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Conserved domains on  [gi|71990653|ref|NP_001023265|]
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Synaptojanin [Caenorhabditis elegans]

Protein Classification

RNA-binding protein( domain architecture ID 13429204)

RNA-binding protein containing an RNA recognition motif (RRM)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 521-829 0e+00

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: 574.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVAFRNESsLSHWIFANSMTRLV----SVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRM 596
Cdd:cd09089    1 LRVFVGTWNVNGGKHFRSIAFKHQS-MTDWLLDNPKLAGQcsndSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  597 WCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHF 676
Cdd:cd09089   80 WGEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  677 AAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTF 756
Cdd:cd09089  160 AAGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  757 VGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKK----------------GKTQLLSYDRSELKTSDH 820
Cdd:cd09089  240 KGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPsdkteeslvetndptwNPGTLLYYGRAELKTSDH 319


                 ....*....
gi 71990653  821 RPVGAVFKV 829
Cdd:cd09089  320 RPVVAIIDI 328
COG5329 super family cl34984
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
50-484 2.19e-88

Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5329:

Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 296.22  E-value: 2.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   50 RRSYQKIvdaYGILGVLAITKDEaVLVAVTGVLSVGQLYGADILKITNVEFISLR-------TFGSVENVDSRIIdLQRL 122
Cdd:COG5329   54 LSSAHKI---YGVIGLIKLKGDI-YLIVITGASLVGVIPGHSIYKILDVDFISLNnnkwddeLEEDEANYDKLSE-LKKL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  123 LSSQMFYFSSlqSYDLTRSAQHRD------SHDCSDARFFWNRSL------HFSfQRYGID--TDNWLLKCMAGSVLVRV 188
Cdd:COG5329  129 LSNGTFYFSY--DFDITNSLQKNLsegleaSVDRADLIFMWNSFLleefinHRS-KLSSLEkqFDNFLTTVIRGFAETVD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  189 VYVGANTGRVALISRLSCERVGTRFNVRGANYLGNVANFVETEQLLLFDEKECSLLQIRGSIPLFWEQPGVNVGSHKVKL 268
Cdd:COG5329  206 IKVGGNTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGPKIKVT 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  269 RAFETSLPAYHRHLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKTQHKSSHFaPLVDFIDFDYHAQMKISKEAIVQ-LKK 347
Cdd:COG5329  286 RSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKK-PKIHYTEFDFHKETSQDGFDDVKkLLY 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  348 KMSPHMTKHGFFYSMGKE--IVKRQTGVIRTNCLDCLDRTNAVQTAIG-----LQMSHDQVAFLNLNagkvnveqrVEEI 420
Cdd:COG5329  365 LIEQDLLEFGYFAYDINEgkSISEQDGVFRTNCLDCLDRTNVIQSLISrvlleQFRSEGVISDGYSP---------FLQI 435

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990653  421 LRDLWQKNGDQCSTIYAGTGALDGK----------SKLKDASRSLARTIQNNLMDGAKQESFDLFLTGaaYDPR 484
Cdd:COG5329  436 HRELWADNGDAISRLYTGTGALKSSftrrgrrsfaGALNDFIKSFSRYYINNFTDGQRQDAIDLLLGK--FRPQ 507
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 844-972 4.47e-13

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


The actual alignment was detected with superfamily member pfam08952:

Pssm-ID: 473069  Cd Length: 146  Bit Score: 67.91  E-value: 4.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    844 EDVVESMGPPDGTIIVSIAGKPRFPPQMFPP--IHEKLKELG--AQVQLSKFDDGDLWIVLNSGEMALAALSMDGLKIGG 919
Cdd:pfam08952   17 KEVIRDQGPPDGTIVVSLCSGDLDEKNIFDEnlMDELIQELTsfGEVTLVRFVEDTMWVTFRDGHSALNALSKDGMKVCG 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 71990653    920 TdQINVKLKSPDWAYALKPHLSDFDLESFEVTAEEEALLGGTDgavFEFADED 972
Cdd:pfam08952   97 R-ALKIRLKSKDWIKGLEEEIILCTDNTIPVSPCANSTLLAED---FDFGSPD 145
 
Name Accession Description Interval E-value
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 521-829 0e+00

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: 574.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVAFRNESsLSHWIFANSMTRLV----SVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRM 596
Cdd:cd09089    1 LRVFVGTWNVNGGKHFRSIAFKHQS-MTDWLLDNPKLAGQcsndSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  597 WCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHF 676
Cdd:cd09089   80 WGEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  677 AAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTF 756
Cdd:cd09089  160 AAGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  757 VGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKK----------------GKTQLLSYDRSELKTSDH 820
Cdd:cd09089  240 KGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPsdkteeslvetndptwNPGTLLYYGRAELKTSDH 319


                 ....*....
gi 71990653  821 RPVGAVFKV 829
Cdd:cd09089  320 RPVVAIIDI 328
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 519-830 5.78e-100

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 318.14  E-value: 5.78e-100
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     519 QSIKIFVGTWNVNGgknihnvAFRNESSLSHWIFANSMtrlvsVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWC 598
Cdd:smart00128    1 RDIKVLIGTWNVGG-------LESPKVDVTSWLFQKIE-----VKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERLWS 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     599 ESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:smart00128   69 DLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAA 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     679 GQNEIRDRNEDFATTLKKIRFPLGREID--SHDVIFWLGDFNYRINL-SGDEVKNAVRNGDYAKLVENDQLTQQKALGQT 755
Cdd:smart00128  149 GASNVEQRNQDYKTILRALSFPERALLSqfDHDVVFWFGDLNFRLDSpSYEEVRRKISKKEFDDLLEKDQLNRQREAGKV 228

                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990653     756 FVGFNEGQLTFAPTYKYDTF-SDDYDTSEKCRAPAWTDRILWKDQrKKGKTQLLSYD-RSELKTSDHRPVGAVFKVE 830
Cdd:smart00128  229 FKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYRSN-GPELIQLSEYHsGMEITTSDHKPVFATFRLK 304
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
50-484 2.19e-88

Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 296.22  E-value: 2.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   50 RRSYQKIvdaYGILGVLAITKDEaVLVAVTGVLSVGQLYGADILKITNVEFISLR-------TFGSVENVDSRIIdLQRL 122
Cdd:COG5329   54 LSSAHKI---YGVIGLIKLKGDI-YLIVITGASLVGVIPGHSIYKILDVDFISLNnnkwddeLEEDEANYDKLSE-LKKL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  123 LSSQMFYFSSlqSYDLTRSAQHRD------SHDCSDARFFWNRSL------HFSfQRYGID--TDNWLLKCMAGSVLVRV 188
Cdd:COG5329  129 LSNGTFYFSY--DFDITNSLQKNLsegleaSVDRADLIFMWNSFLleefinHRS-KLSSLEkqFDNFLTTVIRGFAETVD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  189 VYVGANTGRVALISRLSCERVGTRFNVRGANYLGNVANFVETEQLLLFDEKECSLLQIRGSIPLFWEQPGVNVGSHKVKL 268
Cdd:COG5329  206 IKVGGNTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGPKIKVT 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  269 RAFETSLPAYHRHLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKTQHKSSHFaPLVDFIDFDYHAQMKISKEAIVQ-LKK 347
Cdd:COG5329  286 RSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKK-PKIHYTEFDFHKETSQDGFDDVKkLLY 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  348 KMSPHMTKHGFFYSMGKE--IVKRQTGVIRTNCLDCLDRTNAVQTAIG-----LQMSHDQVAFLNLNagkvnveqrVEEI 420
Cdd:COG5329  365 LIEQDLLEFGYFAYDINEgkSISEQDGVFRTNCLDCLDRTNVIQSLISrvlleQFRSEGVISDGYSP---------FLQI 435

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990653  421 LRDLWQKNGDQCSTIYAGTGALDGK----------SKLKDASRSLARTIQNNLMDGAKQESFDLFLTGaaYDPR 484
Cdd:COG5329  436 HRELWADNGDAISRLYTGTGALKSSftrrgrrsfaGALNDFIKSFSRYYINNFTDGQRQDAIDLLLGK--FRPQ 507
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
 60-336 3.41e-74

SacI homology domain; This Pfam family represents a protein domain which shows homology to the yeast protein SacI. The SacI homology domain is most notably found at the amino terminal of the inositol 5'-phosphatase synaptojanin.


Pssm-ID: 460545  Cd Length: 295  Bit Score: 247.49  E-value: 3.41e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     60 YGILGVLAITKDEAVLVaVTGVLSVGQLYGADILKITNVEFISLR-------TFGSVENVDSRIIDLQR-LLSSQMFYFS 131
Cdd:pfam02383    1 YGILGLIRLLSGYYLIV-ITKREQVGQIGGHPIYKITDVEFIPLNsslsdtqLAKKEHPDEERLLKLLKlFLSSGSFYFS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    132 SlqSYDLTRSAQHR------DSHDCSDARFFWNRSLHFSFQRYGIDTDNWLLKCMAGSVLVRVVYVGANTGRVALISRLS 205
Cdd:pfam02383   80 Y--DYDLTNSLQRNltrsrsPSFDSLDDRFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTLISRRS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    206 CERVGTRFNVRGANYLGNVANFVETEQLLLF-----DEKECSLLQIRGSIPLFWEQPGVNVGSHKVKLRAFETSLPAYHR 280
Cdd:pfam02383  158 RKRAGTRYLRRGIDDDGNVANFVETEQIVSLntsnsEGKIFSFVQIRGSIPLFWSQDPNLKYKPKIQITRPEATQPAFKK 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 71990653    281 HLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKT--QHKSSHFAPLVDFIDFDYHAQMK 336
Cdd:pfam02383  238 HFDDLIERYGPVHIVNLVEKKGRESKLSEAYEEavKYLNQFLPDKLRYTAFDFHHECK 295
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
495-846 7.10e-69

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 238.53  E-value: 7.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  495 PSLIQEYADAVsqLVERSPEIAEPQSIKIFVGTWNVNGgknihNVAfrnESSLSHWIFANSmtrlvsvEDEQLADIVAIG 574
Cdd:COG5411    6 YDPRHPYIVAV--LRQRRSKYVIEKDVSIFVSTFNPPG-----KPP---KASTKRWLFPEI-------EATELADLYVVG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  575 VEELVDLNASNMVKAST-TNQRMWCESIRKTLSE---KAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGG 650
Cdd:COG5411   69 LQEVVELTPGSILSADPyDRLRIWESKVLDCLNGaqsDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  651 ATGNKGSVAFRIVVFSTSICFICSHFAAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKN 730
Cdd:COG5411  149 SSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  731 AVRNGDYA--KLVENDQLTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWkdqrKKGKTQLL 808
Cdd:COG5411  229 EIASDDGRldKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILY----KSEQLTPH 304

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 71990653  809 SY-DRSELKTSDHRPVGAVFKVETFKVGGRKCVELIEDV 846
Cdd:COG5411  305 SYsSIPHLMISDHRPVYATFRAKIKVVDPSKKEGLIEKL 343
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 599-830 2.25e-52

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 195.13  E-value: 2.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   599 ESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:PLN03191  352 DLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTS 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   679 GQN---EIRdRNEDFATTLKKIRFP------LGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQ 749
Cdd:PLN03191  432 GHKdgaEQR-RNADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKE 510

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   750 KALGQTFVGFNEGQLTFAPTYKYDTFSDDY-----DTSEKCRAPAWTDRILWkdqRKKGKTQlLSYDRSELKTSDHRPVG 824
Cdd:PLN03191  511 LRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW---LGKGIKQ-LCYKRSEIRLSDHRPVS 586


                  ....*.
gi 71990653   825 AVFKVE 830
Cdd:PLN03191  587 SMFLVE 592
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
 844-972 4.47e-13

Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known function.


Pssm-ID: 286093  Cd Length: 146  Bit Score: 67.91  E-value: 4.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    844 EDVVESMGPPDGTIIVSIAGKPRFPPQMFPP--IHEKLKELG--AQVQLSKFDDGDLWIVLNSGEMALAALSMDGLKIGG 919
Cdd:pfam08952   17 KEVIRDQGPPDGTIVVSLCSGDLDEKNIFDEnlMDELIQELTsfGEVTLVRFVEDTMWVTFRDGHSALNALSKDGMKVCG 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 71990653    920 TdQINVKLKSPDWAYALKPHLSDFDLESFEVTAEEEALLGGTDgavFEFADED 972
Cdd:pfam08952   97 R-ALKIRLKSKDWIKGLEEEIILCTDNTIPVSPCANSTLLAED---FDFGSPD 145
 
Name Accession Description Interval E-value
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 521-829 0e+00

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: 574.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVAFRNESsLSHWIFANSMTRLV----SVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRM 596
Cdd:cd09089    1 LRVFVGTWNVNGGKHFRSIAFKHQS-MTDWLLDNPKLAGQcsndSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  597 WCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHF 676
Cdd:cd09089   80 WGEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  677 AAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTF 756
Cdd:cd09089  160 AAGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  757 VGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKK----------------GKTQLLSYDRSELKTSDH 820
Cdd:cd09089  240 KGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPsdkteeslvetndptwNPGTLLYYGRAELKTSDH 319


                 ....*....
gi 71990653  821 RPVGAVFKV 829
Cdd:cd09089  320 RPVVAIIDI 328
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 521-829 7.08e-131

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: 401.34  E-value: 7.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVAFRNESsLSHWIF-ANSMTRLVSVEDEQL--ADIVAIGVEELVDLNASNMVKASTTNQRMW 597
Cdd:cd09098    1 IRVCVGTWNVNGGKQFRSIAFKNQT-LTDWLLdAPKKAGIPEFQDVRSkpVDIFAIGFEEMVELNAGNIVSASTTNQKLW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  598 CESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFA 677
Cdd:cd09098   80 AAELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  678 AGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTFV 757
Cdd:cd09098  160 AGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  758 GFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWK---------------------DQRKKGKT----QLLSYDR 812
Cdd:cd09098  240 GFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedldllnasfpDNSKEQYTwspgTLLHYGR 319

                        330
                 ....*....|....*..
gi 71990653  813 SELKTSDHRPVGAVFKV 829
Cdd:cd09098  320 AELKTSDHRPVVALIDI 336
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 521-829 1.66e-112

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: 353.17  E-value: 1.66e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNihnvaFRNE----SSLSHWIF-ANSMTRLVSVEDEQL--ADIVAIGVEELVDLNASNMVKASTTN 593
Cdd:cd09099    1 TRVAMGTWNVNGGKQ-----FRSNilgtSELTDWLLdSPKLSGTPDFQDDESnpPDIFAVGFEEMVELSAGNIVNASTTN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  594 QRMWCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFIC 673
Cdd:cd09099   76 RKMWGEQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFIC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  674 SHFAAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALG 753
Cdd:cd09099  156 SHLTAGQNQVKERNEDYKEITQKLSFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  754 QTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWkdQRKK-------GKTQLLS----------------- 809
Cdd:cd09099  236 KIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLW--WRKKwpfektaGEINLLDsdldfdtkirhtwtpga 313

                        330       340
                 ....*....|....*....|...
gi 71990653  810 ---YDRSELKTSDHRPVGAVFKV 829
Cdd:cd09099  314 lmyYGRAELQASDHRPVLAIVEV 336
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 521-828 5.68e-106

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: 333.92  E-value: 5.68e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNihnvafrnESSLSHWIFANsmtrlvsvEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWCES 600
Cdd:cd09090    1 INIFVGTFNVNGKSY--------KDDLSSWLFPE--------ENDELPDIVVIGLQEVVELTAGQILNSDPSKSSFWEKK 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  601 IRKTLS--EKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:cd09090   65 IKTTLNgrGGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  679 GQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTFVG 758
Cdd:cd09090  145 GLTNYEERNNDYKTIARGLRFSRGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVFPG 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  759 FNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRkkgkTQLLSYDRSELKTSDHRPVGAVFK 828
Cdd:cd09090  225 FSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYRGEN----LRQLSYNSAPLRFSDHRPVYATFE 290
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 521-829 1.19e-102

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: 325.06  E-value: 1.19e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVafrnessLSHWIFansmtrlvsVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWCES 600
Cdd:cd09074    1 VKIFVVTWNVGGGISPPEN-------LENWLS---------PKGTEAPDIYAVGVQEVDMSVQGFVGNDDSAKAREWVDN 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  601 IRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVA--SVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:cd09074   65 IQEALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEgvTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  679 GQNEIRDRNEDFATTLKKIRFPLG----REIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQ 754
Cdd:cd09074  145 GQEEVERRNQDYRDILSKLKFYRGdpaiDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEKGK 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990653  755 TFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKKGKTQlLSYDRSEL-KTSDHRPVGAVFKV 829
Cdd:cd09074  225 VFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQP-LSYTSVPLyKTSDHKPVRATFRV 299
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 521-829 6.24e-102

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: 323.11  E-value: 6.24e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIhnvafrneSSLSHWIFAnsmtrlvsveDEQLADIVAIGVEELvDLNASNMVKASTTNQRMWCES 600
Cdd:cd09093    1 FRIFVGTWNVNGQSPD--------ESLRPWLSC----------DEEPPDIYAIGFQEL-DLSAEAFLFNDSSREQEWVKA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  601 IRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAAGQ 680
Cdd:cd09093   62 VERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHM 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  681 NEIRDRNEDFATTLKKIRFPLGRE----IDSHDVIFWLGDFNYRIN-LSGDEVKNAVRNGDYAKLVENDQLTQQKALGQT 755
Cdd:cd09093  142 EEVERRNQDYKDICARMKFEDPDGpplsISDHDVVFWLGDLNYRIQeLPTEEVKELIEKNDLEELLKYDQLNIQRRAGKV 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990653  756 FVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRkkgkTQLLSYDRS-ELKTSDHRPVGAVFKV 829
Cdd:cd09093  222 FEGFTEGEINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWRGTN----IVQLSYRSHmELKTSDHKPVSALFDI 292
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 519-830 5.78e-100

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 318.14  E-value: 5.78e-100
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     519 QSIKIFVGTWNVNGgknihnvAFRNESSLSHWIFANSMtrlvsVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWC 598
Cdd:smart00128    1 RDIKVLIGTWNVGG-------LESPKVDVTSWLFQKIE-----VKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERLWS 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     599 ESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:smart00128   69 DLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAA 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     679 GQNEIRDRNEDFATTLKKIRFPLGREID--SHDVIFWLGDFNYRINL-SGDEVKNAVRNGDYAKLVENDQLTQQKALGQT 755
Cdd:smart00128  149 GASNVEQRNQDYKTILRALSFPERALLSqfDHDVVFWFGDLNFRLDSpSYEEVRRKISKKEFDDLLEKDQLNRQREAGKV 228

                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990653     756 FVGFNEGQLTFAPTYKYDTF-SDDYDTSEKCRAPAWTDRILWKDQrKKGKTQLLSYD-RSELKTSDHRPVGAVFKVE 830
Cdd:smart00128  229 FKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYRSN-GPELIQLSEYHsGMEITTSDHKPVFATFRLK 304
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
50-484 2.19e-88

Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 296.22  E-value: 2.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   50 RRSYQKIvdaYGILGVLAITKDEaVLVAVTGVLSVGQLYGADILKITNVEFISLR-------TFGSVENVDSRIIdLQRL 122
Cdd:COG5329   54 LSSAHKI---YGVIGLIKLKGDI-YLIVITGASLVGVIPGHSIYKILDVDFISLNnnkwddeLEEDEANYDKLSE-LKKL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  123 LSSQMFYFSSlqSYDLTRSAQHRD------SHDCSDARFFWNRSL------HFSfQRYGID--TDNWLLKCMAGSVLVRV 188
Cdd:COG5329  129 LSNGTFYFSY--DFDITNSLQKNLsegleaSVDRADLIFMWNSFLleefinHRS-KLSSLEkqFDNFLTTVIRGFAETVD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  189 VYVGANTGRVALISRLSCERVGTRFNVRGANYLGNVANFVETEQLLLFDEKECSLLQIRGSIPLFWEQPGVNVGSHKVKL 268
Cdd:COG5329  206 IKVGGNTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGPKIKVT 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  269 RAFETSLPAYHRHLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKTQHKSSHFaPLVDFIDFDYHAQMKISKEAIVQ-LKK 347
Cdd:COG5329  286 RSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKK-PKIHYTEFDFHKETSQDGFDDVKkLLY 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  348 KMSPHMTKHGFFYSMGKE--IVKRQTGVIRTNCLDCLDRTNAVQTAIG-----LQMSHDQVAFLNLNagkvnveqrVEEI 420
Cdd:COG5329  365 LIEQDLLEFGYFAYDINEgkSISEQDGVFRTNCLDCLDRTNVIQSLISrvlleQFRSEGVISDGYSP---------FLQI 435

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990653  421 LRDLWQKNGDQCSTIYAGTGALDGK----------SKLKDASRSLARTIQNNLMDGAKQESFDLFLTGaaYDPR 484
Cdd:COG5329  436 HRELWADNGDAISRLYTGTGALKSSftrrgrrsfaGALNDFIKSFSRYYINNFTDGQRQDAIDLLLGK--FRPQ 507
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
 60-336 3.41e-74

SacI homology domain; This Pfam family represents a protein domain which shows homology to the yeast protein SacI. The SacI homology domain is most notably found at the amino terminal of the inositol 5'-phosphatase synaptojanin.


Pssm-ID: 460545  Cd Length: 295  Bit Score: 247.49  E-value: 3.41e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653     60 YGILGVLAITKDEAVLVaVTGVLSVGQLYGADILKITNVEFISLR-------TFGSVENVDSRIIDLQR-LLSSQMFYFS 131
Cdd:pfam02383    1 YGILGLIRLLSGYYLIV-ITKREQVGQIGGHPIYKITDVEFIPLNsslsdtqLAKKEHPDEERLLKLLKlFLSSGSFYFS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    132 SlqSYDLTRSAQHR------DSHDCSDARFFWNRSLHFSFQRYGIDTDNWLLKCMAGSVLVRVVYVGANTGRVALISRLS 205
Cdd:pfam02383   80 Y--DYDLTNSLQRNltrsrsPSFDSLDDRFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTLISRRS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    206 CERVGTRFNVRGANYLGNVANFVETEQLLLF-----DEKECSLLQIRGSIPLFWEQPGVNVGSHKVKLRAFETSLPAYHR 280
Cdd:pfam02383  158 RKRAGTRYLRRGIDDDGNVANFVETEQIVSLntsnsEGKIFSFVQIRGSIPLFWSQDPNLKYKPKIQITRPEATQPAFKK 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 71990653    281 HLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKT--QHKSSHFAPLVDFIDFDYHAQMK 336
Cdd:pfam02383  238 HFDDLIERYGPVHIVNLVEKKGRESKLSEAYEEavKYLNQFLPDKLRYTAFDFHHECK 295
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
495-846 7.10e-69

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 238.53  E-value: 7.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  495 PSLIQEYADAVsqLVERSPEIAEPQSIKIFVGTWNVNGgknihNVAfrnESSLSHWIFANSmtrlvsvEDEQLADIVAIG 574
Cdd:COG5411    6 YDPRHPYIVAV--LRQRRSKYVIEKDVSIFVSTFNPPG-----KPP---KASTKRWLFPEI-------EATELADLYVVG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  575 VEELVDLNASNMVKAST-TNQRMWCESIRKTLSE---KAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGG 650
Cdd:COG5411   69 LQEVVELTPGSILSADPyDRLRIWESKVLDCLNGaqsDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  651 ATGNKGSVAFRIVVFSTSICFICSHFAAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKN 730
Cdd:COG5411  149 SSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  731 AVRNGDYA--KLVENDQLTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWkdqrKKGKTQLL 808
Cdd:COG5411  229 EIASDDGRldKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILY----KSEQLTPH 304

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 71990653  809 SY-DRSELKTSDHRPVGAVFKVETFKVGGRKCVELIEDV 846
Cdd:COG5411  305 SYsSIPHLMISDHRPVYATFRAKIKVVDPSKKEGLIEKL 343
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 522-827 3.03e-68

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: 231.10  E-value: 3.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  522 KIFVGTWNVngGKNIHNVAFRnesSLSHWifansmtrlvsVEDEQLADIVAIGVEELvdlnASNMVKASTTN--QRMWCE 599
Cdd:cd09094    2 RVYVVTWNV--ATAPPPIDVR---SLLGL-----------QSPEVAPDIYIIGLQEV----NSKPVQFVSDLifDDPWSD 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  600 SIRKTLSEKApFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAAG 679
Cdd:cd09094   62 LFMDILSPKG-YVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAH 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  680 QNEIRDRNEDFATTLKKIRFPLGR--EIDSHDVIFWLGDFNYRI-NLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTF 756
Cdd:cd09094  141 MEKWEQRIDDFETILSTQVFNECNtpSILDHDYVFWFGDLNFRIeDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAF 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990653  757 VGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKKGKTQ------LLSY-DRSELKTSDHRPVGAVF 827
Cdd:cd09094  221 QGFQEGPLNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWKVNPDASTEEkflsitQTSYkSHMEYGISDHKPVTAQF 298
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 519-829 4.72e-57

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: 199.57  E-value: 4.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  519 QSIKIFVGTWNVNGGKNIhnvafrnESSLSHWIFansmtrlvSVEDEQLADIVAIGVEElvdlnasnmvkaSTTNQRMWC 598
Cdd:cd09095    3 RNVGIFVATWNMQGQKEL-------PENLDDFLL--------PTSADFAQDIYVIGVQE------------GCSDRREWE 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  599 ESIRKTLSEKapFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:cd09095   56 IRLQETLGPS--HVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTS 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  679 GQNEIRDRNEDFATTLKKIRFP-----------LGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNG---DYAKLVEND 744
Cdd:cd09095  134 GDGKVKERVLDYNKIIQALNLPrnvptnpykseSGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGqevDVSALLQHD 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  745 QLTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDqRKKGKTQLLSYDR-SELKTSDHRPV 823
Cdd:cd09095  214 QLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRS-RQKGDVCCLKYNScPSIKTSDHRPV 292


                 ....*.
gi 71990653  824 GAVFKV 829
Cdd:cd09095  293 FALFRV 298
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 599-830 2.25e-52

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 195.13  E-value: 2.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   599 ESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAA 678
Cdd:PLN03191  352 DLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTS 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   679 GQN---EIRdRNEDFATTLKKIRFP------LGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQ 749
Cdd:PLN03191  432 GHKdgaEQR-RNADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKE 510

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653   750 KALGQTFVGFNEGQLTFAPTYKYDTFSDDY-----DTSEKCRAPAWTDRILWkdqRKKGKTQlLSYDRSELKTSDHRPVG 824
Cdd:PLN03191  511 LRSGHVFDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW---LGKGIKQ-LCYKRSEIRLSDHRPVS 586


                  ....*.
gi 71990653   825 AVFKVE 830
Cdd:PLN03191  587 SMFLVE 592
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 521-829 6.07e-36

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: 138.97  E-value: 6.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVAfrnesslsHWIFANSM--TRLVSVeDEQLADIVAIGVEElvdlnasnmvkaSTTNQRMWC 598
Cdd:cd09100    1 ITIFIGTWNMGNAPPPKKIT--------SWFQCKGQgkTRDDTA-DYIPHDIYVIGTQE------------DPLGEKEWL 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  599 ESIRKTLSE--KAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHF 676
Cdd:cd09100   60 DTLKHSLREitSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHL 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  677 AAGQNEIRDRNEDFATTLkkiRF-PLG-REIDSHDV------IFWLGDFNYRINLSGDEVKNAV---RNGDYAKLVENDQ 745
Cdd:cd09100  140 TSGSEKKLRRNQNYFNIL---RFlVLGdKKLSPFNIthrfthLFWLGDLNYRVELPNTEAENIIqkiKQQQYQELLPHDQ 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  746 LTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRA-------PAWTDRILWKDQ-------RKKGKTqllsyd 811
Cdd:cd09100  217 LLIERKESKVFLQFEEEEITFAPTYRFERGTRERYAYTKQKAtgmkynlPSWCDRVLWKSYplvhvvcQSYGCT------ 290

                        330
                 ....*....|....*...
gi 71990653  812 rSELKTSDHRPVGAVFKV 829
Cdd:cd09100  291 -DDITTSDHSPVFATFEV 307
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 521-829 2.89e-35

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: 137.00  E-value: 2.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNGGKNIHNVafrnesslSHWIFANSMTR-LVSVEDEQLADIVAIGVEElvdlnasnmvkaSTTNQRMWCE 599
Cdd:cd09091    1 ISIFIGTWNMGSAPPPKNI--------TSWFTSKGQGKtRDDVADYIPHDIYVIGTQE------------DPLGEKEWLD 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  600 SIRKTLSE--KAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFA 677
Cdd:cd09091   61 LLRHSLKEltSLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  678 AGQNEIRDRNEDFATTLkkiRF-PLG-REIDSHDV------IFWLGDFNYRINLSGDEVKNAV---RNGDYAKLVENDQL 746
Cdd:cd09091  141 SGSEKKLRRNQNYLNIL---RFlSLGdKKLSAFNIthrfthLFWLGDLNYRLDLPIQEAENIIqkiEQQQFEPLLRHDQL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  747 TQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDY-------DTSEKCRAPAWTDRILWKDQrkkGKTQLL--SYD-RSELK 816
Cdd:cd09091  218 NLEREEHKVFLRFSEEEITFPPTYRYERGSRDTyaytkqkATGVKYNLPSWCDRILWKSY---PETHIIcqSYGcTDDIV 294

                        330
                 ....*....|...
gi 71990653  817 TSDHRPVGAVFKV 829
Cdd:cd09091  295 TSDHSPVFGTFEV 307
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 521-829 4.34e-35

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: 136.26  E-value: 4.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  521 IKIFVGTWNVNggknihnvAFRNESSLSHWIFANSMTRlvsVEDEQLA----DIVAIGVEElvdlnasnmvkaSTTNQRM 596
Cdd:cd09101    1 ISIFIGTWNMG--------SVPPPKSLASWLTSRGLGK---TLDETTVtiphDIYVFGTQE------------NSVGDRE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  597 WCESIRKTLSE--KAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICS 674
Cdd:cd09101   58 WVDFLRASLKEltDIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNC 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  675 HFAAGQNEIRDRNEDFATTLKKIrfPLG-REIDSHDV------IFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLT 747
Cdd:cd09101  138 HLTSGNEKTHRRNQNYLDILRSL--SLGdKQLNAFDIslrfthLFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLN 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  748 QQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRA-------PAWTDRILWKDQRkkgKTQLL--SYD-RSELKT 817
Cdd:cd09101  216 LEREKNKVFLRFREEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILWKSYP---ETHIVcnSYGcTDDIVT 292

                        330
                 ....*....|..
gi 71990653  818 SDHRPVGAVFKV 829
Cdd:cd09101  293 SDHSPVFGTFEV 304
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
 844-972 4.47e-13

Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known function.


Pssm-ID: 286093  Cd Length: 146  Bit Score: 67.91  E-value: 4.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653    844 EDVVESMGPPDGTIIVSIAGKPRFPPQMFPP--IHEKLKELG--AQVQLSKFDDGDLWIVLNSGEMALAALSMDGLKIGG 919
Cdd:pfam08952   17 KEVIRDQGPPDGTIVVSLCSGDLDEKNIFDEnlMDELIQELTsfGEVTLVRFVEDTMWVTFRDGHSALNALSKDGMKVCG 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 71990653    920 TdQINVKLKSPDWAYALKPHLSDFDLESFEVTAEEEALLGGTDgavFEFADED 972
Cdd:pfam08952   97 R-ALKIRLKSKDWIKGLEEEIILCTDNTIPVSPCANSTLLAED---FDFGSPD 145
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 611-825 3.57e-06

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: 49.40  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  611 FVLIGSEQLVGVCLFLFARPRVSPylkdfAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAAGQNEIRDRNEDF 690
Cdd:cd08372   57 QSGPSRKEGYEGVAILSKTPKFKI-----VEKHQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  691 ATTLKKIRFplgREIDSHDVIFWLGDFNYRInlsgdevknavRNGDYAKLVENDQLTQQKALGQTFVgfnegqlTFAPTY 770
Cdd:cd08372  132 KEVLEFLKR---LRQPNSAPVVICGDFNVRP-----------SEVDSENPSSMLRLFVALNLVDSFE-------TLPHAY 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990653  771 KYDTFSDDYdtsekcraPAWTDRILWkdqrkkGKTQLLSYDRSELKT--------SDHRPVGA 825
Cdd:cd08372  191 TFDTYMHNV--------KSRLDYIFV------SKSLLPSVKSSKILSdaararipSDHYPIEV 239
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 712-823 2.47e-04

Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3.


Pssm-ID: 197326  Cd Length: 383  Bit Score: 44.77  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  712 FWLGDFNYRINL--------------------SGDEVKNAVRNGDYAKLVEN----------DQLTQQKALGQTFVGFN- 760
Cdd:cd09092  219 FVFGDFNFRLDTksvvetlcakatmqtvrkadSNIVVKLEFREKDNDNKVVLqiekkkfdyfNQDVFRDNNGKALLKFDk 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990653  761 ----------EGQLTFAPTYKYdtfSDDYDTSE---KCRAPAWTDRILWKDQRKKGKTQLLS----YDR--SELKTSDHR 821
Cdd:cd09092  299 elevfkdvlyELDISFPPSYPY---SEDPEQGTqymNTRCPAWCDRILMSHSARELKSENEEksvtYDMigPNVCMGDHK 375


                 ..
gi 71990653  822 PV 823
Cdd:cd09092  376 PV 377
 
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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