGGIsPPENLENWLSPKGTEAPD---IYAVGVQEVDMSVQgfVGNDDSAKAREWVDNIQEALNEkENYVLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 132 SSVRMQGVILLLFAKYYHLPFLRDVQTDCTR--TGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQT 209
Cdd:cd09074  79 GSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTvgTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVERRNQDYRD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 210 ILSLQQFQGPG--AQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDqLHQLWEKDQLNMAKNTWPILKGFQEGPLNFA 287
Cdd:cd09074 159 ILSKLKFYRGDpaIDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGD-LDDLLEKDQLKKQKEKGKVFDGFQELPITFP 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50726960 288 PTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGggpspsgrkshrlQVTQHSYRSHMEYTVSDHKPVAAQFLL 362
Cdd:cd09074 238 PTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGS-------------EIQPLSYTSVPLYKTSDHKPVRATFRV 299
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 56-360 3.30e-89

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 279.62  E-value: 3.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960     56 RITVVTWNVGTAMPPD-DVTSLLHLGGGDDSDGAD-MIAIGLQEVNSM--LNKRLKDALFTDQWSELFMDAL-GPFNFVL 130
Cdd:smart00128   4 KVLIGTWNVGGLESPKvDVTSWLFQKIEVKQSEKPdIYVIGLQEVVGLapGVILETIAGKERLWSDLLESSLnGDGQYNV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960    131 VSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTI 210
Cdd:smart00128  84 LAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDYKTI 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960    211 LSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTF 290
Cdd:smart00128 164 LRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFPPTY 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50726960    291 KFDV-GTNKYDTSAKKRKPAWTDRILWKVKAPgggpspsgrkshrlQVTQHS-YRSHMEYTVSDHKPVAAQF 360
Cdd:smart00128 244 KYDSvGTETYDTSEKKRVPAWCDRILYRSNGP--------------ELIQLSeYHSGMEITTSDHKPVFATF 301
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 56-360 3.48e-85

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: 268.41  E-value: 3.48e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNVGTAMPPDDVTSLLHLGGGDDSdgadMIAIGLQEVNsmLNKrlKDALFTD-----QWSELFMDALGPFN-FV 129
Cdd:cd09093   2 RIFVGTWNVNGQSPDESLRPWLSCDEEPPD----IYAIGFQELD--LSA--EAFLFNDssreqEWVKAVERGLHPDAkYK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 130 LVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQT 209
Cdd:cd09093  74 KVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRNQDYKD 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 210 ILSLQQF--QGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFA 287
Cdd:cd09093 154 ICARMKFedPDGPPLSISDHDVVFWLGDLNYRIQELPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINFI 233

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50726960 288 PTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKapgggpspsgrkshrlQVTQHSYRSHMEYTVSDHKPVAAQF 360
Cdd:cd09093 234 PTYKYDPGTDNWDSSEKCRAPAWCDRILWRGT----------------NIVQLSYRSHMELKTSDHKPVSALF 290
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 56-360 3.95e-65

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: 216.05  E-value: 3.95e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNVGTAMPPDDVTSLLHlgGGDDSDGADMIAIGLQEV-----NSMLNKrlkDALFTDQWSELFMDAL---GPFN 127
Cdd:cd09090   2 NIFVGTFNVNGKSYKDDLSSWLF--PEENDELPDIVVIGLQEVveltaGQILNS---DPSKSSFWEKKIKTTLngrGGEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 128 FVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF 207
Cdd:cd09090  77 YVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEERNNDY 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 208 QTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIE-SYDLhfVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNF 286
Cdd:cd09090 157 KTIARGLRF--SRGRTIKDHDHVIWLGDFNYRISlTNED--VRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITF 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50726960 287 APTFKFDVGTNKYDTSAKKRKPAWTDRILwkvkapgggpspsgRKSHRLQvtQHSYRSHMEYtVSDHKPVAAQF 360
Cdd:cd09090 233 PPTYKYDKGTDNYDTSEKQRIPAWTDRIL--------------YRGENLR--QLSYNSAPLR-FSDHRPVYATF 289
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 128-360 5.43e-63

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: 211.48  E-value: 5.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 128 FVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF 207
Cdd:cd09089  94 YVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQVKERNEDF 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 208 QTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIE-SYDLhfVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNF 286
Cdd:cd09089 174 AEIARKLSF--PMGRTLDSHDYVFWCGDFNYRIDlPNDE--VKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINF 249

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50726960 287 APTFKFDVGTNKYDTSAKKRKPAWTDRILW---KVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQF 360
Cdd:cd09089 250 APTYKYDLFSDDYDTSEKCRTPAWTDRVLWrrrKWPSDKTEESLVETNDPTWNPGTLLYYGRAELKTSDHRPVVAII 326
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 90-358 2.53e-56

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: 194.08  E-value: 2.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  90 MIAIGLQEVNSMLNKRLKDALFTDQ--WSELFMDALG-PFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLG 166
Cdd:cd09099  52 IFAVGFEEMVELSAGNIVNASTTNRkmWGEQLQKAISrSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 167 GYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTIlsLQQFQGPGAQGILDHDLVFWFGDLNFRIE-SYDL 245
Cdd:cd09099 132 GKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQVKERNEDYKEI--TQKLSFPMGRNVFSHDYVFWCGDFNYRIDlTYEE 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 246 HFvkFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRIL-WKVKAP--- 321
Cdd:cd09099 210 VF--YFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLwWRKKWPfek 287

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 50726960 322 --------GGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAA 358
Cdd:cd09099 288 tageinllDSDLDFDTKIRHTWTPGALMYYGRAELQASDHRPVLA 332
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 90-358 1.93e-49

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: 175.61  E-value: 1.93e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  90 MIAIGLQEVNSMLNKRLKDALFTDQ--WS-ELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLG 166
Cdd:cd09098  52 IFAIGFEEMVELNAGNIVSASTTNQklWAaELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 167 GYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIESYDLH 246
Cdd:cd09098 132 GATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSF--PMGRMLFSHDYVFWCGDFNYRIDIPNEE 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 247 fVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKApgggpS 326
Cdd:cd09098 210 -VKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRK-----W 283

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 50726960 327 PSGRKSHRLQVTQHSYR--SHMEYT---------------VSDHKPVAA 358
Cdd:cd09098 284 PFDRSAEDLDLLNASFPdnSKEQYTwspgtllhygraelkTSDHRPVVA 332
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
93-375 3.39e-45

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 167.27  E-value: 3.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  93 IGLQEV-----NSMLNKRLKDALftDQWSELFMD----ALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRT 163
Cdd:COG5411  67 VGLQEVveltpGSILSADPYDRL--RIWESKVLDclngAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKT 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 164 GLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIES- 242
Cdd:COG5411 145 GFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICF--SRGLRIYDHDTIFWLGDLNYRVTSt 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 243 YDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILwkvkapg 322
Cdd:COG5411 223 NEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRIL------- 295

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 50726960 323 ggpspsGRKShrlQVTQHSYRSHMEYTVSDHKPVAAQFLLQFAFRDDMPLVRL 375
Cdd:COG5411 296 ------YKSE---QLTPHSYSSIPHLMISDHRPVYATFRAKIKVVDPSKKEGL 339
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 56-360 3.00e-42

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: 154.50  E-value: 3.00e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  56 RITVVTWNV-GTAMPPDDVTSLLhlGGGDDSDGADMIAIGLQEVNSmlNKRlkdalftdQWSELFMDALGPfNFVLVSSV 134
Cdd:cd09095   6 GIFVATWNMqGQKELPENLDDFL--LPTSADFAQDIYVIGVQEGCS--DRR--------EWEIRLQETLGP-SHVLLHSA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 135 RMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF-QTILSL 213
Cdd:cd09095  73 SHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYnKIIQAL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 214 Q-QFQGPG------AQGILDH-DLVFWFGDLNFRIeSYDLHFVKFAIDSDQ---LHQLWEKDQL--NMAKNTwpILKGFQ 280
Cdd:cd09095 153 NlPRNVPTnpykseSGDVTTRfDEVFWFGDFNFRL-SGPRHLVDALINQGQevdVSALLQHDQLtrEMSKGS--IFKGFQ 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 281 EGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGggpspsgrkshrlQVTQHSYRSHMEYTVSDHKPVAAQF 360
Cdd:cd09095 230 EAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSRQKG-------------DVCCLKYNSCPSIKTSDHRPVFALF 296
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 373-471 2.04e-35

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: 128.90  E-value: 2.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960   373 VRLEVADEW-VRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDG--NTYQVTFSEESLPK-GHG 448
Cdd:pfam17751   1 VVFQNVGEWyPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGsnSVRQVLFKASYLPKePEG 80

                          90       100
                  ....*....|....*....|...
gi 50726960   449 DFILGYYSHNHSIlIGITEPFQI 471
Cdd:pfam17751  81 FYQFCYVSNLGSV-VGISTPFQF 102
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 164-387 5.29e-34

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 137.35  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  164 GLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPA-HMDKAEQRKD----------NFQTILSLQQfqgpgAQGILDHDLVFW 232
Cdd:PLN03191 400 GLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRRNadvyeiirrtRFSSVLDTDQ-----PQTIPSHDQIFW 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  233 FGDLNFRIESYDLHFVKFaIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKY-----DTSAKKRK 307
Cdd:PLN03191 475 FGDLNYRLNMLDTEVRKL-VAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRS 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  308 PAWTDRILWKVKApgggpspsgrkshrlqVTQHSYRsHMEYTVSDHKPVAAQFLLQFAFRDDMPLVR-LEV---ADEWVR 383
Cdd:PLN03191 554 PAWCDRILWLGKG----------------IKQLCYK-RSEIRLSDHRPVSSMFLVEVEVFDHRKLQRaLNVnsaAASAVH 616


                 ....
gi 50726960  384 PEQA 387
Cdd:PLN03191 617 PEPS 620
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 57-360 9.56e-31

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: 122.36  E-value: 9.56e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  57 ITVVTWNVGTAMPPDDVTSLLH-------LGGGDDSDGADMIAIGLQEvnsmlnkrlkDALFTDQWSELFMDALGPFNFV 129
Cdd:cd09091   3 IFIGTWNMGSAPPPKNITSWFTskgqgktRDDVADYIPHDIYVIGTQE----------DPLGEKEWLDLLRHSLKELTSL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 130 LVSSVRMQ---GVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDN 206
Cdd:cd09091  73 DYKPIAMQtlwNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQN 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 207 FQTILslqQFQGPGAQGILDHDL------VFWFGDLNFRIE--SYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKG 278
Cdd:cd09091 153 YLNIL---RFLSLGDKKLSAFNIthrfthLFWLGDLNYRLDlpIQEAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFLR 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 279 FQEGPLNFAPTFKFDVGT-NKY------DTSAKKRKPAWTDRILWKvkapgggpspSGRKSHrlqVTQHSYRSHMEYTVS 351
Cdd:cd09091 230 FSEEEITFPPTYRYERGSrDTYaytkqkATGVKYNLPSWCDRILWK----------SYPETH---IICQSYGCTDDIVTS 296


                ....*....
gi 50726960 352 DHKPVAAQF 360
Cdd:cd09091 297 DHSPVFGTF 305
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 57-360 2.26e-29

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: 118.55  E-value: 2.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  57 ITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGAD-------MIAIGLQEvnsmlnkrlkDALFTDQWSELFMDAL---GPF 126
Cdd:cd09100   3 IFIGTWNMGNAPPPKKITSWFQCKGQGKTRDDTadyiphdIYVIGTQE----------DPLGEKEWLDTLKHSLreiTSI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 127 NFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDN 206
Cdd:cd09100  73 SFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQN 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 207 FQTILslqQFQGPGAQGILDHDL------VFWFGDLNFRIE--SYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKG 278
Cdd:cd09100 153 YFNIL---RFLVLGDKKLSPFNIthrfthLFWLGDLNYRVElpNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQ 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 279 FQEGPLNFAPTFKFDVGT-NKY------DTSAKKRKPAWTDRILWKvkapgggpspsgrKSHRLQVTQHSYRSHMEYTVS 351
Cdd:cd09100 230 FEEEEITFAPTYRFERGTrERYaytkqkATGMKYNLPSWCDRVLWK-------------SYPLVHVVCQSYGCTDDITTS 296


                ....*....
gi 50726960 352 DHKPVAAQF 360
Cdd:cd09100 297 DHSPVFATF 305
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 57-360 2.41e-27

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: 112.76  E-value: 2.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  57 ITVVTWNVGTAMPPDDVTSLL-------HLGGGDDSDGADMIAIGLQEvNSMLNKrlkdalftdQWSELFMDALGPFNFV 129
Cdd:cd09101   3 IFIGTWNMGSVPPPKSLASWLtsrglgkTLDETTVTIPHDIYVFGTQE-NSVGDR---------EWVDFLRASLKELTDI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 130 LVSSVRMQ---GVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDN 206
Cdd:cd09101  73 DYQPIALQclwNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTHRRNQN 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 207 FQTILSLQQFqgpGAQGILDHDL------VFWFGDLNFRIEsYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQ 280
Cdd:cd09101 153 YLDILRSLSL---GDKQLNAFDIslrfthLFWFGDLNYRLD-MDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFR 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 281 EGPLNFAPTFKFDVGT-------NKYDTSAKKRKPAWTDRILWKvkapgggpspSGRKSHrlqVTQHSYRSHMEYTVSDH 353
Cdd:cd09101 229 EEEISFPPTYRYERGSrdtymwqKQKTTGMRTNVPSWCDRILWK----------SYPETH---IVCNSYGCTDDIVTSDH 295


                ....*..
gi 50726960 354 KPVAAQF 360
Cdd:cd09101 296 SPVFGTF 302
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 169-362 5.52e-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: 42.84  E-value: 5.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 169 WGNKGGVSVRLAAFGHMLCFLNCHL-------------PAHMDKAEQRKDNFqTI--LSLQQFQGPgaqgildhdLVFWF 233
Cdd:cd09092 152 WSRKGFMRTRWKINNCVFDLVNIHLfhdasnlaacessPSVYSQNRHRALGY-VLerLTDERFEKV---------PFFVF 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 234 GDLNFRIESYDL----------HFVKFAI------------------------------DSDQLHQLWEKDQLNMAKNTW 273
Cdd:cd09092 222 GDFNFRLDTKSVvetlcakatmQTVRKADsnivvklefrekdndnkvvlqiekkkfdyfNQDVFRDNNGKALLKFDKELE 301

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 274 PILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWkvkapgggpSPSGRKShRLQVTQHS--YRS-HMEYTV 350
Cdd:cd09092 302 VFKDVLYELDISFPPSYPYSEDPEQGTQYMNTRCPAWCDRILM---------SHSAREL-KSENEEKSvtYDMiGPNVCM 371

                       250
                ....*....|..
gi 50726960 351 SDHKPVAAQFLL 362
Cdd:cd09092 372 GDHKPVFLTFRI 383
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 59-359 9.24e-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: 41.31  E-value: 9.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960  59 VVTWNVGTAMppddVTSLLHLGGGDDSDGADMIaIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVlvssvrmQG 138
Cdd:cd08372   1 VASYNVNGLN----AATRASGIARWVRELDPDI-VCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSRKEGY-------EG 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 139 VILLLFAKYYHLPFLRDVQTDCTRTGlggywgNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQG 218
Cdd:cd08372  69 VAILSKTPKFKIVEKHQYKFGEGDSG------ERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKRLR 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726960 219 PGaqgilDHDLVFWFGDLNFRIESydlhfvkfaIDSDQLHQLWEKDQLNMAKNTWPIlkgfqegpLNFAPTFKFdvgtnk 298
Cdd:cd08372 143 QP-----NSAPVVICGDFNVRPSE---------VDSENPSSMLRLFVALNLVDSFET--------LPHAYTFDT------ 194

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50726960 299 ydtsAKKRKPAWTDRILWkvkAPGGGPSPsgrksHRLQVTQHSYRSHMeytVSDHKPVAAQ 359
Cdd:cd08372 195 ----YMHNVKSRLDYIFV---SKSLLPSV-----KSSKILSDAARARI---PSDHYPIEVT 240
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH