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Conserved domains on  [gi|972781524|ref|NP_001305431|]
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phosphatidylinositol polyphosphate 5-phosphatase type IV isoform 2 [Homo sapiens]

Protein Classification

PHA03247 and INPP5c_INPP5E-like domain-containing protein( domain architecture ID 10173445)

PHA03247 and INPP5c_INPP5E-like domain-containing protein

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 ...
 295-592 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: 601.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 295 PDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMS 374
Cdd:cd09095    1 PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLHSASHGVLHLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 375 LFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKVAERLLDYTRTVQALVLPRNVPd 453
Cdd:cd09095   81 VFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSgDGKVKERVLDYNKIIQALNLPRNVP- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 454 TNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSY 533
Cdd:cd09095  160 TNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTY 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 972781524 534 KFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09095  240 KFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALFRV 298
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 2-179 3.83e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524    2 PSKAENLRPSEPAPQPPE-GRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATP----------SGEDPPARAAPI 70
Cdd:PHA03247 2562 AAPDRSVPPPRPAPRPSEpAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPdthapdppppSPSPAANEPDPH 2641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   71 APRPPARPRLERALSLDDKGWRRRRFRGSQEDLEA--------RNGTSPSRGSVQSEG-PGAPAHSCSPPCLSTSlQEIP 141
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprRRAARPTVGSLTSLAdPPPPPPTPEPAPHALV-SATP 2720

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 972781524  142 KSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVA 179
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
 
Name Accession Description Interval E-value
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 295-592 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: 601.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 295 PDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMS 374
Cdd:cd09095    1 PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLHSASHGVLHLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 375 LFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKVAERLLDYTRTVQALVLPRNVPd 453
Cdd:cd09095   81 VFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSgDGKVKERVLDYNKIIQALNLPRNVP- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 454 TNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSY 533
Cdd:cd09095  160 TNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTY 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 972781524 534 KFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09095  240 KFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALFRV 298
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 297-594 4.74e-60

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 202.97  E-value: 4.74e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   297 RNVALFVATWNMQGQKElPPSLDEFLLPAEADYAQ----DLYVIGVQE------------GCSDRREWETRLQETLGPH- 359
Cdd:smart00128   1 RDIKVLIGTWNVGGLES-PKVDVTSWLFQKIEVKQsekpDIYVIGLQEvvglapgviletIAGKERLWSDLLESSLNGDg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   360 -YVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCDG-KVAERLLD 437
Cdd:smart00128  80 qYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGAsNVEQRNQD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   438 YTRTVQALVLPRNvPDTNPYRSsaadvttrfDEVFWFGDFNFRLsggrTVVDALLCQGLVV--DVPALLQHDQLIREMRK 515
Cdd:smart00128 160 YKTILRALSFPER-ALLSQFDH---------DVVFWFGDLNFRL----DSPSYEEVRRKISkkEFDDLLEKDQLNRQREA 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   516 GSIFKGFQEPDIHFLPSYKFD-IGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKV 594
Cdd:smart00128 226 GKVFKGFQEGPITFPPTYKYDsVGTETYDTSEKKRVPAWCDRILYRSNGPELIQLSEYHSGMEITTSDHKPVFATFRLKV 305
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
292-594 5.53e-50

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 180.36  E-value: 5.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 292 RYFPDRNVALFVATWNMQGqKELPPSLDEFLLP-AEADYAQDLYVIGVQE------------GCSDR-REWETRLQETL- 356
Cdd:COG5411   23 KYVIEKDVSIFVSTFNPPG-KPPKASTKRWLFPeIEATELADLYVVGLQEvveltpgsilsaDPYDRlRIWESKVLDCLn 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 357 ----GPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKV 431
Cdd:COG5411  102 gaqsDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAgVNNI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 432 AERLLDYTRTVQALVLPRN--VPDTnpyrssaadvttrfDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPaLLQHDQL 509
Cdd:COG5411  182 EERIFDYRSIASNICFSRGlrIYDH--------------DTIFWLGDLNYRVTSTNEEVRPEIASDDGRLDK-LFEYDQL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 510 IREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSrhkgdIC--PVSYSSCPGIKTSDHRPVY 587
Cdd:COG5411  247 LWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS-----EQltPHSYSSIPHLMISDHRPVY 321


                 ....*..
gi 972781524 588 GLFRVKV 594
Cdd:COG5411  322 ATFRAKI 328
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 358-594 1.80e-28

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 120.78  E-value: 1.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 358 PHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC---DGKVAER 434
Cdd:PLN03191 362 QKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSghkDGAEQRR 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 435 LLDY----TRTVQALVLPRNVPDTNPYRssaadvttrfDEVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPALLQHDQLI 510
Cdd:PLN03191 442 NADVyeiiRRTRFSSVLDTDQPQTIPSH----------DQIFWFGDLNYRLNMLDTEVRKLVAQK---RWDELINSDQLI 508

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 511 REMRKGSIFKGFQEPDIHFLPSYKFDIGKDTY-----DSTSKQRTPSYTDRVLYRSrhKGdICPVSYSSCPgIKTSDHRP 585
Cdd:PLN03191 509 KELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLG--KG-IKQLCYKRSE-IRLSDHRP 584


                 ....*....
gi 972781524 586 VYGLFRVKV 594
Cdd:PLN03191 585 VSSMFLVEV 593
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-179 3.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524    2 PSKAENLRPSEPAPQPPE-GRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATP----------SGEDPPARAAPI 70
Cdd:PHA03247 2562 AAPDRSVPPPRPAPRPSEpAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPdthapdppppSPSPAANEPDPH 2641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   71 APRPPARPRLERALSLDDKGWRRRRFRGSQEDLEA--------RNGTSPSRGSVQSEG-PGAPAHSCSPPCLSTSlQEIP 141
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprRRAARPTVGSLTSLAdPPPPPPTPEPAPHALV-SATP 2720

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 972781524  142 KSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVA 179
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
 
Name Accession Description Interval E-value
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 295-592 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: 601.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 295 PDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMS 374
Cdd:cd09095    1 PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLHSASHGVLHLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 375 LFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKVAERLLDYTRTVQALVLPRNVPd 453
Cdd:cd09095   81 VFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSgDGKVKERVLDYNKIIQALNLPRNVP- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 454 TNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSY 533
Cdd:cd09095  160 TNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTY 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 972781524 534 KFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09095  240 KFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNSCPSIKTSDHRPVFALFRV 298
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 299-592 4.17e-121

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: 361.65  E-value: 4.17e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 299 VALFVATWNMQGQKELPPSLDEFLLPAEaDYAQDLYVIGVQEGC------------SDRREWETRLQETLGP--HYVLLS 364
Cdd:cd09074    1 VKIFVVTWNVGGGISPPENLENWLSPKG-TEAPDIYAVGVQEVDmsvqgfvgnddsAKAREWVDNIQEALNEkeNYVLLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 365 SAAHGVLYMSLFIRRDLIWFCS--EVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKVAERLLDYTRT 441
Cdd:cd09074   80 SAQLVGIFLFVFVKKEHLPQIKdlEVEGVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAgQEEVERRNQDYRDI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 442 VQALVLPRNVPdtnpyrssAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPALLQHDQLIREMRKGSIFKG 521
Cdd:cd09074  160 LSKLKFYRGDP--------AIDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQG---DLDDLLEKDQLKKQKEKGKVFDG 228

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972781524 522 FQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09074  229 FQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQPLSYTSVPLYKTSDHKPVRATFRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 299-591 4.37e-66

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: 218.75  E-value: 4.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 299 VALFVATWNMQG--QKElppSLDEFLLPAEADYAQDLYVIGVQE------------GCSDRREWETRLQETL----GPHY 360
Cdd:cd09090    1 INIFVGTFNVNGksYKD---DLSSWLFPEENDELPDIVVIGLQEvveltagqilnsDPSKSSFWEKKIKTTLngrgGEKY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 361 VLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCD-GKVAERLLDYT 439
Cdd:cd09090   78 VLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGlTNYEERNNDYK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 440 RTVQALVLPRN--VPDtnpyrssaadvttrFDEVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPALLQHDQLIREMRKGS 517
Cdd:cd09090  158 TIARGLRFSRGrtIKD--------------HDHVIWLGDFNYRISLTNEDVRRFILNG---KLDKLLEYDQLNQQMNAGE 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972781524 518 IFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRhkgDICPVSYSSCPgIKTSDHRPVYGLFR 591
Cdd:cd09090  221 VFPGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYRGE---NLRQLSYNSAP-LRFSDHRPVYATFE 290
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 297-594 4.74e-60

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 202.97  E-value: 4.74e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   297 RNVALFVATWNMQGQKElPPSLDEFLLPAEADYAQ----DLYVIGVQE------------GCSDRREWETRLQETLGPH- 359
Cdd:smart00128   1 RDIKVLIGTWNVGGLES-PKVDVTSWLFQKIEVKQsekpDIYVIGLQEvvglapgviletIAGKERLWSDLLESSLNGDg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   360 -YVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCDG-KVAERLLD 437
Cdd:smart00128  80 qYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGAsNVEQRNQD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   438 YTRTVQALVLPRNvPDTNPYRSsaadvttrfDEVFWFGDFNFRLsggrTVVDALLCQGLVV--DVPALLQHDQLIREMRK 515
Cdd:smart00128 160 YKTILRALSFPER-ALLSQFDH---------DVVFWFGDLNFRL----DSPSYEEVRRKISkkEFDDLLEKDQLNRQREA 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   516 GSIFKGFQEPDIHFLPSYKFD-IGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKV 594
Cdd:smart00128 226 GKVFKGFQEGPITFPPTYKYDsVGTETYDTSEKKRVPAWCDRILYRSNGPELIQLSEYHSGMEITTSDHKPVFATFRLKV 305
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 302-592 1.27e-54

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: 187.91  E-value: 1.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 302 FVATWNMQGQKElPPSLDEFLLPAEAdyAQDLYVIGVQE----------GCSDR-REWETRLQETLGPH--YVLLSSAAH 368
Cdd:cd09093    4 FVGTWNVNGQSP-DESLRPWLSCDEE--PPDIYAIGFQEldlsaeaflfNDSSReQEWVKAVERGLHPDakYKKVKLIRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 369 GVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCD-GKVAERLLDYTRTVQALVL 447
Cdd:cd09093   81 VGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHmEEVERRNQDYKDICARMKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 448 PRnvPDTNPYRSSAADVttrfdeVFWFGDFNFRLSGGRT-VVDALLCQGLVVDvpaLLQHDQLIREMRKGSIFKGFQEPD 526
Cdd:cd09093  161 ED--PDGPPLSISDHDV------VFWLGDLNYRIQELPTeEVKELIEKNDLEE---LLKYDQLNIQRRAGKVFEGFTEGE 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972781524 527 IHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSrhkGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09093  230 INFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWRG---TNIVQLSYRSHMELKTSDHKPVSALFDI 292
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 301-592 2.52e-50

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This subfamily contains the INPP5c domains of two human synaptojanins, synaptojanin 1 (Synj1) and synaptojanin 2 (Synj2), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs). They belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, Synjs contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25 (a mitochondrial outer membrane protein). Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197323 [Multi-domain]  Cd Length: 328  Bit Score: 177.58  E-value: 2.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 301 LFVATWNMQGQKELPP------SLDEFLLPA------------EADYAQDLYVIGVQE------------GCSDRREWET 350
Cdd:cd09089    3 VFVGTWNVNGGKHFRSiafkhqSMTDWLLDNpklagqcsndseEDEKPVDIFAIGFEEmvdlnasnivsaSTTNQKEWGE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 351 RLQETLGPH--YVLLSSAAH-GV-LYmsLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFT 426
Cdd:cd09089   83 ELQKTISRDhkYVLLTSEQLvGVcLF--VFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 427 C-DGKVAERLLDYTRTVQALVLP--RNVpDTNPYrssaadvttrfdeVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPAL 503
Cdd:cd09089  161 AgQSQVKERNEDFAEIARKLSFPmgRTL-DSHDY-------------VFWCGDFNYRIDLPNDEVKELVRNG---DWLKL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 504 LQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHK-------GDICPVSYSSCP 576
Cdd:cd09089  224 LEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWpsdkteeSLVETNDPTWNP 303

                        330       340
                 ....*....|....*....|....*
gi 972781524 577 G---------IKTSDHRPVYGLFRV 592
Cdd:cd09089  304 GtllyygraeLKTSDHRPVVAIIDI 328
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 301-592 3.43e-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: 176.41  E-value: 3.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 301 LFVATWNMqGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRRE----------WETRLQETLGPH-YVLLSSAAHG 369
Cdd:cd09094    3 VYVVTWNV-ATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQfvsdlifddpWSDLFMDILSPKgYVKVSSIRLQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 370 VLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKVAERLLDYTRTVQALVLP 448
Cdd:cd09094   82 GLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAhMEKWEQRIDDFETILSTQVFN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 449 -RNVPDTNPYrssaadvttrfDEVFWFGDFNFRLSG-GRTVVDALLCQGlvvDVPALLQHDQLIREMRKGSIFKGFQEPD 526
Cdd:cd09094  162 eCNTPSILDH-----------DYVFWFGDLNFRIEDvSIEFVRELVNSK---KYHLLLEKDQLNMAKRKEEAFQGFQEGP 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972781524 527 IHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKG-------DICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09094  228 LNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWKVNPDAsteekflSITQTSYKSHMEYGISDHKPVTAQFRL 300
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
292-594 5.53e-50

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 180.36  E-value: 5.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 292 RYFPDRNVALFVATWNMQGqKELPPSLDEFLLP-AEADYAQDLYVIGVQE------------GCSDR-REWETRLQETL- 356
Cdd:COG5411   23 KYVIEKDVSIFVSTFNPPG-KPPKASTKRWLFPeIEATELADLYVVGLQEvveltpgsilsaDPYDRlRIWESKVLDCLn 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 357 ----GPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKV 431
Cdd:COG5411  102 gaqsDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAgVNNI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 432 AERLLDYTRTVQALVLPRN--VPDTnpyrssaadvttrfDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPaLLQHDQL 509
Cdd:COG5411  182 EERIFDYRSIASNICFSRGlrIYDH--------------DTIFWLGDLNYRVTSTNEEVRPEIASDDGRLDK-LFEYDQL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 510 IREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSrhkgdIC--PVSYSSCPGIKTSDHRPVY 587
Cdd:COG5411  247 LWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS-----EQltPHSYSSIPHLMISDHRPVY 321


                 ....*..
gi 972781524 588 GLFRVKV 594
Cdd:COG5411  322 ATFRAKI 328
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 299-592 6.68e-42

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: 153.95  E-value: 6.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 299 VALFVATWNMqGQKELPPSLDEFLLPA--------EADY-AQDLYVIGVQEGCSDRREW----ETRLQETLGPHYVLLSS 365
Cdd:cd09091    1 ISIFIGTWNM-GSAPPPKNITSWFTSKgqgktrddVADYiPHDIYVIGTQEDPLGEKEWldllRHSLKELTSLDYKPIAM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 366 AAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCDG-KVAERLLDYTRTVQA 444
Cdd:cd09091   80 QTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSeKKLRRNQNYLNILRF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 445 LVLprnvpdtNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQE 524
Cdd:cd09091  160 LSL-------GDKKLSAFNITHRFTHLFWLGDLNYRLDLPIQEAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFLRFSE 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972781524 525 PDIHFLPSYKFDIG-KDTYDSTSKQRT------PSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09091  233 EEITFPPTYRYERGsRDTYAYTKQKATgvkynlPSWCDRILWKSYPETHIICQSYGCTDDIVTSDHSPVFGTFEV 307
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 303-592 6.32e-41

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: 152.10  E-value: 6.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 303 VATWNMQGQKELPPS-----------LDEFLLPAEADYAQD------LYVIGVQE------------GCSDRREWETRLQ 353
Cdd:cd09099    5 MGTWNVNGGKQFRSNilgtseltdwlLDSPKLSGTPDFQDDesnppdIFAVGFEEmvelsagnivnaSTTNRKMWGEQLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 354 ETLGP--HYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGK 430
Cdd:cd09099   85 KAISRshRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTAgQNQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 431 VAERLLDYTRTVQALVLP--RNVpdtnpyrssaadvtTRFDEVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPALLQHDQ 508
Cdd:cd09099  165 VKERNEDYKEITQKLSFPmgRNV--------------FSHDYVFWCGDFNYRIDLTYEEVFYFIKRQ---DWKKLLEFDQ 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 509 LIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVL-YRSRH-----KGDI----------CPVSY 572
Cdd:cd09099  228 LQLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLwWRKKWpfektAGEInlldsdldfdTKIRH 307

                        330       340
                 ....*....|....*....|....*....
gi 972781524 573 SSCPG---------IKTSDHRPVYGLFRV 592
Cdd:cd09099  308 TWTPGalmyygraeLQASDHRPVLAIVEV 336
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 299-592 1.02e-39

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: 147.82  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 299 VALFVATWNMqGQKELPPSLDEFLLPA--------EADY-AQDLYVIGVQEGCSDRREW----ETRLQETLGPHYVLLSS 365
Cdd:cd09100    1 ITIFIGTWNM-GNAPPPKKITSWFQCKgqgktrddTADYiPHDIYVIGTQEDPLGEKEWldtlKHSLREITSISFKVIAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 366 AAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCDG-KVAERLLDYTRTVQA 444
Cdd:cd09100   80 QTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSeKKLRRNQNYFNILRF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 445 LVLPRNvpDTNPYrssaaDVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQE 524
Cdd:cd09100  160 LVLGDK--KLSPF-----NITHRFTHLFWLGDLNYRVELPNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQFEE 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972781524 525 PDIHFLPSYKFDIG-KDTYDSTSKQRT------PSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09100  233 EEITFAPTYRFERGtRERYAYTKQKATgmkynlPSWCDRVLWKSYPLVHVVCQSYGCTDDITTSDHSPVFATFEV 307
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 299-592 3.16e-39

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: 146.27  E-value: 3.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 299 VALFVATWNMqGQKELPPSLDEFLLP---------AEADYAQDLYVIGVQEGCSDRREW----ETRLQETLGPHYVLLSS 365
Cdd:cd09101    1 ISIFIGTWNM-GSVPPPKSLASWLTSrglgktldeTTVTIPHDIYVFGTQENSVGDREWvdflRASLKELTDIDYQPIAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 366 AAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGKVAERLLDYTRTVQA 444
Cdd:cd09101   80 QCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSgNEKTHRRNQNYLDILRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 445 LVLprnvpdtNPYRSSAADVTTRFDEVFWFGDFNFRLSggrTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQE 524
Cdd:cd09101  160 LSL-------GDKQLNAFDISLRFTHLFWFGDLNYRLD---MDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFRE 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972781524 525 PDIHFLPSYKFDIG-KDTY----DSTSKQRT--PSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRV 592
Cdd:cd09101  230 EEISFPPTYRYERGsRDTYmwqkQKTTGMRTnvPSWCDRILWKSYPETHIVCNSYGCTDDIVTSDHSPVFGTFEV 304
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 303-592 1.21e-37

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: 142.87  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 303 VATWNMQGQKELPP------SLDEFLL--PAEADYAQ---------DLYVIGVQE------------GCSDRREWETRLQ 353
Cdd:cd09098    5 VGTWNVNGGKQFRSiafknqTLTDWLLdaPKKAGIPEfqdvrskpvDIFAIGFEEmvelnagnivsaSTTNQKLWAAELQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 354 ETLG--PHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC-DGK 430
Cdd:cd09098   85 KTISrdQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAgQSQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 431 VAERLLDYTRTVQALVLPrnvpdtnpyrssAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPALLQHDQLI 510
Cdd:cd09098  165 VKERNEDFIEIARKLSFP------------MGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQ---NWDSLIAGDQLI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 511 REMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRH----------------KGDICPVSYSS 574
Cdd:cd09098  230 NQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKwpfdrsaedldllnasFPDNSKEQYTW 309

                        330       340
                 ....*....|....*....|....*..
gi 972781524 575 CPG---------IKTSDHRPVYGLFRV 592
Cdd:cd09098  310 SPGtllhygraeLKTSDHRPVVALIDI 336
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 358-594 1.80e-28

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 120.78  E-value: 1.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 358 PHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTC---DGKVAER 434
Cdd:PLN03191 362 QKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSghkDGAEQRR 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 435 LLDY----TRTVQALVLPRNVPDTNPYRssaadvttrfDEVFWFGDFNFRLSGGRTVVDALLCQGlvvDVPALLQHDQLI 510
Cdd:PLN03191 442 NADVyeiiRRTRFSSVLDTDQPQTIPSH----------DQIFWFGDLNYRLNMLDTEVRKLVAQK---RWDELINSDQLI 508

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 511 REMRKGSIFKGFQEPDIHFLPSYKFDIGKDTY-----DSTSKQRTPSYTDRVLYRSrhKGdICPVSYSSCPgIKTSDHRP 585
Cdd:PLN03191 509 KELRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLG--KG-IKQLCYKRSE-IRLSDHRP 584


                 ....*....
gi 972781524 586 VYGLFRVKV 594
Cdd:PLN03191 585 VSSMFLVEV 593
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 303-587 5.22e-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: 54.41  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 303 VATWNMQGqkelppsLDEFLLP---AEADYAQDLYVIGVQE-GCSDRREWETRLQETLGPHYVLlsSAAHGVLYMS---L 375
Cdd:cd08372    1 VASYNVNG-------LNAATRAsgiARWVRELDPDIVCLQEvKDSQYSAVALNQLLPEGYHQYQ--SGPSRKEGYEgvaI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 376 FIRRDLIwFCSEVecsTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTCDGKVAERLLDYTRTVQALVLPRNVPDTN 455
Cdd:cd08372   72 LSKTPKF-KIVEK---HQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKRLRQPNSA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524 456 PyrssaadvttrfdeVFWFGDFNFRLSggrtvvdallcqglvvdvpalLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKF 535
Cdd:cd08372  148 P--------------VVICGDFNVRPS---------------------EVDSENPSSMLRLFVALNLVDSFETLPHAYTF 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 972781524 536 DigkdtydsTSKQRTPSYTDRVLYRSRHKGDICP--VSYSSCPGIKTSDHRPVY 587
Cdd:cd08372  193 D--------TYMHNVKSRLDYIFVSKSLLPSVKSskILSDAARARIPSDHYPIE 238
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-179 3.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524    2 PSKAENLRPSEPAPQPPE-GRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATP----------SGEDPPARAAPI 70
Cdd:PHA03247 2562 AAPDRSVPPPRPAPRPSEpAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPdthapdppppSPSPAANEPDPH 2641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781524   71 APRPPARPRLERALSLDDKGWRRRRFRGSQEDLEA--------RNGTSPSRGSVQSEG-PGAPAHSCSPPCLSTSlQEIP 141
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprRRAARPTVGSLTSLAdPPPPPPTPEPAPHALV-SATP 2720

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 972781524  142 KSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVA 179
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
 
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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