NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2552469067|ref|NP_001410408|]
View 

phosphatidylinositol 4,5-bisphosphate 5-phosphatase A isoform h [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 ...
 56-363 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: 546.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  56 FRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGadMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSV 135
Cdd:cd09094     1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPD--IYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 136 RMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQ 215
Cdd:cd09094    79 RLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 216 QFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDV 295
Cdd:cd09094   159 VFNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2552469067 296 GTNKYDTSAKKRKPAWTDRILWKVKAPGGGPspsgrkSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLL 363
Cdd:cd09094   239 GTDEYDTSGKKRKPAWTDRILWKVNPDASTE------EKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
SKICH super family cl39277
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 374-446 1.35e-17

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.


The actual alignment was detected with superfamily member pfam17751:

Pssm-ID: 465482  Cd Length: 102  Bit Score: 78.44  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 374 VRLEVADEW-VRPEQAVVRYRMETVFARSSWDWIGLYRV----------------------------TFSEESLPK-GHG 423
Cdd:pfam17751   1 VVFQNVGEWyPPDEDIECSYTLTPDFTPSSWDWIGLFKVgwksvndyvtyvwakddevegsnsvrqvLFKASYLPKePEG 80

                          90       100
                  ....*....|....*....|...
gi 2552469067 424 DFILGYYSHNHSIlIGITEPFQI 446
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 ...
 56-363 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: 546.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  56 FRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGadMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSV 135
Cdd:cd09094     1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPD--IYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 136 RMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQ 215
Cdd:cd09094    79 RLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 216 QFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDV 295
Cdd:cd09094   159 VFNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2552469067 296 GTNKYDTSAKKRKPAWTDRILWKVKAPGGGPspsgrkSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLL 363
Cdd:cd09094   239 GTDEYDTSGKKRKPAWTDRILWKVNPDASTE------EKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 54-361 3.00e-90

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 281.55  E-value: 3.00e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067   54 PGFRITVVTWNVGTAMPPD-DVTSLLHLGGGDDSDGAD-MIAIGLQEVNSM--LNKRLKDALFTDQWSELFMDAL-GPFN 128
Cdd:smart00128   1 RDIKVLIGTWNVGGLESPKvDVTSWLFQKIEVKQSEKPdIYVIGLQEVVGLapGVILETIAGKERLWSDLLESSLnGDGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  129 FVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF 208
Cdd:smart00128  81 YNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  209 QTILSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFA 288
Cdd:smart00128 161 KTILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFP 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2552469067  289 PTFKFDV-GTNKYDTSAKKRKPAWTDRILWKVKAPgggpspsgrkshrlQVTQHS-YRSHMEYTVSDHKPVAAQF 361
Cdd:smart00128 241 PTYKYDSvGTETYDTSEKKRVPAWCDRILYRSNGP--------------ELIQLSeYHSGMEITTSDHKPVFATF 301
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
49-376 8.14e-46

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 168.42  E-value: 8.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  49 TWKSDpgFRITVVTWNVGTAMPPDDVTSLLhLGGGDDSDGADMIAIGLQEV-----NSMLNKRLKDALftDQWSELFMD- 122
Cdd:COG5411    25 VIEKD--VSIFVSTFNPPGKPPKASTKRWL-FPEIEATELADLYVVGLQEVveltpGSILSADPYDRL--RIWESKVLDc 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 123 ---ALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMD 199
Cdd:COG5411   100 lngAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVN 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 200 KAEQRKDNFQTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIES-YDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILK 278
Cdd:COG5411   180 NIEERIFDYRSIASNICF--SRGLRIYDHDTIFWLGDLNYRVTStNEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFP 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 279 GFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILwkvkapgggpspsGRKShrlQVTQHSYRSHMEYTVSDHKPVA 358
Cdd:COG5411   258 GFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRIL-------------YKSE---QLTPHSYSSIPHLMISDHRPVY 321

                         330
                  ....*....|....*...
gi 2552469067 359 AQFLLQFAFRDDMPLVRL 376
Cdd:COG5411   322 ATFRAKIKVVDPSKKEGL 339
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 165-388 3.86e-34

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 137.73  E-value: 3.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 165 GLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPA-HMDKAEQRKD----------NFQTILSLQQfqgpgAQGILDHDLVFW 233
Cdd:PLN03191  400 GLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRRNadvyeiirrtRFSSVLDTDQ-----PQTIPSHDQIFW 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 234 FGDLNFRIESYDLHFVKFaIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKY-----DTSAKKRK 308
Cdd:PLN03191  475 FGDLNYRLNMLDTEVRKL-VAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRS 553

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 309 PAWTDRILWKVKApgggpspsgrkshrlqVTQHSYRsHMEYTVSDHKPVAAQFLLQFAFRDDMPLVR-LEV---ADEWVR 384
Cdd:PLN03191  554 PAWCDRILWLGKG----------------IKQLCYK-RSEIRLSDHRPVSSMFLVEVEVFDHRKLQRaLNVnsaAASAVH 616


                  ....
gi 2552469067 385 PEQA 388
Cdd:PLN03191  617 PEPS 620
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 374-446 1.35e-17

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: 78.44  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 374 VRLEVADEW-VRPEQAVVRYRMETVFARSSWDWIGLYRV----------------------------TFSEESLPK-GHG 423
Cdd:pfam17751   1 VVFQNVGEWyPPDEDIECSYTLTPDFTPSSWDWIGLFKVgwksvndyvtyvwakddevegsnsvrqvLFKASYLPKePEG 80

                          90       100
                  ....*....|....*....|...
gi 2552469067 424 DFILGYYSHNHSIlIGITEPFQI 446
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 ...
 56-363 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: 546.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  56 FRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGadMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSV 135
Cdd:cd09094     1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPD--IYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 136 RMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQ 215
Cdd:cd09094    79 RLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 216 QFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDV 295
Cdd:cd09094   159 VFNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2552469067 296 GTNKYDTSAKKRKPAWTDRILWKVKAPGGGPspsgrkSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLL 363
Cdd:cd09094   239 GTDEYDTSGKKRKPAWTDRILWKVNPDASTE------EKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 56-363 1.04e-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: 367.43  E-value: 1.04e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  56 FRITVVTWNVGTAM-PPDDVTSLLHLGGGDDSDgadMIAIGLQEVNSMLN--KRLKDALFTDQWSELFMDALGP-FNFVL 131
Cdd:cd09074     1 VKIFVVTWNVGGGIsPPENLENWLSPKGTEAPD---IYAVGVQEVDMSVQgfVGNDDSAKAREWVDNIQEALNEkENYVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 132 VSSVRMQGVILLLFAKYYHLPFLRDVQTDCTR--TGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQ 209
Cdd:cd09074    78 LGSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTvgTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVERRNQDYR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 210 TILSLQQFQGPG--AQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDqLHQLWEKDQLNMAKNTWPILKGFQEGPLNF 287
Cdd:cd09074   158 DILSKLKFYRGDpaIDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGD-LDDLLEKDQLKKQKEKGKVFDGFQELPITF 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2552469067 288 APTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGggpspsgrkshrlQVTQHSYRSHMEYTVSDHKPVAAQFLL 363
Cdd:cd09074   237 PPTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGS-------------EIQPLSYTSVPLYKTSDHKPVRATFRV 299
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 54-361 3.00e-90

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 281.55  E-value: 3.00e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067   54 PGFRITVVTWNVGTAMPPD-DVTSLLHLGGGDDSDGAD-MIAIGLQEVNSM--LNKRLKDALFTDQWSELFMDAL-GPFN 128
Cdd:smart00128   1 RDIKVLIGTWNVGGLESPKvDVTSWLFQKIEVKQSEKPdIYVIGLQEVVGLapGVILETIAGKERLWSDLLESSLnGDGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  129 FVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF 208
Cdd:smart00128  81 YNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  209 QTILSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFA 288
Cdd:smart00128 161 KTILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFP 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2552469067  289 PTFKFDV-GTNKYDTSAKKRKPAWTDRILWKVKAPgggpspsgrkshrlQVTQHS-YRSHMEYTVSDHKPVAAQF 361
Cdd:smart00128 241 PTYKYDSvGTETYDTSEKKRVPAWCDRILYRSNGP--------------ELIQLSeYHSGMEITTSDHKPVFATF 301
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 56-361 1.92e-86

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: 271.11  E-value: 1.92e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  56 FRITVVTWNVGTAMPPDDVTSLLHLGGGDDSdgadMIAIGLQEVNsmLNKrlKDALFTD-----QWSELFMDALGPFN-F 129
Cdd:cd09093     1 FRIFVGTWNVNGQSPDESLRPWLSCDEEPPD----IYAIGFQELD--LSA--EAFLFNDssreqEWVKAVERGLHPDAkY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 130 VLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQ 209
Cdd:cd09093    73 KKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRNQDYK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 210 TILSLQQF--QGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNF 287
Cdd:cd09093   153 DICARMKFedPDGPPLSISDHDVVFWLGDLNYRIQELPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINF 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2552469067 288 APTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKapgggpspsgrkshrlQVTQHSYRSHMEYTVSDHKPVAAQF 361
Cdd:cd09093   233 IPTYKYDPGTDNWDSSEKCRAPAWCDRILWRGT----------------NIVQLSYRSHMELKTSDHKPVSALF 290
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 57-361 2.41e-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: 2.41e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  57 RITVVTWNVGTAMPPDDVTSLLHlgGGDDSDGADMIAIGLQEV-----NSMLNKrlkDALFTDQWSELFMDAL---GPFN 128
Cdd:cd09090     2 NIFVGTFNVNGKSYKDDLSSWLF--PEENDELPDIVVIGLQEVveltaGQILNS---DPSKSSFWEKKIKTTLngrGGEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 129 FVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF 208
Cdd:cd09090    77 YVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEERNNDY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 209 QTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIE-SYDLhfVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNF 287
Cdd:cd09090   157 KTIARGLRF--SRGRTIKDHDHVIWLGDFNYRISlTNED--VRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITF 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2552469067 288 APTFKFDVGTNKYDTSAKKRKPAWTDRILwkvkapgggpspsgRKSHRLQvtQHSYRSHMEYtVSDHKPVAAQF 361
Cdd:cd09090   233 PPTYKYDKGTDNYDTSEKQRIPAWTDRIL--------------YRGENLR--QLSYNSAPLR-FSDHRPVYATF 289
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 129-361 3.37e-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: 3.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 129 FVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF 208
Cdd:cd09089    94 YVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQVKERNEDF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 209 QTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIE-SYDLhfVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNF 287
Cdd:cd09089   174 AEIARKLSF--PMGRTLDSHDYVFWCGDFNYRIDlPNDE--VKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINF 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552469067 288 APTFKFDVGTNKYDTSAKKRKPAWTDRILW---KVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQF 361
Cdd:cd09089   250 APTYKYDLFSDDYDTSEKCRTPAWTDRVLWrrrKWPSDKTEESLVETNDPTWNPGTLLYYGRAELKTSDHRPVVAII 326
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 91-359 1.66e-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: 1.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  91 MIAIGLQEVNSMLNKRLKDALFTDQ--WSELFMDALG-PFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLG 167
Cdd:cd09099    52 IFAVGFEEMVELSAGNIVNASTTNRkmWGEQLQKAISrSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 168 GYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTIlsLQQFQGPGAQGILDHDLVFWFGDLNFRIE-SYDL 246
Cdd:cd09099   132 GKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQVKERNEDYKEI--TQKLSFPMGRNVFSHDYVFWCGDFNYRIDlTYEE 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 247 HFvkFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRIL-WKVKAP--- 322
Cdd:cd09099   210 VF--YFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLwWRKKWPfek 287

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2552469067 323 --------GGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAA 359
Cdd:cd09099   288 tageinllDSDLDFDTKIRHTWTPGALMYYGRAELQASDHRPVLA 332
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 91-359 1.35e-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: 1.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  91 MIAIGLQEVNSMLNKRLKDALFTDQ--WS-ELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLG 167
Cdd:cd09098    52 IFAIGFEEMVELNAGNIVSASTTNQklWAaELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 168 GYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIESYDLH 247
Cdd:cd09098   132 GATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSF--PMGRMLFSHDYVFWCGDFNYRIDIPNEE 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 248 fVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKApgggpS 327
Cdd:cd09098   210 -VKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRK-----W 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2552469067 328 PSGRKSHRLQVTQHSYR--SHMEYT---------------VSDHKPVAA 359
Cdd:cd09098   284 PFDRSAEDLDLLNASFPdnSKEQYTwspgtllhygraelkTSDHRPVVA 332
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
49-376 8.14e-46

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 168.42  E-value: 8.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  49 TWKSDpgFRITVVTWNVGTAMPPDDVTSLLhLGGGDDSDGADMIAIGLQEV-----NSMLNKRLKDALftDQWSELFMD- 122
Cdd:COG5411    25 VIEKD--VSIFVSTFNPPGKPPKASTKRWL-FPEIEATELADLYVVGLQEVveltpGSILSADPYDRL--RIWESKVLDc 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 123 ---ALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMD 199
Cdd:COG5411   100 lngAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVN 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 200 KAEQRKDNFQTILSLQQFqgPGAQGILDHDLVFWFGDLNFRIES-YDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILK 278
Cdd:COG5411   180 NIEERIFDYRSIASNICF--SRGLRIYDHDTIFWLGDLNYRVTStNEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFP 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 279 GFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILwkvkapgggpspsGRKShrlQVTQHSYRSHMEYTVSDHKPVA 358
Cdd:COG5411   258 GFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRIL-------------YKSE---QLTPHSYSSIPHLMISDHRPVY 321

                         330
                  ....*....|....*...
gi 2552469067 359 AQFLLQFAFRDDMPLVRL 376
Cdd:COG5411   322 ATFRAKIKVVDPSKKEGL 339
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 57-361 3.64e-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: 154.12  E-value: 3.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  57 RITVVTWNV-GTAMPPDDVTSLLhlGGGDDSDGADMIAIGLQEVNSmlNKRlkdalftdQWSELFMDALGPfNFVLVSSV 135
Cdd:cd09095     6 GIFVATWNMqGQKELPENLDDFL--LPTSADFAQDIYVIGVQEGCS--DRR--------EWEIRLQETLGP-SHVLLHSA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 136 RMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNF-QTILSL 214
Cdd:cd09095    73 SHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYnKIIQAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 215 Q-QFQGPG------AQGILDH-DLVFWFGDLNFRIeSYDLHFVKFAIDSDQ---LHQLWEKDQL--NMAKNTwpILKGFQ 281
Cdd:cd09095   153 NlPRNVPTnpykseSGDVTTRfDEVFWFGDFNFRL-SGPRHLVDALINQGQevdVSALLQHDQLtrEMSKGS--IFKGFQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 282 EGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGggpspsgrkshrlQVTQHSYRSHMEYTVSDHKPVAAQF 361
Cdd:cd09095   230 EAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSRQKG-------------DVCCLKYNSCPSIKTSDHRPVFALF 296
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 165-388 3.86e-34

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 137.73  E-value: 3.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 165 GLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPA-HMDKAEQRKD----------NFQTILSLQQfqgpgAQGILDHDLVFW 233
Cdd:PLN03191  400 GLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRRNadvyeiirrtRFSSVLDTDQ-----PQTIPSHDQIFW 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 234 FGDLNFRIESYDLHFVKFaIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKY-----DTSAKKRK 308
Cdd:PLN03191  475 FGDLNYRLNMLDTEVRKL-VAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRS 553

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 309 PAWTDRILWKVKApgggpspsgrkshrlqVTQHSYRsHMEYTVSDHKPVAAQFLLQFAFRDDMPLVR-LEV---ADEWVR 384
Cdd:PLN03191  554 PAWCDRILWLGKG----------------IKQLCYK-RSEIRLSDHRPVSSMFLVEVEVFDHRKLQRaLNVnsaAASAVH 616


                  ....
gi 2552469067 385 PEQA 388
Cdd:PLN03191  617 PEPS 620
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 58-361 8.89e-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: 8.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  58 ITVVTWNVGTAMPPDDVTSLLH-------LGGGDDSDGADMIAIGLQEvnsmlnkrlkDALFTDQWSELFMDALGPFNFV 130
Cdd:cd09091     3 IFIGTWNMGSAPPPKNITSWFTskgqgktRDDVADYIPHDIYVIGTQE----------DPLGEKEWLDLLRHSLKELTSL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 131 LVSSVRMQ---GVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDN 207
Cdd:cd09091    73 DYKPIAMQtlwNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 208 FQTILslqQFQGPGAQGILDHDL------VFWFGDLNFRIE--SYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKG 279
Cdd:cd09091   153 YLNIL---RFLSLGDKKLSAFNIthrfthLFWLGDLNYRLDlpIQEAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFLR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 280 FQEGPLNFAPTFKFDVGT-NKY------DTSAKKRKPAWTDRILWKvkapgggpspSGRKSHrlqVTQHSYRSHMEYTVS 352
Cdd:cd09091   230 FSEEEITFPPTYRYERGSrDTYaytkqkATGVKYNLPSWCDRILWK----------SYPETH---IICQSYGCTDDIVTS 296


                  ....*....
gi 2552469067 353 DHKPVAAQF 361
Cdd:cd09091   297 DHSPVFGTF 305
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 58-361 2.21e-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: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  58 ITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGAD-------MIAIGLQEvnsmlnkrlkDALFTDQWSELFMDAL---GPF 127
Cdd:cd09100     3 IFIGTWNMGNAPPPKKITSWFQCKGQGKTRDDTadyiphdIYVIGTQE----------DPLGEKEWLDTLKHSLreiTSI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 128 NFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDN 207
Cdd:cd09100    73 SFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 208 FQTILslqQFQGPGAQGILDHDL------VFWFGDLNFRIE--SYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKG 279
Cdd:cd09100   153 YFNIL---RFLVLGDKKLSPFNIthrfthLFWLGDLNYRVElpNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 280 FQEGPLNFAPTFKFDVGT-NKY------DTSAKKRKPAWTDRILWKvkapgggpspsgrKSHRLQVTQHSYRSHMEYTVS 352
Cdd:cd09100   230 FEEEEITFAPTYRFERGTrERYaytkqkATGMKYNLPSWCDRVLWK-------------SYPLVHVVCQSYGCTDDITTS 296


                  ....*....
gi 2552469067 353 DHKPVAAQF 361
Cdd:cd09100   297 DHSPVFATF 305
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 58-361 3.30e-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: 111.99  E-value: 3.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  58 ITVVTWNVGTAMPPDDVTSLL-------HLGGGDDSDGADMIAIGLQEvNSMLNKrlkdalftdQWSELFMDALGPFNFV 130
Cdd:cd09101     3 IFIGTWNMGSVPPPKSLASWLtsrglgkTLDETTVTIPHDIYVFGTQE-NSVGDR---------EWVDFLRASLKELTDI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 131 LVSSVRMQ---GVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDN 207
Cdd:cd09101    73 DYQPIALQclwNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTHRRNQN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 208 FQTI---LSLQQFQGPGAQGILDHDLVFWFGDLNFRIEsYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGP 284
Cdd:cd09101   153 YLDIlrsLSLGDKQLNAFDISLRFTHLFWFGDLNYRLD-MDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFREEE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 285 LNFAPTFKFDVGT-------NKYDTSAKKRKPAWTDRILWKvkapgggpspSGRKSHrlqVTQHSYRSHMEYTVSDHKPV 357
Cdd:cd09101   232 ISFPPTYRYERGSrdtymwqKQKTTGMRTNVPSWCDRILWK----------SYPETH---IVCNSYGCTDDIVTSDHSPV 298


                  ....
gi 2552469067 358 AAQF 361
Cdd:cd09101   299 FGTF 302
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 374-446 1.35e-17

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: 78.44  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 374 VRLEVADEW-VRPEQAVVRYRMETVFARSSWDWIGLYRV----------------------------TFSEESLPK-GHG 423
Cdd:pfam17751   1 VVFQNVGEWyPPDEDIECSYTLTPDFTPSSWDWIGLFKVgwksvndyvtyvwakddevegsnsvrqvLFKASYLPKePEG 80

                          90       100
                  ....*....|....*....|...
gi 2552469067 424 DFILGYYSHNHSIlIGITEPFQI 446
Cdd:pfam17751  81 FYQFCYVSNLGSV-VGISTPFQF 102
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 170-363 5.24e-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: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 170 WGNKGGVSVRLAAFGHMLCFLNCHL-------------PAHMDKAEQRKDNFqTI--LSLQQFQGPgaqgildhdLVFWF 234
Cdd:cd09092   152 WSRKGFMRTRWKINNCVFDLVNIHLfhdasnlaacessPSVYSQNRHRALGY-VLerLTDERFEKV---------PFFVF 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 235 GDLNFRIESYDL----------HFVKFAI------------------------------DSDQLHQLWEKDQLNMAKNTW 274
Cdd:cd09092   222 GDFNFRLDTKSVvetlcakatmQTVRKADsnivvklefrekdndnkvvlqiekkkfdyfNQDVFRDNNGKALLKFDKELE 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 275 PILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWkvkapgggpSPSGRKShRLQVTQHS--YRS-HMEYTV 351
Cdd:cd09092   302 VFKDVLYELDISFPPSYPYSEDPEQGTQYMNTRCPAWCDRILM---------SHSAREL-KSENEEKSvtYDMiGPNVCM 371

                         250
                  ....*....|..
gi 2552469067 352 SDHKPVAAQFLL 363
Cdd:cd09092   372 GDHKPVFLTFRI 383
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 94-360 8.96e-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: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067  94 IGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVlvssvrmQGVILLLFAKYYHLPFLRDVQTDCTRTGlggywgNK 173
Cdd:cd08372    30 VCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSRKEGY-------EGVAILSKTPKFKIVEKHQYKFGEGDSG------ER 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 174 GGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGaqgilDHDLVFWFGDLNFRIESydlhfvkfaI 253
Cdd:cd08372    97 RAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKRLRQP-----NSAPVVICGDFNVRPSE---------V 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552469067 254 DSDQLHQLWEKDQLNMAKNTWPIlkgfqegpLNFAPTFKFdvgtnkydtsAKKRKPAWTDRILWkvkAPGGGPSPsgrks 333
Cdd:cd08372   163 DSENPSSMLRLFVALNLVDSFET--------LPHAYTFDT----------YMHNVKSRLDYIFV---SKSLLPSV----- 216

                         250       260
                  ....*....|....*....|....*..
gi 2552469067 334 HRLQVTQHSYRSHMeytVSDHKPVAAQ 360
Cdd:cd08372   217 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