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Conserved domains on  [gi|240254645|ref|NP_181918|]
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Endonuclease/exonuclease/phosphatase family protein [Arabidopsis thaliana]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 13235699)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 576-923 5.82e-106

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: 337.00  E-value: 5.82e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDALMSWLGS-VASDVGILVVGLQEVEMGAGFLAmsaakesvgGNEGSTIGQYWIDTIGKTLDE 654
Cdd:cd09074     1 VKIFVVTWNVGGGISPPENLENWLSPkGTEAPDIYAVGVQEVDMSVQGFV---------GNDDSAKAREWVDNIQEALNE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  655 KAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRA--IGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNR 732
Cdd:cd09074    72 KENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGGGgkLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVER 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  733 RNADFDHIYKTMSFTRssnahnapaagvstgshttksannanvnTEETKQDLAEADMVVFFGDFNYRLFGiSYDEARDFV 812
Cdd:cd09074   152 RNQDYRDILSKLKFYR----------------------------GDPAIDSIFDHDVVFWFGDLNYRIDS-TDDEVRKLI 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  813 SQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESECSl 892
Cdd:cd09074   203 SQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFPPTYKFD---PGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQPLS- 278

                         330       340       350
                  ....*....|....*....|....*....|.
gi 240254645  893 dcpvvasimlYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09074   279 ----------YTSVPLYKTSDHKPVRATFRV 299
WD40 super family cl43672
WD40 repeat [General function prediction only];
174-549 8.97e-05

WD40 repeat [General function prediction only];


The actual alignment was detected with superfamily member COG2319:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  174 AGQESGVRFWNFDDafepgcGLSGRVQRGDEDAApfqESASTSPttclmvdNGNRLVwSGHKDGKIRSWKmdyvLDDGdd 253
Cdd:COG2319    96 ASADGTVRLWDLAT------GLLLRTLTGHTGAV---RSVAFSP-------DGKTLA-SGSADGTVRLWD----LATG-- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  254 spfKEGLAWQAHKGPVNSVIMSSygD---LWSCSEGGVIKIWTWESMEKSLSLRleekhmaallvERSGIDLRAQVTVNG 330
Cdd:COG2319   153 ---KLLRTLTGHSGAVTSVAFSP--DgklLASGSDDGTVRLWDLATGKLLRTLT-----------GHTGAVRSVAFSPDG 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  331 TcnisssevkcLLAdnvrskvWAAQLQTFSLWDGRTKELLKVFNSEGQTENRVDM-PLGQdqpaaedemkaKIASTSKke 409
Cdd:COG2319   217 K----------LLA-------SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDGR-----------LLASGSA-- 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  410 kpHGFLQ-------RSRNAIMGAADAVRRVATRGGGAYedakrteamvLAgdgmiwTGCTNGLLIQWD-GNGNRLQDFRH 481
Cdd:COG2319   267 --DGTVRlwdlatgELLRTLTGHSGGVNSVAFSPDGKL----------LA------SGSDDGTVRLWDlATGKLLRTLTG 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254645  482 HQCAV--LCFCTFGERIYIGYVSGHIQIIDLE-GNLIAGWVAHNNAVIKMA-AADG-YIFSLATHGGIRGWPV 549
Cdd:COG2319   329 HTGAVrsVAFSPDGKTLASGSDDGTVRLWDLAtGELLRTLTGHTGAVTSVAfSPDGrTLASGSADGTVRLWDL 401
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1206-1287 4.64e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1206 SKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKND 1285
Cdd:NF033609  654 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 733


                  ..
gi 240254645 1286 GD 1287
Cdd:NF033609  734 SD 735
 
Name Accession Description Interval E-value
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 576-923 5.82e-106

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: 337.00  E-value: 5.82e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDALMSWLGS-VASDVGILVVGLQEVEMGAGFLAmsaakesvgGNEGSTIGQYWIDTIGKTLDE 654
Cdd:cd09074     1 VKIFVVTWNVGGGISPPENLENWLSPkGTEAPDIYAVGVQEVDMSVQGFV---------GNDDSAKAREWVDNIQEALNE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  655 KAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRA--IGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNR 732
Cdd:cd09074    72 KENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGGGgkLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVER 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  733 RNADFDHIYKTMSFTRssnahnapaagvstgshttksannanvnTEETKQDLAEADMVVFFGDFNYRLFGiSYDEARDFV 812
Cdd:cd09074   152 RNQDYRDILSKLKFYR----------------------------GDPAIDSIFDHDVVFWFGDLNYRIDS-TDDEVRKLI 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  813 SQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESECSl 892
Cdd:cd09074   203 SQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFPPTYKFD---PGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQPLS- 278

                         330       340       350
                  ....*....|....*....|....*....|.
gi 240254645  893 dcpvvasimlYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09074   279 ----------YTSVPLYKTSDHKPVRATFRV 299
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 576-925 9.40e-83

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 273.46  E-value: 9.40e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    576 VRILTGSWNVGQGKASHDALMSWLGSVASDVG-----ILVVGLQEVemgaGFLAMSAAKESVGGNEgstigQYWIDTIGK 650
Cdd:smart00128    3 IKVLIGTWNVGGLESPKVDVTSWLFQKIEVKQsekpdIYVIGLQEV----VGLAPGVILETIAGKE-----RLWSDLLES 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    651 TLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAV 730
Cdd:smart00128   74 SLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNV 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    731 NRRNADFDHIYKTMSFTRSSnahnapaagvstgshttksannanvnteetKQDLAEADMVVFFGDFNYRLFGISYDEARD 810
Cdd:smart00128  154 EQRNQDYKTILRALSFPERA------------------------------LLSQFDHDVVFWFGDLNFRLDSPSYEEVRR 203

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    811 FVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhRPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESEC 890
Cdd:smart00128  204 KISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFPPTYKYD--SVGTETYDTSEKKRVPAWCDRILYRSNGPELIQLS 281

                           330       340       350
                    ....*....|....*....|....*....|....*
gi 240254645    891 SldcpvvasimlYDACMDVTESDHKPVRCKFHVKI 925
Cdd:smart00128  282 E-----------YHSGMEITTSDHKPVFATFRLKV 305
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
548-941 1.47e-48

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 180.36  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  548 PVISPGPLDGIIRSELAEKERTYAQTDSVRILTGSWNVgQGKASHDALMSWL---GSVASDVGILVVGLQE-VEMGAG-F 622
Cdd:COG5411     2 PVPIYDPRHPYIVAVLRQRRSKYVIEKDVSIFVSTFNP-PGKPPKASTKRWLfpeIEATELADLYVVGLQEvVELTPGsI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  623 LAMSAAKESvggnegstigQYWIDTIGKTLDEKAVFE---RMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAI 699
Cdd:COG5411    81 LSADPYDRL----------RIWESKVLDCLNGAQSDEkysLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  700 GNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNRRNADFDHIYKTMSFTRSsnahnapaagvstgshttksannanvntee 779
Cdd:COG5411   151 SNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRG------------------------------ 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  780 tkQDLAEADMVVFFGDFNYRLFGiSYDEARDFVSQ--RSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrP 857
Cdd:COG5411   201 --LRIYDHDTIFWLGDLNYRVTS-TNEEVRPEIASddGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFD---Y 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  858 GLGGYDSGEKKRIPAWCDRVIFRDTRTSPESecsldcpvvasimlYDACMDVTESDHKPVRCKFHVKIEHVDRSVRRQEF 937
Cdd:COG5411   275 GTDEYDTSDKGRIPSWTDRILYKSEQLTPHS--------------YSSIPHLMISDHRPVYATFRAKIKVVDPSKKEGLI 340


                  ....
gi 240254645  938 GRII 941
Cdd:COG5411   341 EKLY 344
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 642-934 3.79e-40

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 158.92  E-value: 3.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  642 QYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINC 721
Cdd:PLN03191  348 QLPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCS 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  722 HLAAHLE--AVNRRNADfdhIYKTMSFTRSSNAHNApaagvstgshttksannanvnteETKQDLAEADMVVFFGDFNYR 799
Cdd:PLN03191  428 HLTSGHKdgAEQRRNAD---VYEIIRRTRFSSVLDT-----------------------DQPQTIPSHDQIFWFGDLNYR 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  800 LfGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPGLGGYD--SGEKKRIPAWCDRV 877
Cdd:PLN03191  482 L-NMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYVGENpkEGEKKRSPAWCDRI 560

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240254645  878 IFRDTRTSPESecsldcpvvasimlYDACmDVTESDHKPVRCKFHVKIEHVD-RSVRR 934
Cdd:PLN03191  561 LWLGKGIKQLC--------------YKRS-EIRLSDHRPVSSMFLVEVEVFDhRKLQR 603
WD40 COG2319
WD40 repeat [General function prediction only];
174-549 8.97e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  174 AGQESGVRFWNFDDafepgcGLSGRVQRGDEDAApfqESASTSPttclmvdNGNRLVwSGHKDGKIRSWKmdyvLDDGdd 253
Cdd:COG2319    96 ASADGTVRLWDLAT------GLLLRTLTGHTGAV---RSVAFSP-------DGKTLA-SGSADGTVRLWD----LATG-- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  254 spfKEGLAWQAHKGPVNSVIMSSygD---LWSCSEGGVIKIWTWESMEKSLSLRleekhmaallvERSGIDLRAQVTVNG 330
Cdd:COG2319   153 ---KLLRTLTGHSGAVTSVAFSP--DgklLASGSDDGTVRLWDLATGKLLRTLT-----------GHTGAVRSVAFSPDG 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  331 TcnisssevkcLLAdnvrskvWAAQLQTFSLWDGRTKELLKVFNSEGQTENRVDM-PLGQdqpaaedemkaKIASTSKke 409
Cdd:COG2319   217 K----------LLA-------SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDGR-----------LLASGSA-- 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  410 kpHGFLQ-------RSRNAIMGAADAVRRVATRGGGAYedakrteamvLAgdgmiwTGCTNGLLIQWD-GNGNRLQDFRH 481
Cdd:COG2319   267 --DGTVRlwdlatgELLRTLTGHSGGVNSVAFSPDGKL----------LA------SGSDDGTVRLWDlATGKLLRTLTG 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254645  482 HQCAV--LCFCTFGERIYIGYVSGHIQIIDLE-GNLIAGWVAHNNAVIKMA-AADG-YIFSLATHGGIRGWPV 549
Cdd:COG2319   329 HTGAVrsVAFSPDGKTLASGSDDGTVRLWDLAtGELLRTLTGHTGAVTSVAfSPDGrTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 215-547 2.80e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 44.25  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  215 TSPTTCLMVDNGNRLVWSGHKDGKIRSWKMDyvlddgDDSPFKEGlawQAHKGPVNSVIMSSYGD-LWSCSEGGVIKIWT 293
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLE------TGELLRTL---KGHTGPVRDVAASADGTyLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  294 WESMEKSlslrleekhmaallversgidlraqVTVNG-TCNISSsevkCLLADNVRSKVWAAQLQTFSLWDGRTKELLKV 372
Cdd:cd00200    80 LETGECV-------------------------RTLTGhTSYVSS----VAFSPDGRILSSSSRDKTIKVWDVETGKCLTT 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  373 FNsegqtenrvdmplgqdqpaaedemkakiastskkekphgflqrsrnaimGAADAVRRVATRGGGayedakrteaMVLA 452
Cdd:cd00200   131 LR-------------------------------------------------GHTDWVNSVAFSPDG----------TFVA 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  453 GdgmiwtGCTNGLLIQWDGNGNRL-QDFRHHQCAVLCFCTF--GERIYIGYVSGHIQIIDL-EGNLIAGWVAHNNAVIKM 528
Cdd:cd00200   152 S------SSQDGTIKLWDLRTGKCvATLTGHTGEVNSVAFSpdGEKLLSSSSDGTIKLWDLsTGKCLGTLRGHENGVNSV 225

                         330       340
                  ....*....|....*....|.
gi 240254645  529 AAA-DGYIFSLATHGG-IRGW 547
Cdd:cd00200   226 AFSpDGYLLASGSEDGtIRVW 246
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1206-1287 4.64e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1206 SKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKND 1285
Cdd:NF033609  654 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 733


                  ..
gi 240254645 1286 GD 1287
Cdd:NF033609  734 SD 735
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1190-1287 1.01e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.74  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1190 GDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSH 1269
Cdd:NF033609  668 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 747

                          90
                  ....*....|....*...
gi 240254645 1270 KKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  748 SDSDSDSDSDSDSDSDSD 765
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1170-1314 1.20e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.36  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1170 SKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKND 1249
Cdd:NF033609  726 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 805

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254645 1250 GDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKNDGDSSSSYKSQSGK-KNSNSSTVEESRNNHN 1314
Cdd:NF033609  806 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSESDSNSDSESGSNNN 871
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1185-1287 1.23e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.36  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1185 SKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDS 1264
Cdd:NF033609  669 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 748

                          90       100
                  ....*....|....*....|...
gi 240254645 1265 SSKSHKKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  749 DSDSDSDSDSDSDSDSDSDSDSD 771
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1178-1287 1.78e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1178 GDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSH 1257
Cdd:NF033609  668 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 747

                          90       100       110
                  ....*....|....*....|....*....|
gi 240254645 1258 KKSDGDSSSKSHKKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  748 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 777
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1194-1312 3.99e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1194 SKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSE 1273
Cdd:NF033609  720 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 799

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 240254645 1274 GDSSSKSHKKNDGDSSSSYKSQSGKKNSNSSTVEESRNN 1312
Cdd:NF033609  800 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 838
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1197-1287 4.57e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.43  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1197 SKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDS 1276
Cdd:NF033609  711 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 790

                          90
                  ....*....|.
gi 240254645 1277 SSKSHKKNDGD 1287
Cdd:NF033609  791 DSDSDSDSDSD 801
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1197-1287 5.65e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1197 SKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDS 1276
Cdd:NF033609  705 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 784

                          90
                  ....*....|.
gi 240254645 1277 SSKSHKKNDGD 1287
Cdd:NF033609  785 DSDSDSDSDSD 795
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1170-1312 6.09e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1170 SKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKND 1249
Cdd:NF033609  720 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 799

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254645 1250 GDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKNDGDSSSSYKSQSGKKNSNSSTVEESRNN 1312
Cdd:NF033609  800 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNS 862
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1190-1287 9.54e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1190 GDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSH 1269
Cdd:NF033609  714 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 793

                          90
                  ....*....|....*...
gi 240254645 1270 KKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  794 SDSDSDSDSDSDSDSDSD 811
 
Name Accession Description Interval E-value
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 576-923 5.82e-106

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: 337.00  E-value: 5.82e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDALMSWLGS-VASDVGILVVGLQEVEMGAGFLAmsaakesvgGNEGSTIGQYWIDTIGKTLDE 654
Cdd:cd09074     1 VKIFVVTWNVGGGISPPENLENWLSPkGTEAPDIYAVGVQEVDMSVQGFV---------GNDDSAKAREWVDNIQEALNE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  655 KAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRA--IGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNR 732
Cdd:cd09074    72 KENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGGGgkLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVER 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  733 RNADFDHIYKTMSFTRssnahnapaagvstgshttksannanvnTEETKQDLAEADMVVFFGDFNYRLFGiSYDEARDFV 812
Cdd:cd09074   152 RNQDYRDILSKLKFYR----------------------------GDPAIDSIFDHDVVFWFGDLNYRIDS-TDDEVRKLI 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  813 SQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESECSl 892
Cdd:cd09074   203 SQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFPPTYKFD---PGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQPLS- 278

                         330       340       350
                  ....*....|....*....|....*....|.
gi 240254645  893 dcpvvasimlYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09074   279 ----------YTSVPLYKTSDHKPVRATFRV 299
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 576-925 9.40e-83

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 273.46  E-value: 9.40e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    576 VRILTGSWNVGQGKASHDALMSWLGSVASDVG-----ILVVGLQEVemgaGFLAMSAAKESVGGNEgstigQYWIDTIGK 650
Cdd:smart00128    3 IKVLIGTWNVGGLESPKVDVTSWLFQKIEVKQsekpdIYVIGLQEV----VGLAPGVILETIAGKE-----RLWSDLLES 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    651 TLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAV 730
Cdd:smart00128   74 SLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNV 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    731 NRRNADFDHIYKTMSFTRSSnahnapaagvstgshttksannanvnteetKQDLAEADMVVFFGDFNYRLFGISYDEARD 810
Cdd:smart00128  154 EQRNQDYKTILRALSFPERA------------------------------LLSQFDHDVVFWFGDLNFRLDSPSYEEVRR 203

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645    811 FVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhRPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESEC 890
Cdd:smart00128  204 KISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFPPTYKYD--SVGTETYDTSEKKRVPAWCDRILYRSNGPELIQLS 281

                           330       340       350
                    ....*....|....*....|....*....|....*
gi 240254645    891 SldcpvvasimlYDACMDVTESDHKPVRCKFHVKI 925
Cdd:smart00128  282 E-----------YHSGMEITTSDHKPVFATFRLKV 305
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 577-923 3.59e-70

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: 237.21  E-value: 3.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  577 RILTGSWNV-GQGKAShdALMSWLGSVASDVGILVVGLQEVEMGA-GFLAMSAAKEsvggnegstigQYWIDTIGKTLDE 654
Cdd:cd09093     2 RIFVGTWNVnGQSPDE--SLRPWLSCDEEPPDIYAIGFQELDLSAeAFLFNDSSRE-----------QEWVKAVERGLHP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  655 KAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNRRN 734
Cdd:cd09093    69 DAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  735 ADFDHIYKTMSFTRSSNAHnapaagVSTGSHttksannanvnteetkqdlaeaDMVVFFGDFNYRLFGISYDEARDFVSQ 814
Cdd:cd09093   149 QDYKDICARMKFEDPDGPP------LSISDH----------------------DVVFWLGDLNYRIQELPTEEVKELIEK 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  815 RSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESecsldc 894
Cdd:cd09093   201 NDLEELLKYDQLNIQRRAGKVFEGFTEGEINFIPTYKYD---PGTDNWDSSEKCRAPAWCDRILWRGTNIVQLS------ 271

                         330       340
                  ....*....|....*....|....*....
gi 240254645  895 pvvasimlYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09093   272 --------YRSHMELKTSDHKPVSALFDI 292
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 576-917 6.50e-62

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: 213.36  E-value: 6.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGqGKASHDALMSWL--GSVASDVGILVVGLQE-VEMGAGFLAMSAAKESvggnegstigQYWIDTIGKTL 652
Cdd:cd09090     1 INIFVGTFNVN-GKSYKDDLSSWLfpEENDELPDIVVIGLQEvVELTAGQILNSDPSKS----------SFWEKKIKTTL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  653 DEKAV--FERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAV 730
Cdd:cd09090    70 NGRGGekYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  731 NRRNADFDHIYKTMSFTRssnahnapaaGVSTGSHttksannanvnteetkqdlaeaDMVVFFGDFNYRLfGISYDEARD 810
Cdd:cd09090   150 EERNNDYKTIARGLRFSR----------GRTIKDH----------------------DHVIWLGDFNYRI-SLTNEDVRR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  811 FVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESec 890
Cdd:cd09090   197 FILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITFPPTYKYD---KGTDNYDTSEKQRIPAWTDRILYRGENLRQLS-- 271

                         330       340
                  ....*....|....*....|....*..
gi 240254645  891 sldcpvvasimlYDACMDVTeSDHKPV 917
Cdd:cd09090   272 ------------YNSAPLRF-SDHRPV 285
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 577-921 4.37e-53

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: 188.35  E-value: 4.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  577 RILTGSWNVGQgKASHDALMSWLGSVASDVG--ILVVGLQEVEMGAGFLAMSAAKESVggnegstigqyWIDTIGKTLDE 654
Cdd:cd09094     2 RVYVVTWNVAT-APPPIDVRSLLGLQSPEVApdIYIIGLQEVNSKPVQFVSDLIFDDP-----------WSDLFMDILSP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  655 KAVFeRMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNRRN 734
Cdd:cd09094    70 KGYV-KVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  735 ADFDHIYKTMSFtrssNAHNAPaagvSTGSHttksannanvnteetkqdlaeaDMVVFFGDFNYRLFGISYDEARDFVSQ 814
Cdd:cd09094   149 DDFETILSTQVF----NECNTP----SILDH----------------------DYVFWFGDLNFRIEDVSIEFVRELVNS 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  815 RSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFR-DTRTSPESEcsld 893
Cdd:cd09094   199 KKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFD---LGTDEYDTSGKKRKPAWTDRILWKvNPDASTEEK---- 271

                         330       340
                  ....*....|....*....|....*...
gi 240254645  894 cPVVASIMLYDACMDVTESDHKPVRCKF 921
Cdd:cd09094   272 -FLSITQTSYKSHMEYGISDHKPVTAQF 298
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
548-941 1.47e-48

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 180.36  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  548 PVISPGPLDGIIRSELAEKERTYAQTDSVRILTGSWNVgQGKASHDALMSWL---GSVASDVGILVVGLQE-VEMGAG-F 622
Cdd:COG5411     2 PVPIYDPRHPYIVAVLRQRRSKYVIEKDVSIFVSTFNP-PGKPPKASTKRWLfpeIEATELADLYVVGLQEvVELTPGsI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  623 LAMSAAKESvggnegstigQYWIDTIGKTLDEKAVFE---RMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAI 699
Cdd:COG5411    81 LSADPYDRL----------RIWESKVLDCLNGAQSDEkysLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  700 GNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNRRNADFDHIYKTMSFTRSsnahnapaagvstgshttksannanvntee 779
Cdd:COG5411   151 SNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRG------------------------------ 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  780 tkQDLAEADMVVFFGDFNYRLFGiSYDEARDFVSQ--RSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrP 857
Cdd:COG5411   201 --LRIYDHDTIFWLGDLNYRVTS-TNEEVRPEIASddGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFD---Y 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  858 GLGGYDSGEKKRIPAWCDRVIFRDTRTSPESecsldcpvvasimlYDACMDVTESDHKPVRCKFHVKIEHVDRSVRRQEF 937
Cdd:COG5411   275 GTDEYDTSDKGRIPSWTDRILYKSEQLTPHS--------------YSSIPHLMISDHRPVYATFRAKIKVVDPSKKEGLI 340


                  ....
gi 240254645  938 GRII 941
Cdd:COG5411   341 EKLY 344
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 576-917 1.92e-47

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: 172.96  E-value: 1.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKA------SHDALMSWL--------------GSVASDVGILVVGLQE-VEMGAGFLAMSAakesvgg 634
Cdd:cd09089     1 LRVFVGTWNVNGGKHfrsiafKHQSMTDWLldnpklagqcsndsEEDEKPVDIFAIGFEEmVDLNASNIVSAS------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  635 negSTIGQYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDR 714
Cdd:cd09089    74 ---TTNQKEWGEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHST 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  715 IMCFINCHLAAHLEAVNRRNADFDHIYKTMSFTRssnahnapaaGVSTGSHttksannanvnteetkqdlaeaDMVVFFG 794
Cdd:cd09089   151 SLCFVCSHFAAGQSQVKERNEDFAEIARKLSFPM----------GRTLDSH----------------------DYVFWCG 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  795 DFNYRLfGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrpgLGG--YDSGEKKRIPA 872
Cdd:cd09089   199 DFNYRI-DLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYD-----LFSddYDTSEKCRTPA 272

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240254645  873 WCDRVIFRDTRTSPESECSLDCPVVAS------IMLYDACmDVTESDHKPV 917
Cdd:cd09089   273 WTDRVLWRRRKWPSDKTEESLVETNDPtwnpgtLLYYGRA-ELKTSDHRPV 322
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 642-934 3.79e-40

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 158.92  E-value: 3.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  642 QYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINC 721
Cdd:PLN03191  348 QLPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCS 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  722 HLAAHLE--AVNRRNADfdhIYKTMSFTRSSNAHNApaagvstgshttksannanvnteETKQDLAEADMVVFFGDFNYR 799
Cdd:PLN03191  428 HLTSGHKdgAEQRRNAD---VYEIIRRTRFSSVLDT-----------------------DQPQTIPSHDQIFWFGDLNYR 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  800 LfGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPGLGGYD--SGEKKRIPAWCDRV 877
Cdd:PLN03191  482 L-NMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYVGENpkEGEKKRSPAWCDRI 560

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240254645  878 IFRDTRTSPESecsldcpvvasimlYDACmDVTESDHKPVRCKFHVKIEHVD-RSVRR 934
Cdd:PLN03191  561 LWLGKGIKQLC--------------YKRS-EIRLSDHRPVSSMFLVEVEVFDhRKLQR 603
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 576-917 1.54e-37

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This subfamily contains the INPP5c domains of human synaptojanin 1 (Synj1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro.


Pssm-ID: 197332  Cd Length: 336  Bit Score: 144.41  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKA------SHDALMSWLGSVASDVG-------------ILVVGLQE-VEMGAGFLAmsaakesvggN 635
Cdd:cd09098     1 IRVCVGTWNVNGGKQfrsiafKNQTLTDWLLDAPKKAGipefqdvrskpvdIFAIGFEEmVELNAGNIV----------S 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  636 EGSTIGQYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRI 715
Cdd:cd09098    71 ASTTNQKLWAAELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  716 MCFINCHLAAHLEAVNRRNADFDHIYKTMSFtrssnahnapAAGVSTGSHttksannanvnteetkqdlaeaDMVVFFGD 795
Cdd:cd09098   151 LCFVCSHFAAGQSQVKERNEDFIEIARKLSF----------PMGRMLFSH----------------------DYVFWCGD 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  796 FNYRLfGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPglgGYDSGEKKRIPAWCD 875
Cdd:cd09098   199 FNYRI-DIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSD---DYDTSEKCRTPAWTD 274

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240254645  876 RVIFRDTR--------------TSPESECSLDCPVVASIMLYDACMDVTESDHKPV 917
Cdd:cd09098   275 RVLWRRRKwpfdrsaedldllnASFPDNSKEQYTWSPGTLLHYGRAELKTSDHRPV 330
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 576-917 4.01e-37

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: 143.24  E-value: 4.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDALMS------WL---------------GSVASDvgILVVGLQE-VEMGAGFLAmsaakesvg 633
Cdd:cd09099     1 TRVAMGTWNVNGGKQFRSNILGtseltdWLldspklsgtpdfqddESNPPD--IFAVGFEEmVELSAGNIV--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  634 gNEGSTIGQYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFD 713
Cdd:cd09099    70 -NASTTNRKMWGEQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  714 RIMCFINCHLAAHLEAVNRRNADFDHIYKTMSFTRSSNAHnapaagvstgSHttksannanvnteetkqdlaeaDMVVFF 793
Cdd:cd09099   149 TSFCFICSHLTAGQNQVKERNEDYKEITQKLSFPMGRNVF----------SH----------------------DYVFWC 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  794 GDFNYRLfGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAW 873
Cdd:cd09099   197 GDFNYRI-DLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYD---VGSEAYDTSDKCRTPAW 272

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240254645  874 CDRVIFRDTRTSPE----------SECSLDCPV----VASIMLYDACMDVTESDHKPV 917
Cdd:cd09099   273 TDRVLWWRKKWPFEktageinlldSDLDFDTKIrhtwTPGALMYYGRAELQASDHRPV 330
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 575-923 5.74e-32

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: 127.15  E-value: 5.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  575 SVRILTGSWNVGQGKASHDALMSWLGSVASDVG--ILVVGLQEvemgagflAMSAAKEsvggnegstigqyWIDTIGKTL 652
Cdd:cd09095     4 NVGIFVATWNMQGQKELPENLDDFLLPTSADFAqdIYVIGVQE--------GCSDRRE-------------WEIRLQETL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  653 DEKAVFerMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNR 732
Cdd:cd09095    63 GPSHVL--LHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKE 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  733 RNADFDHIYKTMSFTRssnahNAPAAGVSTgshttksaNNANVNTEetkqdlaeADMVVFFGDFNYRLfgisyDEARDFV 812
Cdd:cd09095   141 RVLDYNKIIQALNLPR-----NVPTNPYKS--------ESGDVTTR--------FDEVFWFGDFNFRL-----SGPRHLV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  813 SQ-------RSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFErhrPGLGGYDSGEKKRIPAWCDRVIFRdTRTS 885
Cdd:cd09095   195 DAlinqgqeVDVSALLQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFD---IGSDVYDTSSKQRVPSYTDRILYR-SRQK 270

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 240254645  886 PESECsldcpvvasiMLYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09095   271 GDVCC----------LKYNSCPSIKTSDHRPVFALFRV 298
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 576-923 2.12e-27

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: 113.91  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDaLMSW-----LGSVASDVG------ILVVGLQEvemgagflamsaakESVGGNEgstigqyW 644
Cdd:cd09101     1 ISIFIGTWNMGSVPPPKS-LASWltsrgLGKTLDETTvtiphdIYVFGTQE--------------NSVGDRE-------W 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  645 IDTIGKTLDEKAVFER--MGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCH 722
Cdd:cd09101    59 VDFLRASLKELTDIDYqpIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  723 LAAHLEAVNRRNADFDHIYKTMSFTrssnahnapaagvstgshtTKSANNANVNTEETKqdlaeadmVVFFGDFNYRLfG 802
Cdd:cd09101   139 LTSGNEKTHRRNQNYLDILRSLSLG-------------------DKQLNAFDISLRFTH--------LFWFGDLNYRL-D 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  803 ISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERhrpglGGYDS---------GEKKRIPAW 873
Cdd:cd09101   191 MDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFREEEISFPPTYRYER-----GSRDTymwqkqkttGMRTNVPSW 265

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 240254645  874 CDRVIFrdtRTSPESECsldcpVVASimlYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09101   266 CDRILW---KSYPETHI-----VCNS---YGCTDDIVTSDHSPVFGTFEV 304
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 576-923 1.66e-23

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: 102.72  E-value: 1.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDaLMSW-----LGSVASDVG------ILVVGLQEvemgagflamsaakESVGGNEgstigqyW 644
Cdd:cd09091     1 ISIFIGTWNMGSAPPPKN-ITSWftskgQGKTRDDVAdyiphdIYVIGTQE--------------DPLGEKE-------W 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  645 IDTIGKTLDE--KAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCH 722
Cdd:cd09091    59 LDLLRHSLKEltSLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  723 LAAHLEAVNRRNADFDHIYKTMSFTrssnahnapaagvstgshtTKSANNANVNTEETKqdlaeadmVVFFGDFNYRLfG 802
Cdd:cd09091   139 LTSGSEKKLRRNQNYLNILRFLSLG-------------------DKKLSAFNITHRFTH--------LFWLGDLNYRL-D 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  803 ISYDEARDFVS---QRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPGLGGYD----SGEKKRIPAWCD 875
Cdd:cd09091   191 LPIQEAENIIQkieQQQFEPLLRHDQLNLEREEHKVFLRFSEEEITFPPTYRYERGSRDTYAYTkqkaTGVKYNLPSWCD 270

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 240254645  876 RVIFrdtRTSPESECsldcpVVASimlYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09091   271 RILW---KSYPETHI-----ICQS---YGCTDDIVTSDHSPVFGTFEV 307
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 576-923 2.65e-22

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: 99.29  E-value: 2.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  576 VRILTGSWNVGQGKASHDaLMSWL-----GSVASDVG------ILVVGLQEVEMGAgflamsaaKEsvggnegstigqyW 644
Cdd:cd09100     1 ITIFIGTWNMGNAPPPKK-ITSWFqckgqGKTRDDTAdyiphdIYVIGTQEDPLGE--------KE-------------W 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  645 IDTIGKTLDE--KAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCH 722
Cdd:cd09100    59 LDTLKHSLREitSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  723 LAAHLEAVNRRNADFDHIYKTMSFTrssnahnapaagvstgshtTKSANNANVNTEETKqdlaeadmVVFFGDFNYRLfG 802
Cdd:cd09100   139 LTSGSEKKLRRNQNYFNILRFLVLG-------------------DKKLSPFNITHRFTH--------LFWLGDLNYRV-E 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  803 ISYDEARDFVS---QRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPGLGGYD----SGEKKRIPAWCD 875
Cdd:cd09100   191 LPNTEAENIIQkikQQQYQELLPHDQLLIERKESKVFLQFEEEEITFAPTYRFERGTRERYAYTkqkaTGMKYNLPSWCD 270

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 240254645  876 RVIFRDTrtspesecsldcPVVASI-MLYDACMDVTESDHKPVRCKFHV 923
Cdd:cd09100   271 RVLWKSY------------PLVHVVcQSYGCTDDITTSDHSPVFATFEV 307
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 836-923 1.84e-05

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: 48.62  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  836 FQGMREAIITFPPTYKFERHrpglggYDSGE---KKRIPAWCDRVIFRDTRTSPESEcsldcpVVASIMLYDAC-MDVTE 911
Cdd:cd09092   304 KDVLYELDISFPPSYPYSED------PEQGTqymNTRCPAWCDRILMSHSARELKSE------NEEKSVTYDMIgPNVCM 371

                          90
                  ....*....|..
gi 240254645  912 SDHKPVRCKFHV 923
Cdd:cd09092   372 GDHKPVFLTFRI 383
WD40 COG2319
WD40 repeat [General function prediction only];
174-549 8.97e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  174 AGQESGVRFWNFDDafepgcGLSGRVQRGDEDAApfqESASTSPttclmvdNGNRLVwSGHKDGKIRSWKmdyvLDDGdd 253
Cdd:COG2319    96 ASADGTVRLWDLAT------GLLLRTLTGHTGAV---RSVAFSP-------DGKTLA-SGSADGTVRLWD----LATG-- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  254 spfKEGLAWQAHKGPVNSVIMSSygD---LWSCSEGGVIKIWTWESMEKSLSLRleekhmaallvERSGIDLRAQVTVNG 330
Cdd:COG2319   153 ---KLLRTLTGHSGAVTSVAFSP--DgklLASGSDDGTVRLWDLATGKLLRTLT-----------GHTGAVRSVAFSPDG 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  331 TcnisssevkcLLAdnvrskvWAAQLQTFSLWDGRTKELLKVFNSEGQTENRVDM-PLGQdqpaaedemkaKIASTSKke 409
Cdd:COG2319   217 K----------LLA-------SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDGR-----------LLASGSA-- 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  410 kpHGFLQ-------RSRNAIMGAADAVRRVATRGGGAYedakrteamvLAgdgmiwTGCTNGLLIQWD-GNGNRLQDFRH 481
Cdd:COG2319   267 --DGTVRlwdlatgELLRTLTGHSGGVNSVAFSPDGKL----------LA------SGSDDGTVRLWDlATGKLLRTLTG 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254645  482 HQCAV--LCFCTFGERIYIGYVSGHIQIIDLE-GNLIAGWVAHNNAVIKMA-AADG-YIFSLATHGGIRGWPV 549
Cdd:COG2319   329 HTGAVrsVAFSPDGKTLASGSDDGTVRLWDLAtGELLRTLTGHTGAVTSVAfSPDGrTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 215-547 2.80e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 44.25  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  215 TSPTTCLMVDNGNRLVWSGHKDGKIRSWKMDyvlddgDDSPFKEGlawQAHKGPVNSVIMSSYGD-LWSCSEGGVIKIWT 293
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLE------TGELLRTL---KGHTGPVRDVAASADGTyLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  294 WESMEKSlslrleekhmaallversgidlraqVTVNG-TCNISSsevkCLLADNVRSKVWAAQLQTFSLWDGRTKELLKV 372
Cdd:cd00200    80 LETGECV-------------------------RTLTGhTSYVSS----VAFSPDGRILSSSSRDKTIKVWDVETGKCLTT 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  373 FNsegqtenrvdmplgqdqpaaedemkakiastskkekphgflqrsrnaimGAADAVRRVATRGGGayedakrteaMVLA 452
Cdd:cd00200   131 LR-------------------------------------------------GHTDWVNSVAFSPDG----------TFVA 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645  453 GdgmiwtGCTNGLLIQWDGNGNRL-QDFRHHQCAVLCFCTF--GERIYIGYVSGHIQIIDL-EGNLIAGWVAHNNAVIKM 528
Cdd:cd00200   152 S------SSQDGTIKLWDLRTGKCvATLTGHTGEVNSVAFSpdGEKLLSSSSDGTIKLWDLsTGKCLGTLRGHENGVNSV 225

                         330       340
                  ....*....|....*....|.
gi 240254645  529 AAA-DGYIFSLATHGG-IRGW 547
Cdd:cd00200   226 AFSpDGYLLASGSEDGtIRVW 246
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1206-1287 4.64e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1206 SKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKND 1285
Cdd:NF033609  654 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 733


                  ..
gi 240254645 1286 GD 1287
Cdd:NF033609  734 SD 735
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1190-1287 1.01e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.74  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1190 GDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSH 1269
Cdd:NF033609  668 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 747

                          90
                  ....*....|....*...
gi 240254645 1270 KKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  748 SDSDSDSDSDSDSDSDSD 765
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1170-1314 1.20e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.36  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1170 SKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKND 1249
Cdd:NF033609  726 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 805

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254645 1250 GDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKNDGDSSSSYKSQSGK-KNSNSSTVEESRNNHN 1314
Cdd:NF033609  806 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSESDSNSDSESGSNNN 871
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1185-1287 1.23e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.36  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1185 SKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDS 1264
Cdd:NF033609  669 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 748

                          90       100
                  ....*....|....*....|...
gi 240254645 1265 SSKSHKKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  749 DSDSDSDSDSDSDSDSDSDSDSD 771
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1178-1287 1.78e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1178 GDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSH 1257
Cdd:NF033609  668 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 747

                          90       100       110
                  ....*....|....*....|....*....|
gi 240254645 1258 KKSDGDSSSKSHKKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  748 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 777
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1194-1312 3.99e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1194 SKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSE 1273
Cdd:NF033609  720 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 799

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 240254645 1274 GDSSSKSHKKNDGDSSSSYKSQSGKKNSNSSTVEESRNN 1312
Cdd:NF033609  800 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 838
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 219-292 4.01e-03

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 40.78  E-value: 4.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254645  219 TCLMVDNGNRLVWSGHKDGKIRSWkmdyvlddgDDSPFKEGLAWQAHKGPVNSVIMS-SYGDLWSCSEGGVIKIW 292
Cdd:cd00200   223 NSVAFSPDGYLLASGSEDGTIRVW---------DLRTGECVQTLSGHTNSVTSLAWSpDGKRLASGSADGTIRIW 288
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1197-1287 4.57e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.43  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1197 SKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDS 1276
Cdd:NF033609  711 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 790

                          90
                  ....*....|.
gi 240254645 1277 SSKSHKKNDGD 1287
Cdd:NF033609  791 DSDSDSDSDSD 801
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1197-1287 5.65e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1197 SKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDS 1276
Cdd:NF033609  705 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 784

                          90
                  ....*....|.
gi 240254645 1277 SSKSHKKNDGD 1287
Cdd:NF033609  785 DSDSDSDSDSD 795
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1170-1312 6.09e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1170 SKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKND 1249
Cdd:NF033609  720 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 799

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254645 1250 GDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKNDGDSSSSYKSQSGKKNSNSSTVEESRNN 1312
Cdd:NF033609  800 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNS 862
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1190-1287 9.54e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254645 1190 GDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSH 1269
Cdd:NF033609  714 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 793

                          90
                  ....*....|....*...
gi 240254645 1270 KKSEGDSSSKSHKKNDGD 1287
Cdd:NF033609  794 SDSDSDSDSDSDSDSDSD 811
 
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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