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Conserved domains on  [gi|222642150|gb|EEE70282|]
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hypothetical protein OsJ_30444 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 562-1082 1.83e-174

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.


The actual alignment was detected with superfamily member PLN03191:

Pssm-ID: 469791 [Multi-domain]  Cd Length: 621  Bit Score: 524.86  E-value: 1.83e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  562 MGSQRGKQSEkSFWPLIVMKKWLNIKPKLNDFSEDEFDTDGGDEDFSDCAEDASDNFFEIHENNHTINRS------SGDK 635
Cdd:PLN03191    1 MRTRRGKRPE-AFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSvfgnqiSDGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  636 IMPL----RRLQRRKSESLRVNYISNKDMRfglyefifnpqcipchasgdfiivvttrVMIGTWNVAGRAPSEDLDLDQW 711
Cdd:PLN03191   80 VSVSkgysSKHRRGKSETLRAQYINTKDIR----------------------------VTIGTWNVAGRLPSEDLEIEDW 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  712 ICSQEPADMYILGFQEVVPLSVGNVLGAEDSRTVPKWEGIIRRALNKSQQPKANCKSYSAPLSP-LRVPIPSddghDDTK 790
Cdd:PLN03191  132 LSTEEPADIYIIGFQEVVPLNAGNVLGAEDSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPvLRTSIVA----DELA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  791 REYDKMTENLSPQQQCrdkqTSISKCSCDWLDGTSSLDWPECPLDIPAKISVSNRGLRRVMS----MGlFNtdYLENAQG 866
Cdd:PLN03191  208 EEVDSLPLEMMNNEFI----DAATGCPSLEPERNKNIGWPEHSLDATPQVVSSNSKLRRVFSssarLG-FK--WPENPSL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  867 FDLHGVALQ-DGIRRSYRSSGNLGMSWSEQQEKVD------VLSSVDYMSDWTS---DDTTSVVGPDERATFAKGESLKP 936
Cdd:PLN03191  281 FSPQRFALNaRGLKRSHRSFGNLGLSWNEIKQRSEvpevpeVIDSLSDVSDRSSeaeDDTFKEVPSYQLPEDLIKDCRKV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  937 PGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK-------------------------------- 984
Cdd:PLN03191  361 KQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKgsvsismslfqsrlcfvcshltsghkdgaeqr 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  985 -------VI----------------LPSVDcrslhQIFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGN 1041
Cdd:PLN03191  441 rnadvyeIIrrtrfssvldtdqpqtIPSHD-----QIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGH 515

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 222642150 1042 TFAGWKEGLINFPPTYKYETNSSKYVGEKPDEVGNKRSPAW 1082
Cdd:PLN03191  516 VFDGWKEGPIKFPPTYKYEINSDRYVGENPKEGEKKRSPAW 556
PLN03077 super family cl33629
Protein ECB2; Provisional
 69-542 2.40e-96

Protein ECB2; Provisional


The actual alignment was detected with superfamily member PLN03077:

Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 325.65  E-value: 2.40e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150   69 PHLAISLYRSMLSHSRShPNNYTYPPLLAACARLADSDSssaaaaaaaGVALHASLFRRGLESPdRFIRASLLSLYAAAG 148
Cdd:PLN03077  370 PDKALETYALMEQDNVS-PDEITIASVLSACACLGDLDV---------GVKLHELAERKGLISY-VVVANALIEMYSKCK 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  149 DLPAARQVFDLSPpnHRDLPLWNSLLHAYLSRAHYVQVLRLFRTMRTA---DHVTLLALLSACAHLGALHTARWAHAYlA 225
Cdd:PLN03077  439 CIDKALEVFHNIP--EKDVISWTSIIAGLRLNNRCFEALIFFRQMLLTlkpNSVTLIAALSACARIGALMCGKEIHAH-V 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  226 TTCSFPITTNLATALLNMYMRCGDVQTACSLFHStptRHKDVHTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDSVTL 305
Cdd:PLN03077  516 LRTGIGFDGFLPNALLDLYVRCGRMNYAWNQFNS---HEKDVVSWNILLTGYVAHGKGSMAVELFNRMVESGVNPDEVTF 592

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  306 TAVLSACTHAGMVDEGKRILRRMPLDYHLQPTIEHYGCTVDLLGRAGLLEEALALIRAVPFKADVALWGALLVACRCHRN 385
Cdd:PLN03077  593 ISLLCACSRSGMVTQGLEYFHSMEEKYSITPNLKHYACVVDLLGRAGKLTEAYNFINKMPITPDPAVWGALLNACRIHRH 672

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  386 FEMGQMVAMEILRLDPQHAGAWVFLSNVYAAAGKWDLVQEVRSSMKQHRIHKPPGSSVVELDGVVYEFLSGDHSHPQSDQ 465
Cdd:PLN03077  673 VELGELAAQHIFELDPNSVGYYILLCNLYADAGKWDEVARVRKTMRENGLTVDPGCSWVEVKGKVHAFLTDDESHPQIKE 752

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222642150  466 IYAMLDEIGKTLSLKGHKpATKLVTFDIDEEDKEVCISQHSEKLAVAFGLINTRRGAVIRIVKNLRICEDCHSVMKL 542
Cdd:PLN03077  753 INTVLEGFYEKMKASGLA-GSESSSMDEIEVSKDDIFCGHSERLAIAFGLINTVPGMPIWVTKNLYMCENCHNTVKF 828
 
Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 562-1082 1.83e-174

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 524.86  E-value: 1.83e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  562 MGSQRGKQSEkSFWPLIVMKKWLNIKPKLNDFSEDEFDTDGGDEDFSDCAEDASDNFFEIHENNHTINRS------SGDK 635
Cdd:PLN03191    1 MRTRRGKRPE-AFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSvfgnqiSDGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  636 IMPL----RRLQRRKSESLRVNYISNKDMRfglyefifnpqcipchasgdfiivvttrVMIGTWNVAGRAPSEDLDLDQW 711
Cdd:PLN03191   80 VSVSkgysSKHRRGKSETLRAQYINTKDIR----------------------------VTIGTWNVAGRLPSEDLEIEDW 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  712 ICSQEPADMYILGFQEVVPLSVGNVLGAEDSRTVPKWEGIIRRALNKSQQPKANCKSYSAPLSP-LRVPIPSddghDDTK 790
Cdd:PLN03191  132 LSTEEPADIYIIGFQEVVPLNAGNVLGAEDSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPvLRTSIVA----DELA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  791 REYDKMTENLSPQQQCrdkqTSISKCSCDWLDGTSSLDWPECPLDIPAKISVSNRGLRRVMS----MGlFNtdYLENAQG 866
Cdd:PLN03191  208 EEVDSLPLEMMNNEFI----DAATGCPSLEPERNKNIGWPEHSLDATPQVVSSNSKLRRVFSssarLG-FK--WPENPSL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  867 FDLHGVALQ-DGIRRSYRSSGNLGMSWSEQQEKVD------VLSSVDYMSDWTS---DDTTSVVGPDERATFAKGESLKP 936
Cdd:PLN03191  281 FSPQRFALNaRGLKRSHRSFGNLGLSWNEIKQRSEvpevpeVIDSLSDVSDRSSeaeDDTFKEVPSYQLPEDLIKDCRKV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  937 PGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK-------------------------------- 984
Cdd:PLN03191  361 KQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKgsvsismslfqsrlcfvcshltsghkdgaeqr 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  985 -------VI----------------LPSVDcrslhQIFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGN 1041
Cdd:PLN03191  441 rnadvyeIIrrtrfssvldtdqpqtIPSHD-----QIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGH 515

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 222642150 1042 TFAGWKEGLINFPPTYKYETNSSKYVGEKPDEVGNKRSPAW 1082
Cdd:PLN03191  516 VFDGWKEGPIKFPPTYKYEINSDRYVGENPKEGEKKRSPAW 556
PLN03077 PLN03077
Protein ECB2; Provisional
 69-542 2.40e-96

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 325.65  E-value: 2.40e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150   69 PHLAISLYRSMLSHSRShPNNYTYPPLLAACARLADSDSssaaaaaaaGVALHASLFRRGLESPdRFIRASLLSLYAAAG 148
Cdd:PLN03077  370 PDKALETYALMEQDNVS-PDEITIASVLSACACLGDLDV---------GVKLHELAERKGLISY-VVVANALIEMYSKCK 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  149 DLPAARQVFDLSPpnHRDLPLWNSLLHAYLSRAHYVQVLRLFRTMRTA---DHVTLLALLSACAHLGALHTARWAHAYlA 225
Cdd:PLN03077  439 CIDKALEVFHNIP--EKDVISWTSIIAGLRLNNRCFEALIFFRQMLLTlkpNSVTLIAALSACARIGALMCGKEIHAH-V 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  226 TTCSFPITTNLATALLNMYMRCGDVQTACSLFHStptRHKDVHTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDSVTL 305
Cdd:PLN03077  516 LRTGIGFDGFLPNALLDLYVRCGRMNYAWNQFNS---HEKDVVSWNILLTGYVAHGKGSMAVELFNRMVESGVNPDEVTF 592

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  306 TAVLSACTHAGMVDEGKRILRRMPLDYHLQPTIEHYGCTVDLLGRAGLLEEALALIRAVPFKADVALWGALLVACRCHRN 385
Cdd:PLN03077  593 ISLLCACSRSGMVTQGLEYFHSMEEKYSITPNLKHYACVVDLLGRAGKLTEAYNFINKMPITPDPAVWGALLNACRIHRH 672

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  386 FEMGQMVAMEILRLDPQHAGAWVFLSNVYAAAGKWDLVQEVRSSMKQHRIHKPPGSSVVELDGVVYEFLSGDHSHPQSDQ 465
Cdd:PLN03077  673 VELGELAAQHIFELDPNSVGYYILLCNLYADAGKWDEVARVRKTMRENGLTVDPGCSWVEVKGKVHAFLTDDESHPQIKE 752

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222642150  466 IYAMLDEIGKTLSLKGHKpATKLVTFDIDEEDKEVCISQHSEKLAVAFGLINTRRGAVIRIVKNLRICEDCHSVMKL 542
Cdd:PLN03077  753 INTVLEGFYEKMKASGLA-GSESSSMDEIEVSKDDIFCGHSERLAIAFGLINTVPGMPIWVTKNLYMCENCHNTVKF 828
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 932-1082 4.33e-35

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: 135.92  E-value: 4.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  932 ESLKPPGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVA--SVGVGLLGYMGNK------------------------- 984
Cdd:cd09074    67 EALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEgvTVGTGGGGKLGNKggvairfqindtsfcfvnshlaagq 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  985 --------------------VILPSVDCRSLHQ-IFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTF 1043
Cdd:cd09074   147 eeverrnqdyrdilsklkfyRGDPAIDSIFDHDvVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEKGKVF 226

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 222642150 1044 AGWKEGLINFPPTYKYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09074   227 DGFQELPITFPPTYKFDPGTDEY-----DTSDKKRIPAW 260
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 933-1082 2.25e-26

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 110.91  E-value: 2.25e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150    933 SLKPPGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK--------------VILPS--------- 989
Cdd:smart00128   74 SLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKgavavrfklsdtsfCFVNShlaagasnv 153

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150    990 ----------------VDCRSLHQ-----IFWFGDLNYRIDMPDAE-IRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWK 1047
Cdd:smart00128  154 eqrnqdyktilralsfPERALLSQfdhdvVFWFGDLNFRLDSPSYEeVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQ 233

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 222642150   1048 EGLINFPPTYKYETNSSK-YV-GEKpdevgnKRSPAW 1082
Cdd:smart00128  234 EGPITFPPTYKYDSVGTEtYDtSEK------KRVPAW 264
DYW_deaminase pfam14432
DYW family of nucleic acid deaminases; This is the DYW domain found in nucleic acid deaminases ...
 481-542 4.14e-22

DYW family of nucleic acid deaminases; This is the DYW domain found in nucleic acid deaminases prototyped by the plant PPR DYW proteins that are implicated in chloroplast and mitochondrial RNA transcript maturation by numerous C to U editing events. The name derives from the DYW motif present at the C-terminus of the classical plant PPR DYW deaminases. Members containing this domain are present in bacteria, plants, Naegleria, and fungi. Plants and Naegleria show lineage-specific expansions of this family. This domain contains a characteriztic zinc-binding motif (CXXC, HXE) which has been shown to bind zinc ions. This domain is often fused to PPR repeats. Ascomycete versions, which are independent lateral transfers, contain a large insert within the domain and are often fused to ankyrin repeats. Bacterial versions are predicted to function as toxins in polymorphic toxin systems.


Pssm-ID: 464172 [Multi-domain]  Cd Length: 93  Bit Score: 91.71  E-value: 4.14e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222642150   481 GHKPATKLVTFDIDEEDKEVCISQHSEKLAVAFGLINTRRGAVIRIVKNLRICEDCHSVMKL 542
Cdd:pfam14432    1 GYVPDLKFVLHDVDEEEKKQLLHGHSEKLALAYGLLTTPDGATIRITKNLRVCGDCHTAFKY 62
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
998-1082 1.27e-13

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 74.43  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  998 IFWFGDLNYRIDMPDAEIRDLVSMK--RWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTYKYETNSSKYvgekpDEVG 1075
Cdd:COG5411   209 IFWLGDLNYRVTSTNEEVRPEIASDdgRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEY-----DTSD 283


                  ....*..
gi 222642150 1076 NKRSPAW 1082
Cdd:COG5411   284 KGRIPSW 290
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 268-302 7.31e-04

pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR motif, or pentatricopeptide repeat. Its consensus sequence is 35 positions long and typically is found in four or more tandem copies. This family is strongly represented in plant proteins, particularly those sorted to chloroplasts or mitochondria. The pfam01535, domain of unknown function DUF17, consists of 6 copies of this repeat. This family has a similar consensus to the TPR domain (tetratricopeptide), pfam00515, a 33-residue repeat. It is predicted to form a pair of antiparallel helices similar to that of TPR.


Pssm-ID: 273253 [Multi-domain]  Cd Length: 35  Bit Score: 37.82  E-value: 7.31e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 222642150   268 HTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDS 302
Cdd:TIGR00756    1 VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 315-421 3.27e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 39.02  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  315 AGMVDEGKRILRRMpldYHLQPT-IEHYGCTVDLLGRAGLLEEALALIRAV----PfkADVALWGALLVACRCHRNFEMG 389
Cdd:COG4783    17 AGDYDEAEALLEKA---LELDPDnPEAFALLGEILLQLGDLDEAIVLLHEAleldP--DEPEARLNLGLALLKAGDYDEA 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 222642150  390 QMVAMEILRLDPQHAGAWVFLSNVYAAAGKWD 421
Cdd:COG4783    92 LALLEKALKLDPEHPEAYLRLARAYRALGRPD 123
 
Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 562-1082 1.83e-174

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 524.86  E-value: 1.83e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  562 MGSQRGKQSEkSFWPLIVMKKWLNIKPKLNDFSEDEFDTDGGDEDFSDCAEDASDNFFEIHENNHTINRS------SGDK 635
Cdd:PLN03191    1 MRTRRGKRPE-AFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSvfgnqiSDGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  636 IMPL----RRLQRRKSESLRVNYISNKDMRfglyefifnpqcipchasgdfiivvttrVMIGTWNVAGRAPSEDLDLDQW 711
Cdd:PLN03191   80 VSVSkgysSKHRRGKSETLRAQYINTKDIR----------------------------VTIGTWNVAGRLPSEDLEIEDW 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  712 ICSQEPADMYILGFQEVVPLSVGNVLGAEDSRTVPKWEGIIRRALNKSQQPKANCKSYSAPLSP-LRVPIPSddghDDTK 790
Cdd:PLN03191  132 LSTEEPADIYIIGFQEVVPLNAGNVLGAEDSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPvLRTSIVA----DELA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  791 REYDKMTENLSPQQQCrdkqTSISKCSCDWLDGTSSLDWPECPLDIPAKISVSNRGLRRVMS----MGlFNtdYLENAQG 866
Cdd:PLN03191  208 EEVDSLPLEMMNNEFI----DAATGCPSLEPERNKNIGWPEHSLDATPQVVSSNSKLRRVFSssarLG-FK--WPENPSL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  867 FDLHGVALQ-DGIRRSYRSSGNLGMSWSEQQEKVD------VLSSVDYMSDWTS---DDTTSVVGPDERATFAKGESLKP 936
Cdd:PLN03191  281 FSPQRFALNaRGLKRSHRSFGNLGLSWNEIKQRSEvpevpeVIDSLSDVSDRSSeaeDDTFKEVPSYQLPEDLIKDCRKV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  937 PGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK-------------------------------- 984
Cdd:PLN03191  361 KQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKgsvsismslfqsrlcfvcshltsghkdgaeqr 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  985 -------VI----------------LPSVDcrslhQIFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGN 1041
Cdd:PLN03191  441 rnadvyeIIrrtrfssvldtdqpqtIPSHD-----QIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGH 515

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 222642150 1042 TFAGWKEGLINFPPTYKYETNSSKYVGEKPDEVGNKRSPAW 1082
Cdd:PLN03191  516 VFDGWKEGPIKFPPTYKYEINSDRYVGENPKEGEKKRSPAW 556
PLN03077 PLN03077
Protein ECB2; Provisional
 69-542 2.40e-96

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 325.65  E-value: 2.40e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150   69 PHLAISLYRSMLSHSRShPNNYTYPPLLAACARLADSDSssaaaaaaaGVALHASLFRRGLESPdRFIRASLLSLYAAAG 148
Cdd:PLN03077  370 PDKALETYALMEQDNVS-PDEITIASVLSACACLGDLDV---------GVKLHELAERKGLISY-VVVANALIEMYSKCK 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  149 DLPAARQVFDLSPpnHRDLPLWNSLLHAYLSRAHYVQVLRLFRTMRTA---DHVTLLALLSACAHLGALHTARWAHAYlA 225
Cdd:PLN03077  439 CIDKALEVFHNIP--EKDVISWTSIIAGLRLNNRCFEALIFFRQMLLTlkpNSVTLIAALSACARIGALMCGKEIHAH-V 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  226 TTCSFPITTNLATALLNMYMRCGDVQTACSLFHStptRHKDVHTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDSVTL 305
Cdd:PLN03077  516 LRTGIGFDGFLPNALLDLYVRCGRMNYAWNQFNS---HEKDVVSWNILLTGYVAHGKGSMAVELFNRMVESGVNPDEVTF 592

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  306 TAVLSACTHAGMVDEGKRILRRMPLDYHLQPTIEHYGCTVDLLGRAGLLEEALALIRAVPFKADVALWGALLVACRCHRN 385
Cdd:PLN03077  593 ISLLCACSRSGMVTQGLEYFHSMEEKYSITPNLKHYACVVDLLGRAGKLTEAYNFINKMPITPDPAVWGALLNACRIHRH 672

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  386 FEMGQMVAMEILRLDPQHAGAWVFLSNVYAAAGKWDLVQEVRSSMKQHRIHKPPGSSVVELDGVVYEFLSGDHSHPQSDQ 465
Cdd:PLN03077  673 VELGELAAQHIFELDPNSVGYYILLCNLYADAGKWDEVARVRKTMRENGLTVDPGCSWVEVKGKVHAFLTDDESHPQIKE 752

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222642150  466 IYAMLDEIGKTLSLKGHKpATKLVTFDIDEEDKEVCISQHSEKLAVAFGLINTRRGAVIRIVKNLRICEDCHSVMKL 542
Cdd:PLN03077  753 INTVLEGFYEKMKASGLA-GSESSSMDEIEVSKDDIFCGHSERLAIAFGLINTVPGMPIWVTKNLYMCENCHNTVKF 828
PLN03081 PLN03081
pentatricopeptide (PPR) repeat-containing protein; Provisional
 54-542 2.68e-96

pentatricopeptide (PPR) repeat-containing protein; Provisional


Pssm-ID: 215563 [Multi-domain]  Cd Length: 697  Bit Score: 321.43  E-value: 2.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150   54 FSYNSAIRALARGPRPHLAISLYRSMLSHSrSHPNNYTYPPLLAACARLADSDSssaaaaaaaGVALHASLFRRGLESpD 133
Cdd:PLN03081  190 ASWGTIIGGLVDAGNYREAFALFREMWEDG-SDAEPRTFVVMLRASAGLGSARA---------GQQLHCCVLKTGVVG-D 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  134 RFIRASLLSLYAAAGDLPAARQVFDLSPpnHRDLPLWNSLLHAYLSRAHYVQVLRLFRTMRTA----DHVTLLALLSACA 209
Cdd:PLN03081  259 TFVSCALIDMYSKCGDIEDARCVFDGMP--EKTTVAWNSMLAGYALHGYSEEALCLYYEMRDSgvsiDQFTFSIMIRIFS 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  210 HLGALHTARWAHAYLATTcSFPITTNLATALLNMYMRCGDVQTACSLFHSTPtrHKDVHTWTVMIAGLALNGFSTDALHL 289
Cdd:PLN03081  337 RLALLEHAKQAHAGLIRT-GFPLDIVANTALVDLYSKWGRMEDARNVFDRMP--RKNLISWNALIAGYGNHGRGTKAVEM 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  290 FTHMKDHNIQPDSVTLTAVLSACTHAGMVDEGKRILRRMPLDYHLQPTIEHYGCTVDLLGRAGLLEEALALIRAVPFKAD 369
Cdd:PLN03081  414 FERMIAEGVAPNHVTFLAVLSACRYSGLSEQGWEIFQSMSENHRIKPRAMHYACMIELLGREGLLDEAYAMIRRAPFKPT 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  370 VALWGALLVACRCHRNFEMGQMVAMEILRLDPQHAGAWVFLSNVYAAAGKWDLVQEVRSSMKQHRIHKPPGSSVVELDGV 449
Cdd:PLN03081  494 VNMWAALLTACRIHKNLELGRLAAEKLYGMGPEKLNNYVVLLNLYNSSGRQAEAAKVVETLKRKGLSMHPACTWIEVKKQ 573

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  450 VYEFLSGDHSHPQSDQIYAMLDEIGKTLSLKGHKPATKLVTFDIDEEDKEVCISQHSEKLAVAFGLINTRRGAVIRIVKN 529
Cdd:PLN03081  574 DHSFFSGDRLHPQSREIYQKLDELMKEISEYGYVAEENELLPDVDEDEEKVSGRYHSEKLAIAFGLINTSEWTPLQITQS 653

                         490
                  ....*....|...
gi 222642150  530 LRICEDCHSVMKL 542
Cdd:PLN03081  654 HRICKDCHKVIKF 666
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 932-1082 4.33e-35

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: 135.92  E-value: 4.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  932 ESLKPPGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVA--SVGVGLLGYMGNK------------------------- 984
Cdd:cd09074    67 EALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEgvTVGTGGGGKLGNKggvairfqindtsfcfvnshlaagq 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  985 --------------------VILPSVDCRSLHQ-IFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTF 1043
Cdd:cd09074   147 eeverrnqdyrdilsklkfyRGDPAIDSIFDHDvVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEKGKVF 226

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 222642150 1044 AGWKEGLINFPPTYKYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09074   227 DGFQELPITFPPTYKFDPGTDEY-----DTSDKKRIPAW 260
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 932-1082 5.58e-32

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: 126.66  E-value: 5.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  932 ESLKPPGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK----VIL-------------------- 987
Cdd:cd09093    64 RGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKggvaVRFqfhnttfcfvnshlaahmee 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  988 ----------------------PSVDCRSLHQIFWFGDLNYRIDMPDAEI-RDLVSMKRWDDLLKSDQLTKELTNGNTFA 1044
Cdd:cd09093   144 verrnqdykdicarmkfedpdgPPLSISDHDVVFWLGDLNYRIQELPTEEvKELIEKNDLEELLKYDQLNIQRRAGKVFE 223

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 222642150 1045 GWKEGLINFPPTYKYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09093   224 GFTEGEINFIPTYKYDPGTDNW-----DSSEKCRAPAW 256
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 940-1082 1.92e-26

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: 111.71  E-value: 1.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  940 YVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK-------VILPSVDC-------------------- 992
Cdd:cd09089    94 YVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKgavairfLLHSTSLCfvcshfaagqsqvkernedf 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  993 ------------RSL--HQ-IFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTY 1057
Cdd:cd09089   174 aeiarklsfpmgRTLdsHDyVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINFAPTY 253

                         170       180
                  ....*....|....*....|....*
gi 222642150 1058 KYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09089   254 KYDLFSDDY-----DTSEKCRTPAW 273
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 933-1082 2.25e-26

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 110.91  E-value: 2.25e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150    933 SLKPPGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK--------------VILPS--------- 989
Cdd:smart00128   74 SLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKgavavrfklsdtsfCFVNShlaagasnv 153

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150    990 ----------------VDCRSLHQ-----IFWFGDLNYRIDMPDAE-IRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWK 1047
Cdd:smart00128  154 eqrnqdyktilralsfPERALLSQfdhdvVFWFGDLNFRLDSPSYEeVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQ 233

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 222642150   1048 EGLINFPPTYKYETNSSK-YV-GEKpdevgnKRSPAW 1082
Cdd:smart00128  234 EGPITFPPTYKYDSVGTEtYDtSEK------KRVPAW 264
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 689-1082 2.36e-26

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: 110.51  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  689 RVMIGTWNVAGRAPseDLDLDQWIC---SQEPADMYILGFQEVVPLSVGNVLGAeDSRTVPKWEGIIRRALNKSQQPKan 765
Cdd:cd09090     2 NIFVGTFNVNGKSY--KDDLSSWLFpeeNDELPDIVVIGLQEVVELTAGQILNS-DPSKSSFWEKKIKTTLNGRGGEK-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  766 cksysaplsplrvpipsddghddtkreYDKMtenlspqqqcRDKQtsiskcscdwLDGTSsldwpecpLDIPAKISVSNr 845
Cdd:cd09090    77 ---------------------------YVLL----------RSEQ----------LVGTA--------LLFFVKESQLP- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  846 glrrvmsmglfntdYLENAQGfdlhgvalqdgirrSYRSSGNLGMSwseqQEKVDVLSSVDYmsdwtSDDTTSVVGpder 925
Cdd:cd09090   101 --------------KVKNVEG--------------STKKTGLGGMS----GNKGAVAIRFDY-----GDTSFCFVT---- 139

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  926 ATFAKGESlkppgNYVrvvskqmvgiyvsvwvsrklrQHVNNLEVASVGvglLGYMGNKVIlPSVDCrslhqIFWFGDLN 1005
Cdd:cd09090   140 SHLAAGLT-----NYE---------------------ERNNDYKTIARG---LRFSRGRTI-KDHDH-----VIWLGDFN 184

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222642150 1006 YRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTYKYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09090   185 YRISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITFPPTYKYDKGTDNY-----DTSEKQRIPAW 256
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 937-1082 2.89e-25

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: 107.46  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  937 PGNYVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK--VILpSVDC--RSL---------HQ------ 997
Cdd:cd09094    69 PKGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKgaVTV-RFSLygHMIcflnchlpaHMekweqr 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  998 --------------------------IFWFGDLNYRI-DMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWKEGL 1050
Cdd:cd09094   148 iddfetilstqvfnecntpsildhdyVFWFGDLNFRIeDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGP 227

                         170       180       190
                  ....*....|....*....|....*....|..
gi 222642150 1051 INFPPTYKYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09094   228 LNFAPTYKFDLGTDEY-----DTSGKKRKPAW 254
DYW_deaminase pfam14432
DYW family of nucleic acid deaminases; This is the DYW domain found in nucleic acid deaminases ...
 481-542 4.14e-22

DYW family of nucleic acid deaminases; This is the DYW domain found in nucleic acid deaminases prototyped by the plant PPR DYW proteins that are implicated in chloroplast and mitochondrial RNA transcript maturation by numerous C to U editing events. The name derives from the DYW motif present at the C-terminus of the classical plant PPR DYW deaminases. Members containing this domain are present in bacteria, plants, Naegleria, and fungi. Plants and Naegleria show lineage-specific expansions of this family. This domain contains a characteriztic zinc-binding motif (CXXC, HXE) which has been shown to bind zinc ions. This domain is often fused to PPR repeats. Ascomycete versions, which are independent lateral transfers, contain a large insert within the domain and are often fused to ankyrin repeats. Bacterial versions are predicted to function as toxins in polymorphic toxin systems.


Pssm-ID: 464172 [Multi-domain]  Cd Length: 93  Bit Score: 91.71  E-value: 4.14e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222642150   481 GHKPATKLVTFDIDEEDKEVCISQHSEKLAVAFGLINTRRGAVIRIVKNLRICEDCHSVMKL 542
Cdd:pfam14432    1 GYVPDLKFVLHDVDEEEKKQLLHGHSEKLALAYGLLTTPDGATIRITKNLRVCGDCHTAFKY 62
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 940-1082 4.29e-20

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: 92.80  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  940 YVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNKvilPSVDCRSLHQ---------------------- 997
Cdd:cd09098    93 YVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNK---GAVAIRMLFHttslcfvcshfaagqsqvkern 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  998 -----------------------IFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWKEGLINFP 1054
Cdd:cd09098   170 edfieiarklsfpmgrmlfshdyVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFA 249

                         170       180
                  ....*....|....*....|....*...
gi 222642150 1055 PTYKYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09098   250 PTYKYDLFSDDY-----DTSEKCRTPAW 272
PLN03077 PLN03077
Protein ECB2; Provisional
 139-324 1.07e-18

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 91.83  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  139 SLLSLYAAAGDLPAARQVFDLSPpnHRDLPLWNSLLHAYLSRAHYVQVLRLFRTMRTA----DHVTLLALLSACAHLGAL 214
Cdd:PLN03077  126 AMLSMFVRFGELVHAWYVFGKMP--ERDLFSWNVLVGGYAKAGYFDEALCLYHRMLWAgvrpDVYTFPCVLRTCGGIPDL 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  215 HTARWAHAYLATTcSFPITTNLATALLNMYMRCGDVQTACSLFHSTPTRhkDVHTWTVMIAGLALNGFSTDALHLFTHMK 294
Cdd:PLN03077  204 ARGREVHAHVVRF-GFELDVDVVNALITMYVKCGDVVSARLVFDRMPRR--DCISWNAMISGYFENGECLEGLELFFTMR 280

                         170       180       190
                  ....*....|....*....|....*....|
gi 222642150  295 DHNIQPDSVTLTAVLSACTHAGMVDEGKRI 324
Cdd:PLN03077  281 ELSVDPDLMTITSVISACELLGDERLGREM 310
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 998-1082 1.02e-16

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: 82.09  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  998 IFWFGDLNYRIDMPDAEIRDLVSMKRWDD---LLKSDQLTKELTNGNTFAGWKEGLINFPPTYKYETNSSKYvgekpDEV 1074
Cdd:cd09095   177 VFWFGDFNFRLSGPRHLVDALINQGQEVDvsaLLQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVY-----DTS 251


                  ....*...
gi 222642150 1075 GNKRSPAW 1082
Cdd:cd09095   252 SKQRVPSY 259
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 940-1082 3.43e-16

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: 81.22  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  940 YVRVVSKQMVGIYVSVWVSRKLRQHVNNLEVASVGVGLLGYMGNK---------------------------VILPSVDC 992
Cdd:cd09099    93 YILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKgavairfqfystsfcficshltagqnqVKERNEDY 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  993 RSLHQ---------------IFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTY 1057
Cdd:cd09099   173 KEITQklsfpmgrnvfshdyVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTY 252

                         170       180
                  ....*....|....*....|....*
gi 222642150 1058 KYETNSSKYvgekpDEVGNKRSPAW 1082
Cdd:cd09099   253 KYDVGSEAY-----DTSDKCRTPAW 272
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 997-1082 5.47e-16

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: 80.02  E-value: 5.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  997 QIFWFGDLNYRIDMPDAEIRDLVSMKRWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTYKYETNS-SKYVGEKPDEVG 1075
Cdd:cd09101   178 HLFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFREEEISFPPTYRYERGSrDTYMWQKQKTTG 257


                  ....*...
gi 222642150 1076 NKRS-PAW 1082
Cdd:cd09101   258 MRTNvPSW 265
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 959-1082 1.37e-14

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: 75.75  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  959 RKLRQHVNNLEVASVGVgllgyMGNKVILPSVDCRSLHQIFWFGDLNYRIDMPDAEIRDLVSMKR---WDDLLKSDQLTK 1035
Cdd:cd09091   145 KKLRRNQNYLNILRFLS-----LGDKKLSAFNITHRFTHLFWLGDLNYRLDLPIQEAENIIQKIEqqqFEPLLRHDQLNL 219

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 222642150 1036 ELTNGNTFAGWKEGLINFPPTYKYETNS-SKYVGEKPDEVGNKRS-PAW 1082
Cdd:cd09091   220 EREEHKVFLRFSEEEITFPPTYRYERGSrDTYAYTKQKATGVKYNlPSW 268
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
998-1082 1.27e-13

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 74.43  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  998 IFWFGDLNYRIDMPDAEIRDLVSMK--RWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTYKYETNSSKYvgekpDEVG 1075
Cdd:COG5411   209 IFWLGDLNYRVTSTNEEVRPEIASDdgRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEY-----DTSD 283


                  ....*..
gi 222642150 1076 NKRSPAW 1082
Cdd:COG5411   284 KGRIPSW 290
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 981-1082 6.39e-13

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: 70.78  E-value: 6.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  981 MGNKVILPSVDCRSLHQIFWFGDLNYRIDMPDAEIRDLVS---MKRWDDLLKSDQLTKELTNGNTFAGWKEGLINFPPTY 1057
Cdd:cd09100   162 LGDKKLSPFNITHRFTHLFWLGDLNYRVELPNTEAENIIQkikQQQYQELLPHDQLLIERKESKVFLQFEEEEITFAPTY 241

                          90       100
                  ....*....|....*....|....*..
gi 222642150 1058 KYETNS-SKYVGEKPDEVGNKRS-PAW 1082
Cdd:cd09100   242 RFERGTrERYAYTKQKATGMKYNlPSW 268
E_motif pfam20431
E motif; This entry represents the E motif found in plant pentatricopeptide repeat (PPR) ...
 383-445 1.04e-10

E motif; This entry represents the E motif found in plant pentatricopeptide repeat (PPR) proteins which contain a DYW deaminase domain. The DYW domain is required for RNA editing, a process that deaminates specific cytidines to uridines. This motif, together with the E+ motif, precedes the DYW domain and, although their role is not clear, they are essential in the RNA editing reaction. The E/E+ motifs may contain two degenerate PPR motifs that could be involved in RNA or protein binding.


Pssm-ID: 466580 [Multi-domain]  Cd Length: 63  Bit Score: 58.32  E-value: 1.04e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222642150   383 HRNFEMGQMVAMEILRLDPQHAGAWVFLSNVYAAAGKWDLVQEVRSSMKQHRIHKPPGSSVVE 445
Cdd:pfam20431    1 YSNVELAEKAANILLELEKTNDGNYTLLSNIYAYAGRWKDVERIRKLMKSSGIKKRPGCSWIE 63
PLN03077 PLN03077
Protein ECB2; Provisional
 171-319 7.87e-10

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 63.33  E-value: 7.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  171 NSLLHAYLSRAHYVQVLRLFRTMR----TADHVTLLALLSACAHLGALHTARWAHAY-LATTCSFPIttNLATALLNMYM 245
Cdd:PLN03077   55 NSQLRALCSHGQLEQALKLLESMQelrvPVDEDAYVALFRLCEWKRAVEEGSRVCSRaLSSHPSLGV--RLGNAMLSMFV 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222642150  246 RCGDVQTACSLFHSTPTRhkDVHTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDSVTLTAVLSACthAGMVD 319
Cdd:PLN03077  133 RFGELVHAWYVFGKMPER--DLFSWNVLVGGYAKAGYFDEALCLYHRMLWAGVRPDVYTFPCVLRTC--GGIPD 202
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 188-456 6.44e-08

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 57.19  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  188 RLFRTMRTADHVTLLALLSACAHL----GALHTARwahayLATTCSFPITTNLATALLNMYMRCGDVQTACSLFH--STP 261
Cdd:PLN03218  427 RFAKLIRNPTLSTFNMLMSVCASSqdidGALRVLR-----LVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHemVNA 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  262 TRHKDVHTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDSVTLTAVLSACTHAGMVDEGKRILRRMPLDYH-LQPTIEH 340
Cdd:PLN03218  502 GVEANVHTFGALIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKAETHpIDPDHIT 581

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  341 YGCTVDLLGRAGLLEEALA---LIRAVPFKADVALWGALLVACRCHRNFEMGQMVAMEILRLD--PQHagawVFLSNVYA 415
Cdd:PLN03218  582 VGALMKACANAGQVDRAKEvyqMIHEYNIKGTPEVYTIAVNSCSQKGDWDFALSIYDDMKKKGvkPDE----VFFSALVD 657

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 222642150  416 AAGKWDLVQEVRSSMKQHRIHK-PPGSsvveldgVVYEFLSG 456
Cdd:PLN03218  658 VAGHAGDLDKAFEILQDARKQGiKLGT-------VSYSSLMG 692
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 265-312 2.69e-07

PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is found in up to 18 copies in some proteins. The family appears to be greatly expanded in plants and fungi. The repeat has been called PPR.


Pssm-ID: 463778 [Multi-domain]  Cd Length: 50  Bit Score: 48.13  E-value: 2.69e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 222642150   265 KDVHTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDSVTLTAVLSAC 312
Cdd:pfam13041    1 PDVVTYNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGL 48
Eplus_motif pfam20430
E+ motif; This is the E+ motif found in some plant pentatricopeptide repeat (PPR) proteins ...
 450-473 3.76e-06

E+ motif; This is the E+ motif found in some plant pentatricopeptide repeat (PPR) proteins which contain a C-terminal DYW deaminase domain. The DYW domain is required for RNA editing, a process that deaminates specific cytidines to uridines. This motif, together with the E motif, precedes the DYW domain and, although their role is not clear, they are essential in th RNA editing reaction. The E/E+ motifs may contain two degenerate PPR motifs that could be involved in RNA or protein binding.


Pssm-ID: 466579 [Multi-domain]  Cd Length: 28  Bit Score: 44.19  E-value: 3.76e-06
                           10        20
                   ....*....|....*....|....
gi 222642150   450 VYEFLSGDHSHPQSDQIYAMLDEI 473
Cdd:pfam20430    1 THTFFAGDKSHPESKQIYEKLSDL 24
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 268-302 7.31e-04

pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR motif, or pentatricopeptide repeat. Its consensus sequence is 35 positions long and typically is found in four or more tandem copies. This family is strongly represented in plant proteins, particularly those sorted to chloroplasts or mitochondria. The pfam01535, domain of unknown function DUF17, consists of 6 copies of this repeat. This family has a similar consensus to the TPR domain (tetratricopeptide), pfam00515, a 33-residue repeat. It is predicted to form a pair of antiparallel helices similar to that of TPR.


Pssm-ID: 273253 [Multi-domain]  Cd Length: 35  Bit Score: 37.82  E-value: 7.31e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 222642150   268 HTWTVMIAGLALNGFSTDALHLFTHMKDHNIQPDS 302
Cdd:TIGR00756    1 VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 315-421 3.27e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 39.02  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  315 AGMVDEGKRILRRMpldYHLQPT-IEHYGCTVDLLGRAGLLEEALALIRAV----PfkADVALWGALLVACRCHRNFEMG 389
Cdd:COG4783    17 AGDYDEAEALLEKA---LELDPDnPEAFALLGEILLQLGDLDEAIVLLHEAleldP--DEPEARLNLGLALLKAGDYDEA 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 222642150  390 QMVAMEILRLDPQHAGAWVFLSNVYAAAGKWD 421
Cdd:COG4783    92 LALLEKALKLDPEHPEAYLRLARAYRALGRPD 123
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 238-278 5.13e-03

PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is found in up to 18 copies in some proteins. The family appears to be greatly expanded in plants and fungi. The repeat has been called PPR.


Pssm-ID: 463778 [Multi-domain]  Cd Length: 50  Bit Score: 36.19  E-value: 5.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 222642150   238 TALLNMYMRCGDVQTACSLFHS------TPtrhkDVHTWTVMIAGLA 278
Cdd:pfam13041    7 NTLINGYCKKGKVEEAFKLFNEmkkrgvKP----NVYTYTILINGLC 49
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 347-421 6.16e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.06  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222642150  347 LLGRA----GLLEEAL-ALIRAVPFK-ADVALWGALLVACRCHRNFEMGQMVAMEILRLDPQHAGAWVFLSNVYAAAGKW 420
Cdd:COG4235    22 LLGRAylrlGRYDEALaAYEKALRLDpDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDY 101


                  .
gi 222642150  421 D 421
Cdd:COG4235   102 A 102
PPR pfam01535
PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ...
 269-298 6.21e-03

PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up to 18 copies in some proteins. This family appears to be greatly expanded in plants. This repeat occurs in PET309 that may be involved in RNA stabilization. This domain occurs in crp1 that is involved in RNA processing. This repeat is associated with a predicted plant protein Swiss:O49549 that has a domain organization similar to the human BRCA1 protein. The repeat has been called PPR.


Pssm-ID: 366695 [Multi-domain]  Cd Length: 31  Bit Score: 35.13  E-value: 6.21e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 222642150   269 TWTVMIAGLALNGFSTDALHLFTHMKDHNI 298
Cdd:pfam01535    2 TYNSLISGYCKNGKLEEALELFKEMKEKGI 31
 
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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