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Conserved domains on  [gi|449020140|ref|NP_446084|]
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phosphatidylinositol polyphosphate 5-phosphatase type IV [Rattus norvegicus]

Protein Classification

phosphatidylinositol polyphosphate 5-phosphatase type IV( domain architecture ID 10173445)

phosphatidylinositol polyphosphate 5-phosphatase type IV specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2)

CATH:  3.60.10.10
EC:  3.1.3.36
Gene Ontology:  GO:0006661|GO:0046856|GO:0046030
PubMed:  10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 299-597 0e+00

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: 612.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 299 PDRNMALFVATWNMQGQKELPASLDEFLLPTEADYTQDLYVIGVQEGCSDRREWETRLQETLGPQYVLLSSAAHGVLYMS 378
Cdd:cd09095    1 PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLHSASHGVLHLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 379 LFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQALALPRNVPd 458
Cdd:cd09095   81 VFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYNKIIQALNLPRNVP- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 459 TNPYRSSAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEEAEIHFLPSY 538
Cdd:cd09095  160 TNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTY 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 449020140 539 KFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09095  240 KFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALFRV 298
 
Name Accession Description Interval E-value
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 299-597 0e+00

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: 612.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 299 PDRNMALFVATWNMQGQKELPASLDEFLLPTEADYTQDLYVIGVQEGCSDRREWETRLQETLGPQYVLLSSAAHGVLYMS 378
Cdd:cd09095    1 PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLHSASHGVLHLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 379 LFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQALALPRNVPd 458
Cdd:cd09095   81 VFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYNKIIQALNLPRNVP- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 459 TNPYRSSAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEEAEIHFLPSY 538
Cdd:cd09095  160 TNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTY 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 449020140 539 KFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09095  240 KFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALFRV 298
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 301-599 3.63e-66

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 219.53  E-value: 3.63e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140   301 RNMALFVATWNMQGQKElPASLDEFLLPTEADYTQ----DLYVIGVQE------------GCSDRREWETRLQETLGP-- 362
Cdd:smart00128   1 RDIKVLIGTWNVGGLES-PKVDVTSWLFQKIEVKQsekpDIYVIGLQEvvglapgviletIAGKERLWSDLLESSLNGdg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140   363 QYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLD 442
Cdd:smart00128  80 QYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140   443 YNRTIQALALPRNvPDTNPYRSsagdvttrfDEVFWFGDFNFRL-SGGRVAVEAFLKQDpevDVLALLQHDQLTREMKKG 521
Cdd:smart00128 160 YKTILRALSFPER-ALLSQFDH---------DVVFWFGDLNFRLdSPSYEEVRRKISKK---EFDDLLEKDQLNRQREAG 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449020140   522 SIFKGFEEAEIHFLPSYKFD-IGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRVKV 599
Cdd:smart00128 227 KVFKGFQEGPITFPPTYKYDsVGTETYDTSEKKRVPAWCDRILYRSNGPELIQLSEYHSGMEITTSDHKPVFATFRLKV 305
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
296-599 1.93e-53

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 189.99  E-value: 1.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 296 RYFPDRNMALFVATWNMQGqKELPASLDEFLLP-TEADYTQDLYVIGVQE------------GCSDR-REWETRLQETL- 360
Cdd:COG5411   23 KYVIEKDVSIFVSTFNPPG-KPPKASTKRWLFPeIEATELADLYVVGLQEvveltpgsilsaDPYDRlRIWESKVLDCLn 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 361 ----GPQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKV 436
Cdd:COG5411  102 gaqsDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 437 AERLLDYNRTIQALALPRN--VPDTnpyrssagdvttrfDEVFWFGDFNFRLSGGRVAVEAFLKQDpEVDVLALLQHDQL 514
Cdd:COG5411  182 EERIFDYRSIASNICFSRGlrIYDH--------------DTIFWLGDLNYRVTSTNEEVRPEIASD-DGRLDKLFEYDQL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 515 TREMKKGSIFKGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSrhkgdIC--PMKYSSCPGIKTSDHRPVY 592
Cdd:COG5411  247 LWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS-----EQltPHSYSSIPHLMISDHRPVY 321


                 ....*..
gi 449020140 593 GLFRVKV 599
Cdd:COG5411  322 ATFRAKI 328
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 362-599 6.13e-29

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 122.32  E-value: 6.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 362 PQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSG--DGKVAER 439
Cdd:PLN03191 362 QKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGhkDGAEQRR 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 440 LLDY----NRTIQALALPRNVPDTNPYRssagdvttrfDEVFWFGDFNFRL--SGGRVAVEAFLKQDPEvdvlaLLQHDQ 513
Cdd:PLN03191 442 NADVyeiiRRTRFSSVLDTDQPQTIPSH----------DQIFWFGDLNYRLnmLDTEVRKLVAQKRWDE-----LINSDQ 506

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 514 LTREMKKGSIFKGFEEAEIHFLPSYKFDIGKDTY-----DSTSKQRTPSYTDRVLYKSRHKGDICpMKYSScpgIKTSDH 588
Cdd:PLN03191 507 LIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQLC-YKRSE---IRLSDH 582

                        250
                 ....*....|.
gi 449020140 589 RPVYGLFRVKV 599
Cdd:PLN03191 583 RPVSSMFLVEV 593
 
Name Accession Description Interval E-value
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 299-597 0e+00

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: 612.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 299 PDRNMALFVATWNMQGQKELPASLDEFLLPTEADYTQDLYVIGVQEGCSDRREWETRLQETLGPQYVLLSSAAHGVLYMS 378
Cdd:cd09095    1 PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLHSASHGVLHLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 379 LFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQALALPRNVPd 458
Cdd:cd09095   81 VFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYNKIIQALNLPRNVP- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 459 TNPYRSSAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEEAEIHFLPSY 538
Cdd:cd09095  160 TNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTY 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 449020140 539 KFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09095  240 KFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALFRV 298
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 304-597 9.11e-117

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: 350.48  E-value: 9.11e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 304 ALFVATWNMQGQKELPASLDEFLLPtEADYTQDLYVIGVQEGC------------SDRREWETRLQETLGP--QYVLLSS 369
Cdd:cd09074    2 KIFVVTWNVGGGISPPENLENWLSP-KGTEAPDIYAVGVQEVDmsvqgfvgnddsAKAREWVDNIQEALNEkeNYVLLGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 370 AAHGVLYMSLFIRRDLIWFCS--EVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTI 447
Cdd:cd09074   81 AQLVGIFLFVFVKKEHLPQIKdlEVEGVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVERRNQDYRDIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 448 QALALPRNVPdtnpyrssAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDpevDVLALLQHDQLTREMKKGSIFKGF 527
Cdd:cd09074  161 SKLKFYRGDP--------AIDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQG---DLDDLLEKDQLKKQKEKGKVFDGF 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 528 EEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09074  230 QELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQPLSYTSVPLYKTSDHKPVRATFRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 303-596 4.43e-69

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: 226.45  E-value: 4.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 303 MALFVATWNMQGqKELPASLDEFLLPTEADYTQDLYVIGVQE------------GCSDRREWETRLQETL----GPQYVL 366
Cdd:cd09090    1 INIFVGTFNVNG-KSYKDDLSSWLFPEENDELPDIVVIGLQEvveltagqilnsDPSKSSFWEKKIKTTLngrgGEKYVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 367 LSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRT 446
Cdd:cd09090   80 LRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEERNNDYKTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 447 IQALALPRN--VPDtnpyrssagdvttrFDEVFWFGDFNFRLSGGRVAVEAFLKQDpevDVLALLQHDQLTREMKKGSIF 524
Cdd:cd09090  160 ARGLRFSRGrtIKD--------------HDHVIWLGDFNYRISLTNEDVRRFILNG---KLDKLLEYDQLNQQMNAGEVF 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449020140 525 KGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRhkgDICPMKYSSCPgIKTSDHRPVYGLFR 596
Cdd:cd09090  223 PGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYRGE---NLRQLSYNSAP-LRFSDHRPVYATFE 290
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 301-599 3.63e-66

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 219.53  E-value: 3.63e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140   301 RNMALFVATWNMQGQKElPASLDEFLLPTEADYTQ----DLYVIGVQE------------GCSDRREWETRLQETLGP-- 362
Cdd:smart00128   1 RDIKVLIGTWNVGGLES-PKVDVTSWLFQKIEVKQsekpDIYVIGLQEvvglapgviletIAGKERLWSDLLESSLNGdg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140   363 QYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLD 442
Cdd:smart00128  80 QYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140   443 YNRTIQALALPRNvPDTNPYRSsagdvttrfDEVFWFGDFNFRL-SGGRVAVEAFLKQDpevDVLALLQHDQLTREMKKG 521
Cdd:smart00128 160 YKTILRALSFPER-ALLSQFDH---------DVVFWFGDLNFRLdSPSYEEVRRKISKK---EFDDLLEKDQLNRQREAG 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449020140   522 SIFKGFEEAEIHFLPSYKFD-IGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRVKV 599
Cdd:smart00128 227 KVFKGFQEGPITFPPTYKYDsVGTETYDTSEKKRVPAWCDRILYRSNGPELIQLSEYHSGMEITTSDHKPVFATFRLKV 305
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 306-597 2.50e-56

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: 192.91  E-value: 2.50e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 306 FVATWNMQGQKElPASLDEFLLPTEAdyTQDLYVIGVQE----------GCSDR-REWETRLQETLGPQ--YVLLSSAAH 372
Cdd:cd09093    4 FVGTWNVNGQSP-DESLRPWLSCDEE--PPDIYAIGFQEldlsaeaflfNDSSReQEWVKAVERGLHPDakYKKVKLIRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 373 GVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQALAL 452
Cdd:cd09093   81 VGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRNQDYKDICARMKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 453 PRnvPDTNPYRSSAGDVttrfdeVFWFGDFNFRLSGGRVA-VEAFLKQDpevDVLALLQHDQLTREMKKGSIFKGFEEAE 531
Cdd:cd09093  161 ED--PDGPPLSISDHDV------VFWLGDLNYRIQELPTEeVKELIEKN---DLEELLKYDQLNIQRRAGKVFEGFTEGE 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449020140 532 IHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSrhkGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09093  230 INFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWRG---TNIVQLSYRSHMELKTSDHKPVSALFDI 292
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 303-597 5.25e-54

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: 187.60  E-value: 5.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 303 MALFVATWNMQGQKELPA------SLDEFLL-----------PTEADYTQ-DLYVIGVQE------------GCSDRREW 352
Cdd:cd09089    1 LRVFVGTWNVNGGKHFRSiafkhqSMTDWLLdnpklagqcsnDSEEDEKPvDIFAIGFEEmvdlnasnivsaSTTNQKEW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 353 ETRLQETLG--PQYVLLSSAAH-GV-LYmsLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSH 428
Cdd:cd09089   81 GEELQKTISrdHKYVLLTSEQLvGVcLF--VFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 429 FTSGDGKVAERLLDYNRTIQALALPRnvpdtnpyrssaGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDpevDVLAL 508
Cdd:cd09089  159 FAAGQSQVKERNEDFAEIARKLSFPM------------GRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNG---DWLKL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 509 LQHDQLTREMKKGSIFKGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRHK-------GDICPMKYSSCP 581
Cdd:cd09089  224 LEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWpsdkteeSLVETNDPTWNP 303

                        330       340
                 ....*....|....*....|....*
gi 449020140 582 G---------IKTSDHRPVYGLFRV 597
Cdd:cd09089  304 GtllyygraeLKTSDHRPVVAIIDI 328
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
296-599 1.93e-53

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 189.99  E-value: 1.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 296 RYFPDRNMALFVATWNMQGqKELPASLDEFLLP-TEADYTQDLYVIGVQE------------GCSDR-REWETRLQETL- 360
Cdd:COG5411   23 KYVIEKDVSIFVSTFNPPG-KPPKASTKRWLFPeIEATELADLYVVGLQEvveltpgsilsaDPYDRlRIWESKVLDCLn 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 361 ----GPQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKV 436
Cdd:COG5411  102 gaqsDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 437 AERLLDYNRTIQALALPRN--VPDTnpyrssagdvttrfDEVFWFGDFNFRLSGGRVAVEAFLKQDpEVDVLALLQHDQL 514
Cdd:COG5411  182 EERIFDYRSIASNICFSRGlrIYDH--------------DTIFWLGDLNYRVTSTNEEVRPEIASD-DGRLDKLFEYDQL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 515 TREMKKGSIFKGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSrhkgdIC--PMKYSSCPGIKTSDHRPVY 592
Cdd:COG5411  247 LWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS-----EQltPHSYSSIPHLMISDHRPVY 321


                 ....*..
gi 449020140 593 GLFRVKV 599
Cdd:COG5411  322 ATFRAKI 328
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 305-597 5.75e-50

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: 176.02  E-value: 5.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 305 LFVATWNMqGQKELPASLDEFLLPTEADYTQDLYVIGVQEGCSDRRE----------WETRLQETLGPQ-YVLLSSAAHG 373
Cdd:cd09094    3 VYVVTWNV-ATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQfvsdlifddpWSDLFMDILSPKgYVKVSSIRLQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 374 VLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQALALP 453
Cdd:cd09094   82 GLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVFN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 454 -RNVPDTNPYrssagdvttrfDEVFWFGDFNFRLSG-GRVAVEaFLKQDPEVDVLalLQHDQLTREMKKGSIFKGFEEAE 531
Cdd:cd09094  162 eCNTPSILDH-----------DYVFWFGDLNFRIEDvSIEFVR-ELVNSKKYHLL--LEKDQLNMAKRKEEAFQGFQEGP 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449020140 532 IHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKG-------DICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09094  228 LNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWKVNPDAsteekflSITQTSYKSHMEYGISDHKPVTAQFRL 300
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 303-597 7.20e-48

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: 170.51  E-value: 7.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 303 MALFVATWNMqGQKELPASLDEFLLPT--------EADYT-QDLYVIGVQEGCSDRREW----ETRLQETLGPQYVLLSS 369
Cdd:cd09091    1 ISIFIGTWNM-GSAPPPKNITSWFTSKgqgktrddVADYIpHDIYVIGTQEDPLGEKEWldllRHSLKELTSLDYKPIAM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 370 AAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQA 449
Cdd:cd09091   80 QTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQNYLNILRF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 450 LALprnvpdtNPYRSSAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEE 529
Cdd:cd09091  160 LSL-------GDKKLSAFNITHRFTHLFWLGDLNYRLDLPIQEAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFLRFSE 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449020140 530 AEIHFLPSYKFDIG-KDTYDSTSKQRT------PSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09091  233 EEITFPPTYRYERGsRDTYAYTKQKATgvkynlPSWCDRILWKSYPETHIICQSYGCTDDIVTSDHSPVFGTFEV 307
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 307-597 1.11e-46

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: 168.27  E-value: 1.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 307 VATWNMQGQKELPAS-----------LDEFLLPTEADYTQD------LYVIGVQE------------GCSDRREWETRLQ 357
Cdd:cd09099    5 MGTWNVNGGKQFRSNilgtseltdwlLDSPKLSGTPDFQDDesnppdIFAVGFEEmvelsagnivnaSTTNRKMWGEQLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 358 ETLGP--QYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGK 435
Cdd:cd09099   85 KAISRshRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 436 VAERLLDYNRTIQALALPrnvpdtnpyrssAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDpevDVLALLQHDQLT 515
Cdd:cd09099  165 VKERNEDYKEITQKLSFP------------MGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQ---DWKKLLEFDQLQ 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 516 REMKKGSIFKGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLY-------------------------KSRHKG 570
Cdd:cd09099  230 LQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWwrkkwpfektageinlldsdldfdtKIRHTW 309

                        330       340
                 ....*....|....*....|....*..
gi 449020140 571 DICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09099  310 TPGALMYYGRAELQASDHRPVLAIVEV 336
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 303-597 1.17e-45

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: 164.38  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 303 MALFVATWNMqGQKELPASLDEFLLPTEADYTQD---------LYVIGVQEGCSDRREW----ETRLQETLGPQYVLLSS 369
Cdd:cd09101    1 ISIFIGTWNM-GSVPPPKSLASWLTSRGLGKTLDettvtiphdIYVFGTQENSVGDREWvdflRASLKELTDIDYQPIAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 370 AAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQA 449
Cdd:cd09101   80 QCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTHRRNQNYLDILRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 450 LALprnvpdtNPYRSSAGDVTTRFDEVFWFGDFNFRLSggrVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEE 529
Cdd:cd09101  160 LSL-------GDKQLNAFDISLRFTHLFWFGDLNYRLD---MDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFRE 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449020140 530 AEIHFLPSYKFDIG-KDTY----DSTSKQRT--PSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09101  230 EEISFPPTYRYERGsRDTYmwqkQKTTGMRTnvPSWCDRILWKSYPETHIVCNSYGCTDDIVTSDHSPVFGTFEV 304
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 303-597 1.41e-44

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: 161.31  E-value: 1.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 303 MALFVATWNMqGQKELPASLDEFLLPT--------EADYT-QDLYVIGVQEGCSDRREW----ETRLQETLGPQYVLLSS 369
Cdd:cd09100    1 ITIFIGTWNM-GNAPPPKKITSWFQCKgqgktrddTADYIpHDIYVIGTQEDPLGEKEWldtlKHSLREITSISFKVIAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 370 AAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQA 449
Cdd:cd09100   80 QTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQNYFNILRF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 450 LALPRNvpDTNPYrssagDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEE 529
Cdd:cd09100  160 LVLGDK--KLSPF-----NITHRFTHLFWLGDLNYRVELPNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQFEE 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449020140 530 AEIHFLPSYKFDIG-KDTYDSTSKQRT------PSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRV 597
Cdd:cd09100  233 EEITFAPTYRFERGtRERYAYTKQKATgmkynlPSWCDRVLWKSYPLVHVVCQSYGCTDDITTSDHSPVFATFEV 307
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 307-597 4.76e-42

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: 155.20  E-value: 4.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 307 VATWNMQGQKELPA------SLDEFLL--PTEADYTQ---------DLYVIGVQE------------GCSDRREWETRLQ 357
Cdd:cd09098    5 VGTWNVNGGKQFRSiafknqTLTDWLLdaPKKAGIPEfqdvrskpvDIFAIGFEEmvelnagnivsaSTTNQKLWAAELQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 358 ETLG--PQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGK 435
Cdd:cd09098   85 KTISrdQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 436 VAERLLDYNRTIQALALPrnvpdtnpyrssAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDpevDVLALLQHDQLT 515
Cdd:cd09098  165 VKERNEDFIEIARKLSFP------------MGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQ---NWDSLIAGDQLI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 516 REMKKGSIFKGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRH----------------KGDICPMKYSS 579
Cdd:cd09098  230 NQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKwpfdrsaedldllnasFPDNSKEQYTW 309

                        330       340
                 ....*....|....*....|....*..
gi 449020140 580 CPG---------IKTSDHRPVYGLFRV 597
Cdd:cd09098  310 SPGtllhygraeLKTSDHRPVVALIDI 336
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 362-599 6.13e-29

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 122.32  E-value: 6.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 362 PQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSG--DGKVAER 439
Cdd:PLN03191 362 QKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGhkDGAEQRR 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 440 LLDY----NRTIQALALPRNVPDTNPYRssagdvttrfDEVFWFGDFNFRL--SGGRVAVEAFLKQDPEvdvlaLLQHDQ 513
Cdd:PLN03191 442 NADVyeiiRRTRFSSVLDTDQPQTIPSH----------DQIFWFGDLNYRLnmLDTEVRKLVAQKRWDE-----LINSDQ 506

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 514 LTREMKKGSIFKGFEEAEIHFLPSYKFDIGKDTY-----DSTSKQRTPSYTDRVLYKSRHKGDICpMKYSScpgIKTSDH 588
Cdd:PLN03191 507 LIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQLC-YKRSE---IRLSDH 582

                        250
                 ....*....|.
gi 449020140 589 RPVYGLFRVKV 599
Cdd:PLN03191 583 RPVSSMFLVEV 593
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 307-592 3.23e-08

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 54.79  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 307 VATWNMQGqkeLPASLDEFLLPtEADYTQDLYVIGVQEgCSDRREWETRLQETLGPQYVLLSSAAHGVLYMS---LFIRR 383
Cdd:cd08372    1 VASYNVNG---LNAATRASGIA-RWVRELDPDIVCLQE-VKDSQYSAVALNQLLPEGYHQYQSGPSRKEGYEgvaILSKT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 384 DLIwFCSEVeYSTVTTRIVSQikTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNR---TIQALALPRNVPdtn 460
Cdd:cd08372   76 PKF-KIVEK-HQYKFGEGDSG--ERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEvleFLKRLRQPNSAP--- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 461 pyrssagdvttrfdeVFWFGDFNFRLSggrvaveaflkqdpevdvlalLQHDQLTREMKKGSIFKGFEEAEIHFLPSYKF 540
Cdd:cd08372  149 ---------------VVICGDFNVRPS---------------------EVDSENPSSMLRLFVALNLVDSFETLPHAYTF 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 449020140 541 DigkdtydsTSKQRTPSYTDRVLYKSRHKGDICPMK--YSSCPGIKTSDHRPVY 592
Cdd:cd08372  193 D--------TYMHNVKSRLDYIFVSKSLLPSVKSSKilSDAARARIPSDHYPIE 238
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 307-592 1.15e-05

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 47.39  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 307 VATWNMQ-----GQKELPASLDEFLLPTEADytqdlyVIGVQEGCSDRREWET--RLQETL---GPQY-VLLSSAAHGVL 375
Cdd:cd10283    3 IASWNILnfgnsKGKEKNPAIAEIISAFDLD------LIALQEVMDNGGGLDAlaKLVNELnkpGGTWkYIVSDKTGGSS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 376 YMSlfIRRDLIWFCSEVEYSTvttRIVSQIKTKGA------LGVSFTF--FGTSFLFITSHFTSGDGKVAERLLDYNRTI 447
Cdd:cd10283   77 GDK--ERYAFLYKSSKVRKVG---KAVLEKDSNTDgfarppYAAKFKSggTGFDFTLVNVHLKSGGSSKSGQGAKRVAEA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 448 QALAlprnvpdtNPYRSSAGDVTTrfDEVFWFGDFNfrLSGGRVAVEAFLKqdpevdvlallqhdqltremkkgsifKGF 527
Cdd:cd10283  152 QALA--------EYLKELADEDPD--DDVILLGDFN--IPADEDAFKALTK--------------------------AGF 193

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449020140 528 EEAEIHF-LPSYKFDIGKDTYD---STSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKT-SDHRPVY 592
Cdd:cd10283  194 KSLLPDStNLSTSFKGYANSYDnifVSGNLKEKFSNSGVFDFNILVDEAGEEDLDYSKWRKQiSDHDPVW 263
 
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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