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Conserved domains on  [gi|1207189676|ref|XP_694550|]
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inositol polyphosphate 5-phosphatase K isoform X3 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
15-336 1.78e-166

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: 471.08  E-value: 1.78e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  15 FRLHMVTWNVGTAEPPADVRSLLQLDS-QPTTDLYVIGLQEVNATPVRYISDLIVEDTWSHLLMETLAPEGYIKVTSVRM 93
Cdd:cd09094     1 LRVYVVTWNVATAPPPIDVRSLLGLQSpEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  94 QGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDTQEF 173
Cdd:cd09094    81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 174 DMFNTPQVLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTYKFDRFS 253
Cdd:cd09094   161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 254 ETYDTraprtwfglTGKKRKPAWTDRILWRIKPKATEiedeksstassaddDEFSVKVTQDMYTCDVSYGVSDHKPVIGT 333
Cdd:cd09094   241 DEYDT---------SGKKRKPAWTDRILWKVNPDAST--------------EEKFLSITQTSYKSHMEYGISDHKPVTAQ 297

                  ...
gi 1207189676 334 FNL 336
Cdd:cd09094   298 FRL 300
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
347-447 3.73e-32

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: 118.12  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 347 VALTVEGIWS-ADEDAIFTYTILENFESSTFDWIGLYKIGFKSASDYSTFAWVKDDEVAANGEVVMVQMNKNELPLL-AG 424
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPKEpEG 80
                          90       100
                  ....*....|....*....|...
gi 1207189676 425 DYVLGYFStNMQTLIAFSPNFQI 447
Cdd:pfam17751  81 FYQFCYVS-NLGSVVGISTPFQF 102
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
15-336 1.78e-166

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: 471.08  E-value: 1.78e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  15 FRLHMVTWNVGTAEPPADVRSLLQLDS-QPTTDLYVIGLQEVNATPVRYISDLIVEDTWSHLLMETLAPEGYIKVTSVRM 93
Cdd:cd09094     1 LRVYVVTWNVATAPPPIDVRSLLGLQSpEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  94 QGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDTQEF 173
Cdd:cd09094    81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 174 DMFNTPQVLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTYKFDRFS 253
Cdd:cd09094   161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 254 ETYDTraprtwfglTGKKRKPAWTDRILWRIKPKATEiedeksstassaddDEFSVKVTQDMYTCDVSYGVSDHKPVIGT 333
Cdd:cd09094   241 DEYDT---------SGKKRKPAWTDRILWKVNPDAST--------------EEKFLSITQTSYKSHMEYGISDHKPVTAQ 297

                  ...
gi 1207189676 334 FNL 336
Cdd:cd09094   298 FRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
13-337 6.16e-82

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 255.74  E-value: 6.16e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676   13 QAFRLHMVTWNVGTA-EPPADVRSLLQLDSQPT----TDLYVIGLQEVNATPVRYISDLI--VEDTWSHLLMETLAPEG- 84
Cdd:smart00128   1 RDIKVLIGTWNVGGLeSPKVDVTSWLFQKIEVKqsekPDIYVIGLQEVVGLAPGVILETIagKERLWSDLLESSLNGDGq 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676   85 YIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEF 164
Cdd:smart00128  81 YNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  165 EYILDTQEFDMFNTPQVLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFK 244
Cdd:smart00128 161 KTILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  245 PTYKFDRF-SETYDTraprtwfglTGKKRKPAWTDRILWRikPKATEIEDEKSstassadddefsvkvtqdmYTCDVSYG 323
Cdd:smart00128 241 PTYKYDSVgTETYDT---------SEKKRVPAWCDRILYR--SNGPELIQLSE-------------------YHSGMEIT 290
                          330
                   ....*....|....
gi 1207189676  324 VSDHKPVIGTFNLE 337
Cdd:smart00128 291 TSDHKPVFATFRLK 304
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
12-349 3.04e-43

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 158.41  E-value: 3.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  12 HQAFRLHMVTWNVGTAEPPADVRSLLQLDSQ--PTTDLYVIGLQEVNA-TPVRYIS------DLIVEDTWSHLLMETLAP 82
Cdd:COG5411    27 EKDVSIFVSTFNPPGKPPKASTKRWLFPEIEatELADLYVVGLQEVVElTPGSILSadpydrLRIWESKVLDCLNGAQSD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  83 EGYIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMD 162
Cdd:COG5411   107 EKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 163 EFEYILDTQEFDmfNTPQVLDHKVVFWFGDLNFRIAdhGMHF-LRSSINN--SRFNLLWDRDQLSMLKKKEPILQEFEEG 239
Cdd:COG5411   187 DYRSIASNICFS--RGLRIYDHDTIFWLGDLNYRVT--STNEeVRPEIASddGRLDKLFEYDQLLWEMEVGNVFPGFKEP 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 240 PLRFKPTYKFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRikpkateiedeksstassadddefSVKVTQDMYTCD 319
Cdd:COG5411   263 VITFPPTYKFDYGTDEYDT---------SDKGRIPSWTDRILYK------------------------SEQLTPHSYSSI 309
                         330       340       350
                  ....*....|....*....|....*....|
gi 1207189676 320 VSYGVSDHKPVIGTFNLEMRKKVETPLVAL 349
Cdd:COG5411   310 PHLMISDHRPVYATFRAKIKVVDPSKKEGL 339
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
347-447 3.73e-32

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: 118.12  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 347 VALTVEGIWS-ADEDAIFTYTILENFESSTFDWIGLYKIGFKSASDYSTFAWVKDDEVAANGEVVMVQMNKNELPLL-AG 424
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPKEpEG 80
                          90       100
                  ....*....|....*....|...
gi 1207189676 425 DYVLGYFStNMQTLIAFSPNFQI 447
Cdd:pfam17751  81 FYQFCYVS-NLGSVVGISTPFQF 102
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
85-338 2.02e-29

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 121.55  E-value: 2.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  85 YIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAA-HMNYALQR--M 161
Cdd:PLN03191  364 YVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRrnA 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 162 DEFEYILDTQEFDMFNTPQ---VLDHKVVFWFGDLNFRI----ADhgmhfLRSSINNSRFNLLWDRDQLSMLKKKEPILQ 234
Cdd:PLN03191  444 DVYEIIRRTRFSSVLDTDQpqtIPSHDQIFWFGDLNYRLnmldTE-----VRKLVAQKRWDELINSDQLIKELRSGHVFD 518
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 235 EFEEGPLRFKPTYKFDRFSETYDTRAPRTwfglTGKKRKPAWTDRILWrikpkateiedeksstassadddeFSVKVTQD 314
Cdd:PLN03191  519 GWKEGPIKFPPTYKYEINSDRYVGENPKE----GEKKRSPAWCDRILW------------------------LGKGIKQL 570
                         250       260
                  ....*....|....*....|....
gi 1207189676 315 MYTcDVSYGVSDHKPVIGTFNLEM 338
Cdd:PLN03191  571 CYK-RSEIRLSDHRPVSSMFLVEV 593
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
15-336 1.78e-166

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: 471.08  E-value: 1.78e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  15 FRLHMVTWNVGTAEPPADVRSLLQLDS-QPTTDLYVIGLQEVNATPVRYISDLIVEDTWSHLLMETLAPEGYIKVTSVRM 93
Cdd:cd09094     1 LRVYVVTWNVATAPPPIDVRSLLGLQSpEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  94 QGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDTQEF 173
Cdd:cd09094    81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 174 DMFNTPQVLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTYKFDRFS 253
Cdd:cd09094   161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 254 ETYDTraprtwfglTGKKRKPAWTDRILWRIKPKATEiedeksstassaddDEFSVKVTQDMYTCDVSYGVSDHKPVIGT 333
Cdd:cd09094   241 DEYDT---------SGKKRKPAWTDRILWKVNPDAST--------------EEKFLSITQTSYKSHMEYGISDHKPVTAQ 297

                  ...
gi 1207189676 334 FNL 336
Cdd:cd09094   298 FRL 300
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
15-336 7.47e-85

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


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 262.65  E-value: 7.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  15 FRLHMVTWNVGTAE-PPADVRSLLQLDSQPTTDLYVIGLQEVNATPVRYISDLIVEDT--WSHLLMETLAP-EGYIKVTS 90
Cdd:cd09074     1 VKIFVVTWNVGGGIsPPENLENWLSPKGTEAPDIYAVGVQEVDMSVQGFVGNDDSAKAreWVDNIQEALNEkENYVLLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  91 VRMQGLLLILFAKQVHLPFIRDIQSTYTR--TGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYIL 168
Cdd:cd09074    81 AQLVGIFLFVFVKKEHLPQIKDLEVEGVTvgTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVERRNQDYRDIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 169 DTQEFDMFNTP--QVLDHKVVFWFGDLNFRIaDHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPT 246
Cdd:cd09074   161 SKLKFYRGDPAidSIFDHDVVFWFGDLNYRI-DSTDDEVRKLISQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFPPT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 247 YKFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRIKPKateiedeksstassadddefsVKVTQDMYTCDVSYGVSD 326
Cdd:cd09074   240 YKFDPGTDEYDT---------SDKKRIPAWCDRILYKSKAG---------------------SEIQPLSYTSVPLYKTSD 289
                         330
                  ....*....|
gi 1207189676 327 HKPVIGTFNL 336
Cdd:cd09074   290 HKPVRATFRV 299
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
13-337 6.16e-82

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 255.74  E-value: 6.16e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676   13 QAFRLHMVTWNVGTA-EPPADVRSLLQLDSQPT----TDLYVIGLQEVNATPVRYISDLI--VEDTWSHLLMETLAPEG- 84
Cdd:smart00128   1 RDIKVLIGTWNVGGLeSPKVDVTSWLFQKIEVKqsekPDIYVIGLQEVVGLAPGVILETIagKERLWSDLLESSLNGDGq 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676   85 YIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEF 164
Cdd:smart00128  81 YNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  165 EYILDTQEFDMFNTPQVLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFK 244
Cdd:smart00128 161 KTILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  245 PTYKFDRF-SETYDTraprtwfglTGKKRKPAWTDRILWRikPKATEIEDEKSstassadddefsvkvtqdmYTCDVSYG 323
Cdd:smart00128 241 PTYKYDSVgTETYDT---------SEKKRVPAWCDRILYR--SNGPELIQLSE-------------------YHSGMEIT 290
                          330
                   ....*....|....
gi 1207189676  324 VSDHKPVIGTFNLE 337
Cdd:smart00128 291 TSDHKPVFATFRLK 304
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
15-335 1.29e-75

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: 238.75  E-value: 1.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  15 FRLHMVTWNVGTAEPPADVRSLLQLDSQPTtDLYVIGLQEVNATPVRYI-SDLIVEDTWSHLLMETLAPEG-YIKVTSVR 92
Cdd:cd09093     1 FRIFVGTWNVNGQSPDESLRPWLSCDEEPP-DIYAIGFQELDLSAEAFLfNDSSREQEWVKAVERGLHPDAkYKKVKLIR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  93 MQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDTQE 172
Cdd:cd09093    80 LVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRNQDYKDICARMK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 173 FDMFNTPQ--VLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTYKFD 250
Cdd:cd09093   160 FEDPDGPPlsISDHDVVFWLGDLNYRIQELPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEGEINFIPTYKYD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 251 RFSETYDTRaprtwfgltGKKRKPAWTDRILWRIKpkateiedeksstassadddefsvKVTQDMYTCDVSYGVSDHKPV 330
Cdd:cd09093   240 PGTDNWDSS---------EKCRAPAWCDRILWRGT------------------------NIVQLSYRSHMELKTSDHKPV 286

                  ....*
gi 1207189676 331 IGTFN 335
Cdd:cd09093   287 SALFD 291
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
16-334 2.58e-52

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: 178.30  E-value: 2.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  16 RLHMVTWNVGTAEPPADVRSLL---QLDSQPttDLYVIGLQE-VNATPVRYI-SDLIVEDTWSHLLMETLA---PEGYIK 87
Cdd:cd09090     2 NIFVGTFNVNGKSYKDDLSSWLfpeENDELP--DIVVIGLQEvVELTAGQILnSDPSKSSFWEKKIKTTLNgrgGEKYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  88 VTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYI 167
Cdd:cd09090    80 LRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEERNNDYKTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 168 LDTQEFDMFNTpqVLDHKVVFWFGDLNFRIaDHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTY 247
Cdd:cd09090   160 ARGLRFSRGRT--IKDHDHVIWLGDFNYRI-SLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITFPPTY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 248 KFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRIKPkateiedeksstassadddefsvkVTQDMYTCDVSYgVSDH 327
Cdd:cd09090   237 KYDKGTDNYDT---------SEKQRIPAWTDRILYRGEN------------------------LRQLSYNSAPLR-FSDH 282

                  ....*..
gi 1207189676 328 KPVIGTF 334
Cdd:cd09090   283 RPVYATF 289
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
40-335 2.51e-50

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: 174.12  E-value: 2.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  40 DSQPTtDLYVIGLQEV---NAtpvryiSDLIVEDT-----WSHLLMETLAPEG-YIKVTSVRMQGLLLILFAKQVHLPFI 110
Cdd:cd09089    47 DEKPV-DIFAIGFEEMvdlNA------SNIVSASTtnqkeWGEELQKTISRDHkYVLLTSEQLVGVCLFVFVRPQHAPFI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 111 RDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDTQEFDMFNTpqVLDHKVVFWF 190
Cdd:cd09089   120 RDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQVKERNEDFAEIARKLSFPMGRT--LDSHDYVFWC 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 191 GDLNFRIaDHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTYKFDRFSETYDTraprtwfglTGK 270
Cdd:cd09089   198 GDFNYRI-DLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDT---------SEK 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 271 KRKPAWTDRILWRIKPKATEIEDEKSSTASSADDDEFSVkvtqdmytcdVSYG-----VSDHKPVIGTFN 335
Cdd:cd09089   268 CRTPAWTDRVLWRRRKWPSDKTEESLVETNDPTWNPGTL----------LYYGraelkTSDHRPVVAIID 327
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
16-331 5.98e-47

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: 165.58  E-value: 5.98e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  16 RLHMVTWNV-----------GTAE--------PPADVRSLLQLDSQPTTDLYVIGLQE---------VNATPVRyisdli 67
Cdd:cd09099     2 RVAMGTWNVnggkqfrsnilGTSEltdwlldsPKLSGTPDFQDDESNPPDIFAVGFEEmvelsagniVNASTTN------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  68 vEDTWSHLLMETLA-PEGYIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFL 146
Cdd:cd09099    76 -RKMWGEQLQKAISrSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 147 NCHLAAHMNYALQRMDEFEYIldTQEFDMFNTPQVLDHKVVFWFGDLNFRIA---DHGMHFLRssinNSRFNLLWDRDQL 223
Cdd:cd09099   155 CSHLTAGQNQVKERNEDYKEI--TQKLSFPMGRNVFSHDYVFWCGDFNYRIDltyEEVFYFIK----RQDWKKLLEFDQL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 224 SMLKKKEPILQEFEEGPLRFKPTYKFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRIKPKATEIEDEKSSTASSAD 303
Cdd:cd09099   229 QLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDT---------SDKCRTPAWTDRVLWWRKKWPFEKTAGEINLLDSDL 299
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1207189676 304 DDEFSVKVTQD----MYTCDVSYGVSDHKPVI 331
Cdd:cd09099   300 DFDTKIRHTWTpgalMYYGRAELQASDHRPVL 331
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
10-336 1.64e-43

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: 156.35  E-value: 1.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  10 GGHQ----AFRLHMVTWNVGTAEPPADVRSLLQLDSQPTtDLYVIGLQE---VNATPVRYISDlIVEDTWSHLLMETLAP 82
Cdd:cd09098    12 GGKQfrsiAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPV-DIFAIGFEEmveLNAGNIVSAST-TNQKLWAAELQKTISR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  83 EG-YIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRM 161
Cdd:cd09098    90 DQkYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 162 DEFEYILDTQEFDMFNTpqVLDHKVVFWFGDLNFRIaDHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPL 241
Cdd:cd09098   170 EDFIEIARKLSFPMGRM--LFSHDYVFWCGDFNYRI-DIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 242 RFKPTYKFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRIK--PKATEIEDEKSSTASSADDDEFSVKVTQD--MYT 317
Cdd:cd09098   247 DFAPTYKYDLFSDDYDT---------SEKCRTPAWTDRVLWRRRkwPFDRSAEDLDLLNASFPDNSKEQYTWSPGtlLHY 317
                         330
                  ....*....|....*....
gi 1207189676 318 CDVSYGVSDHKPVIGTFNL 336
Cdd:cd09098   318 GRAELKTSDHRPVVALIDI 336
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
12-349 3.04e-43

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 158.41  E-value: 3.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  12 HQAFRLHMVTWNVGTAEPPADVRSLLQLDSQ--PTTDLYVIGLQEVNA-TPVRYIS------DLIVEDTWSHLLMETLAP 82
Cdd:COG5411    27 EKDVSIFVSTFNPPGKPPKASTKRWLFPEIEatELADLYVVGLQEVVElTPGSILSadpydrLRIWESKVLDCLNGAQSD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  83 EGYIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMD 162
Cdd:COG5411   107 EKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 163 EFEYILDTQEFDmfNTPQVLDHKVVFWFGDLNFRIAdhGMHF-LRSSINN--SRFNLLWDRDQLSMLKKKEPILQEFEEG 239
Cdd:COG5411   187 DYRSIASNICFS--RGLRIYDHDTIFWLGDLNYRVT--STNEeVRPEIASddGRLDKLFEYDQLLWEMEVGNVFPGFKEP 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 240 PLRFKPTYKFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRikpkateiedeksstassadddefSVKVTQDMYTCD 319
Cdd:COG5411   263 VITFPPTYKFDYGTDEYDT---------SDKGRIPSWTDRILYK------------------------SEQLTPHSYSSI 309
                         330       340       350
                  ....*....|....*....|....*....|
gi 1207189676 320 VSYGVSDHKPVIGTFNLEMRKKVETPLVAL 349
Cdd:COG5411   310 PHLMISDHRPVYATFRAKIKVVDPSKKEGL 339
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
16-336 8.90e-40

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: 145.26  E-value: 8.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  16 RLHMVTWNV-GTAEPPADVRS-LLQLDSQPTTDLYVIGLQEvnATPVRYisdlivedTWSHLLMETLAPEgYIKVTSVRM 93
Cdd:cd09095     6 GIFVATWNMqGQKELPENLDDfLLPTSADFAQDIYVIGVQE--GCSDRR--------EWEIRLQETLGPS-HVLLHSASH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  94 QGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYI-----L 168
Cdd:cd09095    75 GVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYNKIiqalnL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 169 DTQEFDM---FNTPQVLDH-KVVFWFGDLNFRIaDHGMHFLRSSINNSRFNL---LWDRDQLSMLKKKEPILQEFEEGPL 241
Cdd:cd09095   155 PRNVPTNpykSESGDVTTRfDEVFWFGDFNFRL-SGPRHLVDALINQGQEVDvsaLLQHDQLTREMSKGSIFKGFQEAPI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 242 RFKPTYKFDRFSETYDTraprtwfglTGKKRKPAWTDRILWRIKPKATeiedeksstassadddefsVKVTQdmYTCDVS 321
Cdd:cd09095   234 HFPPTYKFDIGSDVYDT---------SSKQRVPSYTDRILYRSRQKGD-------------------VCCLK--YNSCPS 283
                         330
                  ....*....|....*
gi 1207189676 322 YGVSDHKPVIGTFNL 336
Cdd:cd09095   284 IKTSDHRPVFALFRV 298
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
21-334 1.62e-36

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: 136.61  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  21 TWNVGTAEPPADVRSLLQLDSQPTT----------DLYVIGLQEvnatpvryisDLIVEDTWSHLLMETLAPEGYIKVTS 90
Cdd:cd09091     7 TWNMGSAPPPKNITSWFTSKGQGKTrddvadyiphDIYVIGTQE----------DPLGEKEWLDLLRHSLKELTSLDYKP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  91 VRMQGLL---LILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYI 167
Cdd:cd09091    77 IAMQTLWnirIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQNYLNI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 168 -----LDTQEFDMFNTPQVLDHkvVFWFGDLNFRIADHGMHFLR--SSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGP 240
Cdd:cd09091   157 lrflsLGDKKLSAFNITHRFTH--LFWLGDLNYRLDLPIQEAENiiQKIEQQQFEPLLRHDQLNLEREEHKVFLRFSEEE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 241 LRFKPTYKFDRFS-ETYDTRAPRTwfglTGKKRK-PAWTDRILWRIKPKateiedeksstassadddefsVKVTQDMYTC 318
Cdd:cd09091   235 ITFPPTYRYERGSrDTYAYTKQKA----TGVKYNlPSWCDRILWKSYPE---------------------THIICQSYGC 289
                         330
                  ....*....|....*.
gi 1207189676 319 DVSYGVSDHKPVIGTF 334
Cdd:cd09091   290 TDDIVTSDHSPVFGTF 305
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
21-334 5.92e-34

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


Pssm-ID: 197334  Cd Length: 307  Bit Score: 129.72  E-value: 5.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  21 TWNVGTAEPPADVRSLLQLDSQPTT----------DLYVIGLQEvnatpvryisDLIVEDTWSHLLMETLAPEGYIKVTS 90
Cdd:cd09100     7 TWNMGNAPPPKKITSWFQCKGQGKTrddtadyiphDIYVIGTQE----------DPLGEKEWLDTLKHSLREITSISFKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  91 VRMQGLL---LILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYI 167
Cdd:cd09100    77 IAIQTLWnirIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQNYFNI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 168 L-----DTQEFDMFNTPQVLDHkvVFWFGDLNFRI--ADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGP 240
Cdd:cd09100   157 LrflvlGDKKLSPFNITHRFTH--LFWLGDLNYRVelPNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQFEEEE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 241 LRFKPTYKFDRFSEtydTRAPRTWFGLTGKKRK-PAWTDRILWRIKPKateiedeksstassadddefsVKVTQDMYTCD 319
Cdd:cd09100   235 ITFAPTYRFERGTR---ERYAYTKQKATGMKYNlPSWCDRVLWKSYPL---------------------VHVVCQSYGCT 290
                         330
                  ....*....|....*
gi 1207189676 320 VSYGVSDHKPVIGTF 334
Cdd:cd09100   291 DDITTSDHSPVFATF 305
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
21-336 4.32e-33

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: 127.01  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  21 TWNVGTAEPPADVRSLL-------QLDSQPTT---DLYVIGLQEvnatpvryisDLIVEDTWSHLLMETLAPEGYIKVTS 90
Cdd:cd09101     7 TWNMGSVPPPKSLASWLtsrglgkTLDETTVTiphDIYVFGTQE----------NSVGDREWVDFLRASLKELTDIDYQP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  91 VRMQGLL---LILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYI 167
Cdd:cd09101    77 IALQCLWnikMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTHRRNQNYLDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 168 LDT-----QEFDMFNTPQVLDHkvVFWFGDLNFRIaDHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLR 242
Cdd:cd09101   157 LRSlslgdKQLNAFDISLRFTH--LFWFGDLNYRL-DMDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFREEEIS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 243 FKPTYKFDRFSetydtRAPRTW--FGLTGKKRK-PAWTDRILWRIKPKATEIEDeksstassadddefSVKVTQDMYTcd 319
Cdd:cd09101   234 FPPTYRYERGS-----RDTYMWqkQKTTGMRTNvPSWCDRILWKSYPETHIVCN--------------SYGCTDDIVT-- 292
                         330
                  ....*....|....*..
gi 1207189676 320 vsygvSDHKPVIGTFNL 336
Cdd:cd09101   293 -----SDHSPVFGTFEV 304
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
347-447 3.73e-32

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: 118.12  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 347 VALTVEGIWS-ADEDAIFTYTILENFESSTFDWIGLYKIGFKSASDYSTFAWVKDDEVAANGEVVMVQMNKNELPLL-AG 424
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPKEpEG 80
                          90       100
                  ....*....|....*....|...
gi 1207189676 425 DYVLGYFStNMQTLIAFSPNFQI 447
Cdd:pfam17751  81 FYQFCYVS-NLGSVVGISTPFQF 102
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
85-338 2.02e-29

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 121.55  E-value: 2.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  85 YIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAA-HMNYALQR--M 161
Cdd:PLN03191  364 YVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRrnA 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 162 DEFEYILDTQEFDMFNTPQ---VLDHKVVFWFGDLNFRI----ADhgmhfLRSSINNSRFNLLWDRDQLSMLKKKEPILQ 234
Cdd:PLN03191  444 DVYEIIRRTRFSSVLDTDQpqtIPSHDQIFWFGDLNYRLnmldTE-----VRKLVAQKRWDELINSDQLIKELRSGHVFD 518
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 235 EFEEGPLRFKPTYKFDRFSETYDTRAPRTwfglTGKKRKPAWTDRILWrikpkateiedeksstassadddeFSVKVTQD 314
Cdd:PLN03191  519 GWKEGPIKFPPTYKYEINSDRYVGENPKE----GEKKRSPAWCDRILW------------------------LGKGIKQL 570
                         250       260
                  ....*....|....*....|....
gi 1207189676 315 MYTcDVSYGVSDHKPVIGTFNLEM 338
Cdd:PLN03191  571 CYK-RSEIRLSDHRPVSSMFLVEV 593
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
126-336 7.07e-11

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: 63.64  E-value: 7.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 126 WGNKGGISVRFSFYGEMLCFLNCHL--------AAHMN---YALQRMDEFEYILDTQEFDMFNTPQVldhkvvFWFGDLN 194
Cdd:cd09092   152 WSRKGFMRTRWKINNCVFDLVNIHLfhdasnlaACESSpsvYSQNRHRALGYVLERLTDERFEKVPF------FVFGDFN 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 195 FRI----------ADHGMHFLRSSINNSRFNLLWDRDQ------LSMLKKK------------------------EPILQ 234
Cdd:cd09092   226 FRLdtksvvetlcAKATMQTVRKADSNIVVKLEFREKDndnkvvLQIEKKKfdyfnqdvfrdnngkallkfdkelEVFKD 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 235 EFEEGPLRFKPTYKFdrfSEtyDTRAPRTWFgltgKKRKPAWTDRILWRIKPKATEIEDEKSStassadddefsvkVTQD 314
Cdd:cd09092   306 VLYELDISFPPSYPY---SE--DPEQGTQYM----NTRCPAWCDRILMSHSARELKSENEEKS-------------VTYD 363
                         250       260
                  ....*....|....*....|..
gi 1207189676 315 MYTCDVSYGvsDHKPVIGTFNL 336
Cdd:cd09092   364 MIGPNVCMG--DHKPVFLTFRI 383
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
21-312 8.41e-05

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: 44.01  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  21 TWNVGTAEPPADVRSLLQLDSQptTDLYVIGLQEVNATPvryisdlivedtWSHLLMETLAPEGYIKVTSVRMQG----- 95
Cdd:cd08372     3 SYNVNGLNAATRASGIARWVRE--LDPDIVCLQEVKDSQ------------YSAVALNQLLPEGYHQYQSGPSRKegyeg 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676  96 -LLLILFAKQvhlpfirDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDtqefD 174
Cdd:cd08372    69 vAILSKTPKF-------KIVEKHQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLE----F 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207189676 175 MFNTPQVLDHKVVfWFGDLNFRIADHGMHFLRSSIN-NSRFNLLWdrdqlsmlkkkepilqEFEEGPlrFKPTYKFDRfs 253
Cdd:cd08372   138 LKRLRQPNSAPVV-ICGDFNVRPSEVDSENPSSMLRlFVALNLVD----------------SFETLP--HAYTFDTYM-- 196
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207189676 254 etydtraprtwfgltgkKRKPAWTDRILWR----IKPKATEIEDEKSSTASSAddDEFSVKVT 312
Cdd:cd08372   197 -----------------HNVKSRLDYIFVSksllPSVKSSKILSDAARARIPS--DHYPIEVT 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.
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