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Conserved domains on  [gi|442616634|ref|NP_001259623|]
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uncharacterized protein Dmel_CG9784, isoform C [Drosophila melanogaster]

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 ...
 31-341 9.05e-172

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: 486.49  E-value: 9.05e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  31 YRVYVVTWNVGSRfPDNISLRHLLGLQDvtvdkdtketNAHLPDIYALGLQEVNAQPQQQVLGLFKEDPWTHKAKELLRN 110
Cdd:cd09094    1 LRVYVVTWNVATA-PPPIDVRSLLGLQS----------PEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 111 YDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDERIE 190
Cdd:cd09094   70 KGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRID 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 191 DYKQILENHHYHVKRYREIYDHDYVFWFGDLNFRLQGsDSSTEVRELVRDEsQHEALIQRDQLYQVREKsQLAFQVLQER 270
Cdd:cd09094  150 DFETILSTQVFNECNTPSILDHDYVFWFGDLNFRIED-VSIEFVRELVNSK-KYHLLLEKDQLNMAKRK-EEAFQGFQEG 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616634 271 LPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYAVQPLNRQPGMQLSIEQCSYKSHPLYTISDHKPVTSDFTI 341
Cdd:cd09094  227 PLNFAPTYKFDLGTDEYDTsgkKRKPAWTDRILWKVNPDASTEEKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
SKICH super family cl39277
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 352-415 4.28e-08

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: 51.09  E-value: 4.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442616634  352 VVFSPLSLWK-IGDENTVEYHKQAEFDEGSNDWIGIFPSEYASLADYVAYEYVNQAESPSSSDSN 415
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVR 65
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 31-341 9.05e-172

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: 486.49  E-value: 9.05e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  31 YRVYVVTWNVGSRfPDNISLRHLLGLQDvtvdkdtketNAHLPDIYALGLQEVNAQPQQQVLGLFKEDPWTHKAKELLRN 110
Cdd:cd09094    1 LRVYVVTWNVATA-PPPIDVRSLLGLQS----------PEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 111 YDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDERIE 190
Cdd:cd09094   70 KGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRID 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 191 DYKQILENHHYHVKRYREIYDHDYVFWFGDLNFRLQGsDSSTEVRELVRDEsQHEALIQRDQLYQVREKsQLAFQVLQER 270
Cdd:cd09094  150 DFETILSTQVFNECNTPSILDHDYVFWFGDLNFRIED-VSIEFVRELVNSK-KYHLLLEKDQLNMAKRK-EEAFQGFQEG 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616634 271 LPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYAVQPLNRQPGMQLSIEQCSYKSHPLYTISDHKPVTSDFTI 341
Cdd:cd09094  227 PLNFAPTYKFDLGTDEYDTsgkKRKPAWTDRILWKVNPDASTEEKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 32-342 4.81e-76

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 241.87  E-value: 4.81e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634    32 RVYVVTWNVGSRFPDNISLRHLLGLQDVTVDKdtketnaHLPDIYALGLQEVN--AQPQQQVLGLFKEDPW-THKAKELL 108
Cdd:smart00128   4 KVLIGTWNVGGLESPKVDVTSWLFQKIEVKQS-------EKPDIYVIGLQEVVglAPGVILETIAGKERLWsDLLESSLN 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634   109 RNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDER 188
Cdd:smart00128  77 GDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634   189 IEDYKQILENHHYHVKRYREIYDHDYVFWFGDLNFRLQgSDSSTEVRELVRdESQHEALIQRDQLYQVREKSQlAFQVLQ 268
Cdd:smart00128 157 NQDYKTILRALSFPERALLSQFDHDVVFWFGDLNFRLD-SPSYEEVRRKIS-KKEFDDLLEKDQLNRQREAGK-VFKGFQ 233

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616634   269 ERLPAFPPTFKF-REGTSEYDL---KRRPAWTDRIMYavqplnRQPGMQLsIEQCSYKSHPLYTISDHKPVTSDFTIK 342
Cdd:smart00128 234 EGPITFPPTYKYdSVGTETYDTsekKRVPAWCDRILY------RSNGPEL-IQLSEYHSGMEITTSDHKPVFATFRLK 304
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
10-356 8.27e-53

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 185.37  E-value: 8.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  10 PKIPDSEPDGSKGKGKQQLETYRVYV-VTWNVGSRFPDNISLRHLLGLQDVTVDKDTKetnahLPDIYALGLQEVNAQPQ 88
Cdd:COG5411    3 VPIYDPRHPYIVAVLRQRRSKYVIEKdVSIFVSTFNPPGKPPKASTKRWLFPEIEATE-----LADLYVVGLQEVVELTP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  89 QQVLGLF---KEDPWTHKAKELL----RNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVS 161
Cdd:COG5411   78 GSILSADpydRLRIWESKVLDCLngaqSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 162 VRFTLYGCGLAFVVAHLTAHDHMMDERIEDYKQILENHHYhvKRYREIYDHDYVFWFGDLNFRLQgSDSSTEVRELVRDE 241
Cdd:COG5411  158 IRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICF--SRGLRIYDHDTIFWLGDLNYRVT-STNEEVRPEIASDD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 242 SQHEALIQRDQLYQVREKsQLAFQVLQERLPAFPPTFKFREGTSEYDLK---RRPAWTDRIMYAvqplnrqpGMQLsiEQ 318
Cdd:COG5411  235 GRLDKLFEYDQLLWEMEV-GNVFPGFKEPVITFPPTYKFDYGTDEYDTSdkgRIPSWTDRILYK--------SEQL--TP 303

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 442616634 319 CSYKSHPLYTISDHKPVtsdftiklYPNVRAPGVVFSP 356
Cdd:COG5411  304 HSYSSIPHLMISDHRPV--------YATFRAKIKVVDP 333
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 113-343 9.65e-35

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 138.12  E-value: 9.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 113 YVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTA--HDHMMDERIE 190
Cdd:PLN03191 364 YVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSghKDGAEQRRNA 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 191 DYKQILENHHYH----VKRYREIYDHDYVFWFGDLNFRLQGSDssTEVRELVrDESQHEALIQRDQLyqVRE-KSQLAFQ 265
Cdd:PLN03191 444 DVYEIIRRTRFSsvldTDQPQTIPSHDQIFWFGDLNYRLNMLD--TEVRKLV-AQKRWDELINSDQL--IKElRSGHVFD 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 266 VLQERLPAFPPTFKFR--------EGTSEYDLKRRPAWTDRIMYavqplnrqpgMQLSIEQCSYKSHPLyTISDHKPVTS 337
Cdd:PLN03191 519 GWKEGPIKFPPTYKYEinsdryvgENPKEGEKKRSPAWCDRILW----------LGKGIKQLCYKRSEI-RLSDHRPVSS 587


                 ....*.
gi 442616634 338 DFTIKL 343
Cdd:PLN03191 588 MFLVEV 593
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 352-415 4.28e-08

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: 51.09  E-value: 4.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442616634  352 VVFSPLSLWK-IGDENTVEYHKQAEFDEGSNDWIGIFPSEYASLADYVAYEYVNQAESPSSSDSN 415
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVR 65
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 31-341 9.05e-172

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: 486.49  E-value: 9.05e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  31 YRVYVVTWNVGSRfPDNISLRHLLGLQDvtvdkdtketNAHLPDIYALGLQEVNAQPQQQVLGLFKEDPWTHKAKELLRN 110
Cdd:cd09094    1 LRVYVVTWNVATA-PPPIDVRSLLGLQS----------PEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 111 YDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDERIE 190
Cdd:cd09094   70 KGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRID 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 191 DYKQILENHHYHVKRYREIYDHDYVFWFGDLNFRLQGsDSSTEVRELVRDEsQHEALIQRDQLYQVREKsQLAFQVLQER 270
Cdd:cd09094  150 DFETILSTQVFNECNTPSILDHDYVFWFGDLNFRIED-VSIEFVRELVNSK-KYHLLLEKDQLNMAKRK-EEAFQGFQEG 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616634 271 LPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYAVQPLNRQPGMQLSIEQCSYKSHPLYTISDHKPVTSDFTI 341
Cdd:cd09094  227 PLNFAPTYKFDLGTDEYDTsgkKRKPAWTDRILWKVNPDASTEEKFLSITQTSYKSHMEYGISDHKPVTAQFRL 300
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 32-341 5.53e-80

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: 251.87  E-value: 5.53e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNVGSRFPDNISLRHLLGLQDVtvdkdtketnaHLPDIYALGLQEVNAQPQQQVLGLF--KEDPWTHKAKELL- 108
Cdd:cd09074    2 KIFVVTWNVGGGISPPENLENWLSPKGT-----------EAPDIYAVGVQEVDMSVQGFVGNDDsaKAREWVDNIQEALn 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 109 RNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFG--GIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMD 186
Cdd:cd09074   71 EKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGggGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 187 ERIEDYKQILenhHYHVKRYRE-----IYDHDYVFWFGDLNFRLQGSDSstEVRELVrDESQHEALIQRDQLYQVREKSQ 261
Cdd:cd09074  151 RRNQDYRDIL---SKLKFYRGDpaidsIFDHDVVFWFGDLNYRIDSTDD--EVRKLI-SQGDLDDLLEKDQLKKQKEKGK 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 262 LaFQVLQERLPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYAVQPlnrqpgmQLSIEQCSYKSHPLYTISDHKPVTSD 338
Cdd:cd09074  225 V-FDGFQELPITFPPTYKFDPGTDEYDTsdkKRIPAWCDRILYKSKA-------GSEIQPLSYTSVPLYKTSDHKPVRAT 296


                 ...
gi 442616634 339 FTI 341
Cdd:cd09074  297 FRV 299
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 32-342 4.81e-76

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 241.87  E-value: 4.81e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634    32 RVYVVTWNVGSRFPDNISLRHLLGLQDVTVDKdtketnaHLPDIYALGLQEVN--AQPQQQVLGLFKEDPW-THKAKELL 108
Cdd:smart00128   4 KVLIGTWNVGGLESPKVDVTSWLFQKIEVKQS-------EKPDIYVIGLQEVVglAPGVILETIAGKERLWsDLLESSLN 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634   109 RNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDER 188
Cdd:smart00128  77 GDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634   189 IEDYKQILENHHYHVKRYREIYDHDYVFWFGDLNFRLQgSDSSTEVRELVRdESQHEALIQRDQLYQVREKSQlAFQVLQ 268
Cdd:smart00128 157 NQDYKTILRALSFPERALLSQFDHDVVFWFGDLNFRLD-SPSYEEVRRKIS-KKEFDDLLEKDQLNRQREAGK-VFKGFQ 233

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616634   269 ERLPAFPPTFKF-REGTSEYDL---KRRPAWTDRIMYavqplnRQPGMQLsIEQCSYKSHPLYTISDHKPVTSDFTIK 342
Cdd:smart00128 234 EGPITFPPTYKYdSVGTETYDTsekKRVPAWCDRILY------RSNGPEL-IQLSEYHSGMEITTSDHKPVFATFRLK 304
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 32-341 1.28e-62

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: 206.40  E-value: 1.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNVGSRFPDNiSLRHLLglqdvtvDKDTKEtnahlPDIYALGLQEVNAQPQQQVLG-LFKEDPWtHKA--KELL 108
Cdd:cd09093    2 RIFVGTWNVNGQSPDE-SLRPWL-------SCDEEP-----PDIYAIGFQELDLSAEAFLFNdSSREQEW-VKAveRGLH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 109 RNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDER 188
Cdd:cd09093   68 PDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 189 IEDYKQILENHHYHVKRYRE--IYDHDYVFWFGDLNFRLQGSDSStEVRELVrDESQHEALIQRDQLYQVREKSQlAFQV 266
Cdd:cd09093  148 NQDYKDICARMKFEDPDGPPlsISDHDVVFWLGDLNYRIQELPTE-EVKELI-EKNDLEELLKYDQLNIQRRAGK-VFEG 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616634 267 LQERLPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYAVQplnrqpgmqlSIEQCSYKSHPLYTISDHKPVTSDFTI 341
Cdd:cd09093  225 FTEGEINFIPTYKYDPGTDNWDSsekCRAPAWCDRILWRGT----------NIVQLSYRSHMELKTSDHKPVSALFDI 292
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 32-339 9.96e-61

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: 201.41  E-value: 9.96e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNVGSRFPDnISLRHLLglqdvtvdkdTKETNAHLPDIYALGLQEVNAQPQQQVLGLFKEDP--WTHKAKELLR 109
Cdd:cd09090    2 NIFVGTFNVNGKSYK-DDLSSWL----------FPEENDELPDIVVIGLQEVVELTAGQILNSDPSKSsfWEKKIKTTLN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 110 NYD---YVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMD 186
Cdd:cd09090   71 GRGgekYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 187 ERIEDYKQILENHHYhvKRYREIYDHDYVFWFGDLNFRLqgSDSSTEVRELVRDESQHEaLIQRDQLYQVReKSQLAFQV 266
Cdd:cd09090  151 ERNNDYKTIARGLRF--SRGRTIKDHDHVIWLGDFNYRI--SLTNEDVRRFILNGKLDK-LLEYDQLNQQM-NAGEVFPG 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442616634 267 LQERLPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYavqplnrqpgMQLSIEQCSYKSHPLYtISDHKPVTSDF 339
Cdd:cd09090  225 FSEGPITFPPTYKYDKGTDNYDTsekQRIPAWTDRILY----------RGENLRQLSYNSAPLR-FSDHRPVYATF 289
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
10-356 8.27e-53

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 185.37  E-value: 8.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  10 PKIPDSEPDGSKGKGKQQLETYRVYV-VTWNVGSRFPDNISLRHLLGLQDVTVDKDTKetnahLPDIYALGLQEVNAQPQ 88
Cdd:COG5411    3 VPIYDPRHPYIVAVLRQRRSKYVIEKdVSIFVSTFNPPGKPPKASTKRWLFPEIEATE-----LADLYVVGLQEVVELTP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  89 QQVLGLF---KEDPWTHKAKELL----RNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVS 161
Cdd:COG5411   78 GSILSADpydRLRIWESKVLDCLngaqSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 162 VRFTLYGCGLAFVVAHLTAHDHMMDERIEDYKQILENHHYhvKRYREIYDHDYVFWFGDLNFRLQgSDSSTEVRELVRDE 241
Cdd:COG5411  158 IRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICF--SRGLRIYDHDTIFWLGDLNYRVT-STNEEVRPEIASDD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 242 SQHEALIQRDQLYQVREKsQLAFQVLQERLPAFPPTFKFREGTSEYDLK---RRPAWTDRIMYAvqplnrqpGMQLsiEQ 318
Cdd:COG5411  235 GRLDKLFEYDQLLWEMEV-GNVFPGFKEPVITFPPTYKFDYGTDEYDTSdkgRIPSWTDRILYK--------SEQL--TP 303

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 442616634 319 CSYKSHPLYTISDHKPVtsdftiklYPNVRAPGVVFSP 356
Cdd:COG5411  304 HSYSSIPHLMISDHRPV--------YATFRAKIKVVDP 333
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 32-341 7.13e-52

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: 179.51  E-value: 7.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNV-GSRFPDNISLRH------LLGLQDVT-VDKDTKETNAHLPDIYALGLQE---------VNA-QPQQQVLG 93
Cdd:cd09089    2 RVFVGTWNVnGGKHFRSIAFKHqsmtdwLLDNPKLAgQCSNDSEEDEKPVDIFAIGFEEmvdlnasniVSAsTTNQKEWG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  94 LFKEdpwthkaKELLRNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAF 173
Cdd:cd09089   82 EELQ-------KTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCF 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 174 VVAHLTAHDHMMDERIEDYKQILENHHYHVKryREIYDHDYVFWFGDLNFRLQGSDSstEVRELVRDESqHEALIQRDQL 253
Cdd:cd09089  155 VCSHFAAGQSQVKERNEDFAEIARKLSFPMG--RTLDSHDYVFWCGDFNYRIDLPND--EVKELVRNGD-WLKLLEFDQL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 254 yQVREKSQLAFQVLQERLPAFPPTFKFREGTSEYDLK---RRPAWTDRIMYAVQPLNRQPGMQLSIEQCSYKSHP----- 325
Cdd:cd09089  230 -TKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDTSekcRTPAWTDRVLWRRRKWPSDKTEESLVETNDPTWNPgtlly 308

                        330       340
                 ....*....|....*....|.
gi 442616634 326 -----LYTiSDHKPVTSDFTI 341
Cdd:cd09089  309 ygraeLKT-SDHRPVVAIIDI 328
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 32-301 6.72e-44

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: 158.26  E-value: 6.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNV--GSRFPDNIslrhlLGLQDVT---VDK-------DTKETNAHLPDIYALGLQE---------VNAQPQQQ 90
Cdd:cd09099    2 RVAMGTWNVngGKQFRSNI-----LGTSELTdwlLDSpklsgtpDFQDDESNPPDIFAVGFEEmvelsagniVNASTTNR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  91 VLglfkedpWTHK-AKELLRNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGC 169
Cdd:cd09099   77 KM-------WGEQlQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYST 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 170 GLAFVVAHLTAHDHMMDERIEDYKQIleNHHYHVKRYREIYDHDYVFWFGDLNFRLqgSDSSTEVRELVRDESQhEALIQ 249
Cdd:cd09099  150 SFCFICSHLTAGQNQVKERNEDYKEI--TQKLSFPMGRNVFSHDYVFWCGDFNYRI--DLTYEEVFYFIKRQDW-KKLLE 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442616634 250 RDQLyQVREKSQLAFQVLQERLPAFPPTFKFREGTSEYDLK---RRPAWTDRIMY 301
Cdd:cd09099  225 FDQL-QLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSdkcRTPAWTDRVLW 278
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 32-337 1.76e-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: 157.12  E-value: 1.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNV--GSRFpDNISLRH------LLGLQDVTVDKDTKETNAHLPDIYALGLQE---------VNAQPQQQVLgl 94
Cdd:cd09098    2 RVCVGTWNVngGKQF-RSIAFKNqtltdwLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEmvelnagniVSASTTNQKL-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  95 fkedpWTHK-AKELLRNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAF 173
Cdd:cd09098   79 -----WAAElQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 174 VVAHLTAHDHMMDERIEDYKQILENHHYHVKRYreIYDHDYVFWFGDLNFRLQGSDSstEVRELVRDESQhEALIQRDQL 253
Cdd:cd09098  154 VCSHFAAGQSQVKERNEDFIEIARKLSFPMGRM--LFSHDYVFWCGDFNYRIDIPNE--EVKELIRQQNW-DSLIAGDQL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 254 YQVREKSQLAFQVLQERLpAFPPTFKFREGTSEYDLK---RRPAWTDRIMYAVQ--PLNRQP-GMQLSIEQCSYKSHPLY 327
Cdd:cd09098  229 INQKNAGQVFRGFLEGKL-DFAPTYKYDLFSDDYDTSekcRTPAWTDRVLWRRRkwPFDRSAeDLDLLNASFPDNSKEQY 307

                        330       340
                 ....*....|....*....|....*
gi 442616634 328 T---------------ISDHKPVTS 337
Cdd:cd09098  308 TwspgtllhygraelkTSDHRPVVA 332
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 32-335 6.80e-38

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: 141.02  E-value: 6.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  32 RVYVVTWNVGSR--FPDNislrhllgLQDVTVDKDTKetnaHLPDIYALGLQEvnaqpqqqvlGLFKEDPWTHKAKELLR 109
Cdd:cd09095    6 GIFVATWNMQGQkeLPEN--------LDDFLLPTSAD----FAQDIYVIGVQE----------GCSDRREWEIRLQETLG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 110 NYdYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDERI 189
Cdd:cd09095   64 PS-HVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 190 EDYKQILENHHYHVKRYREIYDH---------DYVFWFGDLNFRLQGsdSSTEVRELVRDESQH--EALIQRDQLYQVRE 258
Cdd:cd09095  143 LDYNKIIQALNLPRNVPTNPYKSesgdvttrfDEVFWFGDFNFRLSG--PRHLVDALINQGQEVdvSALLQHDQLTREMS 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 259 KSQlAFQVLQERLPAFPPTFKFREGTSEYDL---KRRPAWTDRIMYavqpLNRQPGmqlSIEQCSYKSHPLYTISDHKPV 335
Cdd:cd09095  221 KGS-IFKGFQEAPIHFPPTYKFDIGSDVYDTsskQRVPSYTDRILY----RSRQKG---DVCCLKYNSCPSIKTSDHRPV 292
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 113-343 9.65e-35

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 138.12  E-value: 9.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 113 YVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTA--HDHMMDERIE 190
Cdd:PLN03191 364 YVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSghKDGAEQRRNA 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 191 DYKQILENHHYH----VKRYREIYDHDYVFWFGDLNFRLQGSDssTEVRELVrDESQHEALIQRDQLyqVRE-KSQLAFQ 265
Cdd:PLN03191 444 DVYEIIRRTRFSsvldTDQPQTIPSHDQIFWFGDLNYRLNMLD--TEVRKLV-AQKRWDELINSDQL--IKElRSGHVFD 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 266 VLQERLPAFPPTFKFR--------EGTSEYDLKRRPAWTDRIMYavqplnrqpgMQLSIEQCSYKSHPLyTISDHKPVTS 337
Cdd:PLN03191 519 GWKEGPIKFPPTYKYEinsdryvgENPKEGEKKRSPAWCDRILW----------LGKGIKQLCYKRSEI-RLSDHRPVSS 587


                 ....*.
gi 442616634 338 DFTIKL 343
Cdd:PLN03191 588 MFLVEV 593
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 33-341 7.05e-32

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: 124.67  E-value: 7.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  33 VYVVTWNVGSRFP-DNISLRHLLGLQDVTVDkDTKETNAHlpDIYALGLQEvNAQPQQQVLGLFKedpwtHKAKELlRNY 111
Cdd:cd09091    3 IFIGTWNMGSAPPpKNITSWFTSKGQGKTRD-DVADYIPH--DIYVIGTQE-DPLGEKEWLDLLR-----HSLKEL-TSL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 112 DYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDERIED 191
Cdd:cd09091   73 DYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 192 YKQILENHHYHVKR---YREIYDHDYVFWFGDLNFRLQGSDSSTEVRELVRDESQHEALIQRDQLYQVREKSQLAFQVLQ 268
Cdd:cd09091  153 YLNILRFLSLGDKKlsaFNITHRFTHLFWLGDLNYRLDLPIQEAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFLRFSE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 269 ERLpAFPPTFKFREGTSE-------------YDLkrrPAWTDRIMYAVQPlnrqpgmQLSIEQCSYKSHPLYTISDHKPV 335
Cdd:cd09091  233 EEI-TFPPTYRYERGSRDtyaytkqkatgvkYNL---PSWCDRILWKSYP-------ETHIICQSYGCTDDIVTSDHSPV 301


                 ....*.
gi 442616634 336 TSDFTI 341
Cdd:cd09091  302 FGTFEV 307
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 33-341 5.15e-30

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: 119.32  E-value: 5.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  33 VYVVTWNVGSRFP-DNISLRHLLGLQDVTVDkdtkETNAHLP-DIYALGLQEvnaQPQqqvlglfKEDPWTHKAKELLRN 110
Cdd:cd09100    3 IFIGTWNMGNAPPpKKITSWFQCKGQGKTRD----DTADYIPhDIYVIGTQE---DPL-------GEKEWLDTLKHSLRE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 111 YDYVAVKTEQMQGLL---LSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDE 187
Cdd:cd09100   69 ITSISFKVIAIQTLWnirIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 188 RIEDYKQILENHHYHVKR---YREIYDHDYVFWFGDLNFRLQgsDSSTEVRELVRD--ESQHEALIQRDQLYQVREKSQL 262
Cdd:cd09100  149 RNQNYFNILRFLVLGDKKlspFNITHRFTHLFWLGDLNYRVE--LPNTEAENIIQKikQQQYQELLPHDQLLIERKESKV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 263 AFQVLQERLpAFPPTFKFREGTSE-------------YDLkrrPAWTDRIMYAVQPLnrqpgmqLSIEQCSYKSHPLYTI 329
Cdd:cd09100  227 FLQFEEEEI-TFAPTYRFERGTREryaytkqkatgmkYNL---PSWCDRVLWKSYPL-------VHVVCQSYGCTDDITT 295

                        330
                 ....*....|..
gi 442616634 330 SDHKPVTSDFTI 341
Cdd:cd09100  296 SDHSPVFATFEV 307
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 33-341 1.21e-26

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: 109.68  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  33 VYVVTWNVGSRFPDN-----ISLRHLLGLQDvtvdkdtkETNAHLP-DIYALGLQEVNAQPQQQVlglfkeDPWTHKAKE 106
Cdd:cd09101    3 IFIGTWNMGSVPPPKslaswLTSRGLGKTLD--------ETTVTIPhDIYVFGTQENSVGDREWV------DFLRASLKE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 107 LLrNYDYVAVKTEQMQGLLLSMFVRRQHVEHLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMD 186
Cdd:cd09101   69 LT-DIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTH 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 187 ERIEDYKQILENHHYHVKRYREiYD----HDYVFWFGDLNFRLqgsdsSTEVRELVR--DESQHEALIQRDQLYQVREKS 260
Cdd:cd09101  148 RRNQNYLDILRSLSLGDKQLNA-FDislrFTHLFWFGDLNYRL-----DMDIQEILNyiTRKEFDPLLAVDQLNLEREKN 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 261 QLAFQVLQERLpAFPPTFKFREGTSE-YDLKRR---------PAWTDRIMYAVQPlnrqpgmQLSIEQCSYKSHPLYTIS 330
Cdd:cd09101  222 KVFLRFREEEI-SFPPTYRYERGSRDtYMWQKQkttgmrtnvPSWCDRILWKSYP-------ETHIVCNSYGCTDDIVTS 293

                        330
                 ....*....|.
gi 442616634 331 DHKPVTSDFTI 341
Cdd:cd09101  294 DHSPVFGTFEV 304
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 35-336 1.27e-09

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: 58.65  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634  35 VVTWNVGsrfpdnislrhllGLQDVTVDKD-TKETNAHLPDIyaLGLQEVNAQPQQQVLGLFKEDPWthkakellrnYDY 113
Cdd:cd08372    1 VASYNVN-------------GLNAATRASGiARWVRELDPDI--VCLQEVKDSQYSAVALNQLLPEG----------YHQ 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 114 VAVKTEQMQGLL-LSMFVRRQhvehLQDIEAEFTRTGFGGIWGNKGAVSVRFTLYGCGLAFVVAHLTAHDHMMDERIEDY 192
Cdd:cd08372   56 YQSGPSRKEGYEgVAILSKTP----KFKIVEKHQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 193 KQILENhhyhVKRYREiYDHDYVFWFGDLNfrlqgsdsstevrelVRDESQHEALIQRdqlyQVREKSQLAFQVLQERLP 272
Cdd:cd08372  132 KEVLEF----LKRLRQ-PNSAPVVICGDFN---------------VRPSEVDSENPSS----MLRLFVALNLVDSFETLP 187

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616634 273 aFPPTFKFregtseyDLKRRPAWTDRIMYAvqplnrqPGMQLSIeqCSYKSHPLY----TISDHKPVT 336
Cdd:cd08372  188 -HAYTFDT-------YMHNVKSRLDYIFVS-------KSLLPSV--KSSKILSDAararIPSDHYPIE 238
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 154-341 3.19e-08

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: 55.55  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 154 WGNKGAVSVRFTLYGCGLAFVVAHLTaHDH----MMDERIEDYKQILENHHYHVkrYREIYDHDY----VFWFGDLNFRL 225
Cdd:cd09092  152 WSRKGFMRTRWKINNCVFDLVNIHLF-HDAsnlaACESSPSVYSQNRHRALGYV--LERLTDERFekvpFFVFGDFNFRL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 226 ------------------QGSDSSTEVRELVRD-ESQHEALIQ------------------RDQLYQVREKSQLAFQVLQ 268
Cdd:cd09092  229 dtksvvetlcakatmqtvRKADSNIVVKLEFREkDNDNKVVLQiekkkfdyfnqdvfrdnnGKALLKFDKELEVFKDVLY 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616634 269 ERLPAFPPTFKFREGTSE---YDLKRRPAWTDRIMyavqpLNRQPGMQLSIEQcsyKSHPLY-------TISDHKPVTSD 338
Cdd:cd09092  309 ELDISFPPSYPYSEDPEQgtqYMNTRCPAWCDRIL-----MSHSARELKSENE---EKSVTYdmigpnvCMGDHKPVFLT 380


                 ...
gi 442616634 339 FTI 341
Cdd:cd09092  381 FRI 383
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 352-415 4.28e-08

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: 51.09  E-value: 4.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442616634  352 VVFSPLSLWK-IGDENTVEYHKQAEFDEGSNDWIGIFPSEYASLADYVAYEYVNQAESPSSSDSN 415
Cdd:pfam17751   1 VVFQNVGEWYpPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVR 65
 
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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