NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462583457|ref|XP_054180920|]
View 

synaptojanin-1 isoform X15 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
572-907 0e+00

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: 768.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWA 651
Cdd:cd09098      1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 731
Cdd:cd09098     81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  732 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 811
Cdd:cd09098    161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  812 FLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 891
Cdd:cd09098    241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                          330
                   ....*....|....*.
gi 2462583457  892 ELKTSDHRPVVALIDI 907
Cdd:cd09098    321 ELKTSDHRPVVALIDI 336
COG5329 super family cl34984
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
73-519 7.79e-93

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


The actual alignment was detected with superfamily member COG5329:

Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 311.25  E-value: 7.79e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   73 ESGAVAVLSSAEKEAIKGTYSKvldaYGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLR------ 146
Cdd:COG5329     39 ELVGVRFEPDEGFSSLSSAHKI----YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNnnkwdd 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  147 IDSSDEDRI---SEVRKVLNSGNFYFA--WSASGiSLDLSLNAHRSMQEQTTDNRFFWNQSL------HLHLKHYGVNCD 215
Cdd:COG5329    111 ELEEDEANYdklSELKKLLSNGTFYFSydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQF 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  216 D-WLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPL 294
Cdd:COG5329    190 DnFLTTVIRGFAETVDIKVGGNTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  295 FWEQPGLQVGShRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHaADIQMVNFDY 374
Cdd:COG5329    270 FWEQSNLLYGP-KIKVTRSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKK-PKIHYTEFDF 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  375 HQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFNGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAE 452
Cdd:COG5329    348 HKETSQDGFDDVKKLLYLIEQDLLEFGYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISD 427
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  453 KpqlVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKA----------KLKDGARSVTRTIQNNFFDSSKQEAIDVLL 519
Cdd:COG5329    428 G---YSPFLQIHRELWADNGDAISRLYTGTGALKSSFtrrgrrsfagALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
906-1047 4.79e-68

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


:

Pssm-ID: 286093  Cd Length: 146  Bit Score: 225.46  E-value: 4.79e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  906 DIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKS-SLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEG 984
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583457  985 SSALNVLSLNGKELLNRTITIALKSPDWIKNLEEEM---SLEKISIAlpSSTSSTLLGEDAEVAAD 1047
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIilcTDNTIPVS--PCANSTLLAEDFDFGSP 144
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1093-1301 1.21e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.42  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1093 PTISEGPV-PSLPIRPSRAPS----RTPGPPSAQSSPidAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPP 1167
Cdd:PHA03247  2742 PAVPAGPAtPGGPARPARPPTtagpPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP 2819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1168 PSGARSPAPTRKEFGAPKSPGTTRkdniGRSQPS-PQAGLAGPG-------PAGYSTARPTIP--PRAGVISAPQSHARA 1237
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPP----GPPPPSlPLGGSVAPGgdvrrrpPSRSPAAKPAAParPPVRRLARPAVSRST 2895
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457 1238 SAGRLTPESQSKTSETSkgstfLPEPLKPQAAFPPQSSL---PPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQ-----APPPPQPQPQPPPPPQPqppPPPPPRPQPPLAPTTDPAGAGEPSG 2957
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
572-907 0e+00

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: 768.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWA 651
Cdd:cd09098      1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 731
Cdd:cd09098     81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  732 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 811
Cdd:cd09098    161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  812 FLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 891
Cdd:cd09098    241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                          330
                   ....*....|....*.
gi 2462583457  892 ELKTSDHRPVVALIDI 907
Cdd:cd09098    321 ELKTSDHRPVVALIDI 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
570-910 6.14e-128

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 396.72  E-value: 6.14e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   570 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKL 649
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   650 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   730 AAGQSQVKERNEDFIEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 806
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   807 QVFRGFLEGKVTFAPTYKYDLF-SDDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 885
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 2462583457   886 lHYGRAELKTSDHRPVVALIDIDIF 910
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
73-519 7.79e-93

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 311.25  E-value: 7.79e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   73 ESGAVAVLSSAEKEAIKGTYSKvldaYGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLR------ 146
Cdd:COG5329     39 ELVGVRFEPDEGFSSLSSAHKI----YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNnnkwdd 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  147 IDSSDEDRI---SEVRKVLNSGNFYFA--WSASGiSLDLSLNAHRSMQEQTTDNRFFWNQSL------HLHLKHYGVNCD 215
Cdd:COG5329    111 ELEEDEANYdklSELKKLLSNGTFYFSydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQF 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  216 D-WLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPL 294
Cdd:COG5329    190 DnFLTTVIRGFAETVDIKVGGNTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  295 FWEQPGLQVGShRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHaADIQMVNFDY 374
Cdd:COG5329    270 FWEQSNLLYGP-KIKVTRSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKK-PKIHYTEFDF 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  375 HQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFNGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAE 452
Cdd:COG5329    348 HKETSQDGFDDVKKLLYLIEQDLLEFGYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISD 427
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  453 KpqlVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKA----------KLKDGARSVTRTIQNNFFDSSKQEAIDVLL 519
Cdd:COG5329    428 G---YSPFLQIHRELWADNGDAISRLYTGTGALKSSFtrrgrrsfagALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
99-379 2.07e-87

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


Pssm-ID: 460545  Cd Length: 295  Bit Score: 286.01  E-value: 2.07e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   99 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRIDSSD----------EDRI-SEVRKVLNSGNF 167
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGHPIYKITDVEFIPLNSSLSDtqlakkehpdEERLlKLLKLFLSSGSF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  168 YFAWSasgisLDLSlnahRSMQEQTT----------DNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQ 237
Cdd:pfam02383   77 YFSYD-----YDLT----NSLQRNLTrsrspsfdslDDRFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  238 AKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDS-----VSSFIQIRGSVPLFWEQPGLQVGSHRVRMSR 312
Cdd:pfam02383  148 VTLTLISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTSnsegkIFSFVQIRGSIPLFWSQDPNLKYKPKIQITR 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583457  313 gFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKAS--EHAADIQMVNFDYHQMVK 379
Cdd:pfam02383  228 -PEATQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEEAVKYLnqFLPDKLRYTAFDFHHECK 295
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
565-933 1.25e-71

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 247.39  E-value: 1.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  565 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVSA 642
Cdd:COG5411     23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  643 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 717
Cdd:COG5411     84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  718 HTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 795
Cdd:COG5411    163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  796 GDQLINQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 875
Cdd:COG5411    243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462583457  876 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIA--VQGPPDG 933
Cdd:COG5411    299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
906-1047 4.79e-68

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


Pssm-ID: 286093  Cd Length: 146  Bit Score: 225.46  E-value: 4.79e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  906 DIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKS-SLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEG 984
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583457  985 SSALNVLSLNGKELLNRTITIALKSPDWIKNLEEEM---SLEKISIAlpSSTSSTLLGEDAEVAAD 1047
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIilcTDNTIPVS--PCANSTLLAEDFDFGSP 144
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
663-915 8.59e-51

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 190.89  E-value: 8.59e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  663 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 740
Cdd:PLN03191   363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  741 EDFIEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLE 814
Cdd:PLN03191   443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  815 GKVTFAPTYKYDLFSDDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 889
Cdd:PLN03191   523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                          250       260
                   ....*....|....*....|....*.
gi 2462583457  890 RAELKTSDHRPVVAlididIFEVEAE 915
Cdd:PLN03191   574 RSEIRLSDHRPVSS-----MFLVEVE 594
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
932-1008 8.78e-42

RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup corresponds to the RRM of synaptojanin-1, also termed synaptojanin, or synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1, originally identified as one of the major Grb2-binding proteins that may participate in synaptic vesicle endocytosis. It also acts as a Src homology 3 (SH3) domain-binding brain-specific inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Synaptojanin-1 contains an N-terminal domain homologous to the cytoplasmic portion of the yeast protein Sac1p, a central inositol 5-phosphatase domain followed by a putative RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal proline-rich region mediating the binding of synaptojanin-1 to various SH3 domain-containing proteins including amphiphysin, SH3p4, SH3p8, SH3p13, and Grb2. Synaptojanin-1 has two tissue-specific alternative splicing isoforms, synaptojanin-145 expressed in brain and synaptojanin-170 expressed in peripheral tissues. Synaptojanin-145 is very abundant in nerve terminals and may play an essential role in the clathrin-mediated endocytosis of synaptic vesicles. In contrast to synaptojanin-145, synaptojanin-170 contains three unique asparagine-proline-phenylalanine (NPF) motifs in the C-terminal region and may functions as a potential binding partner for Eps15, a clathrin coat-associated protein acting as a major substrate for the tyrosine kinase activity of the epidermal growth factor receptor.


Pssm-ID: 410118  Cd Length: 77  Bit Score: 147.55  E-value: 8.78e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  932 DGTVLVSIKSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITIALK 1008
Cdd:cd12719      1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
1093-1301 1.21e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.42  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1093 PTISEGPV-PSLPIRPSRAPS----RTPGPPSAQSSPidAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPP 1167
Cdd:PHA03247  2742 PAVPAGPAtPGGPARPARPPTtagpPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP 2819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1168 PSGARSPAPTRKEFGAPKSPGTTRkdniGRSQPS-PQAGLAGPG-------PAGYSTARPTIP--PRAGVISAPQSHARA 1237
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPP----GPPPPSlPLGGSVAPGgdvrrrpPSRSPAAKPAAParPPVRRLARPAVSRST 2895
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457 1238 SAGRLTPESQSKTSETSkgstfLPEPLKPQAAFPPQSSL---PPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQ-----APPPPQPQPQPPPPPQPqppPPPPPRPQPPLAPTTDPAGAGEPSG 2957
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1049-1329 1.22e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 62.86  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1049 DMEGDVDDySAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPSAQSSPID-- 1126
Cdd:pfam03154  153 DNESDSDS-SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTli 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1127 AQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTR------KEFGAPKSPGTTRKDNIGRSQP 1200
Cdd:pfam03154  232 QQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQtgpshmQHPVPPQPFPLTPQSSQSQVPP 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1201 SPQAGLAGPG------PAGYSTARPTIPPRAGVIS-APQSHARASAGRLTPESQSKTSETSKG-------STF-----LP 1261
Cdd:pfam03154  312 GPSPAAPGQSqqrihtPPSQSQLQSQQPPREQPLPpAPLSMPHIKPPPTTPIPQLPNPQSHKHpphlsgpSPFqmnsnLP 391
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462583457 1262 EP--LKPQAAFP---PQSSLPPPAQrlqepLVPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQQ 1329
Cdd:pfam03154  392 PPpaLKPLSSLSthhPPSAHPPPLQ-----LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQ 459
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1091-1301 1.53e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1091 QSPTISEGPVPSLPiRPSRAPSrtPGPPSAQSSPidaQPATPLPQKDPAqplepkrpppprpvapptrpappqrppppsg 1170
Cdd:NF033839   282 DTPKEPGNKKPSAP-KPGMQPS--PQPEKKEVKP---EPETPKPEVKPQ------------------------------- 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1171 ARSPAPTRKEfgAPKSPGTTRKDNIGRSQPSPQAGLAGPGPA---GYSTARPTIPPRAGViSAPQSHARASagrlTPESQ 1247
Cdd:NF033839   325 LEKPKPEVKP--QPEKPKPEVKPQLETPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPET-PKPEVKPQPE----KPKPE 397
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462583457 1248 SKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPlvpvaAPMPQSGPQP 1301
Cdd:NF033839   398 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-----KPKPEVKPQP 446
RRM smart00360
RNA recognition motif;
947-1005 1.80e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.80e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583457   947 NFFDDALIDELLQQFASFGEVILIRFVEDKMW--------VTFLEGSSALNVLS-LNGKELLNRTITI 1005
Cdd:smart00360    6 NLPPDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
1096-1234 3.16e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 40.06  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1096 SEGPVPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATP---------LPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPP 1166
Cdd:cd21975     27 GAGLAAGLDVRATREVAKGPGPPGPAWKPDGADSPGLvtaaphllaANVLAPLRGPSVEGSSLESGDADMGSDSDVAPAS 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583457 1167 PPSGARSPApTRKEFGAPKSPGttrkdnigrsqPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSH 1234
Cdd:cd21975    107 GAAASTSPE-SSSDAASSPSPL-----------SLLHPGEAGLEPERPRPRVRRGVRRRGVTPAAKRH 162
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
572-907 0e+00

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: 768.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWA 651
Cdd:cd09098      1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 731
Cdd:cd09098     81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  732 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 811
Cdd:cd09098    161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  812 FLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 891
Cdd:cd09098    241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                          330
                   ....*....|....*.
gi 2462583457  892 ELKTSDHRPVVALIDI 907
Cdd:cd09098    321 ELKTSDHRPVVALIDI 336
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
572-907 0e+00

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


Pssm-ID: 197323 [Multi-domain]  Cd Length: 328  Bit Score: 689.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQ-EFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLW 650
Cdd:cd09089      1 LRVFVGTWNVNGGKHFRSIAFKHQSMTDWLLDNPKLAGQCsNDSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKEW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  651 AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFA 730
Cdd:cd09089     81 GEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  731 AGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFR 810
Cdd:cd09089    161 AGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  811 GFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDllnasfqdeSKILYTWTPGTLLHYGR 890
Cdd:cd09089    241 GFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPSDKTEESLV---------ETNDPTWNPGTLLYYGR 311
                          330
                   ....*....|....*..
gi 2462583457  891 AELKTSDHRPVVALIDI 907
Cdd:cd09089    312 AELKTSDHRPVVAIIDI 328
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
572-907 0e+00

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: 563.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWA 651
Cdd:cd09099      1 TRVAMGTWNVNGGKQFRSNILGTSELTDWLLDSPKLSGTPDFQDDESNPPDIFAVGFEEMVELSAGNIVNASTTNRKMWG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 731
Cdd:cd09099     81 EQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  732 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 811
Cdd:cd09099    161 GQNQVKERNEDYKEITQKLSFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKD 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  812 FLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 891
Cdd:cd09099    241 FHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWRKKWPFEKTAGEINLLDSDLDFDTKIRHTWTPGALMYYGRA 320
                          330
                   ....*....|....*.
gi 2462583457  892 ELKTSDHRPVVALIDI 907
Cdd:cd09099    321 ELQASDHRPVLAIVEV 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
570-910 6.14e-128

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 396.72  E-value: 6.14e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   570 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKL 649
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   650 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   730 AAGQSQVKERNEDFIEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 806
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   807 QVFRGFLEGKVTFAPTYKYDLF-SDDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 885
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 2462583457   886 lHYGRAELKTSDHRPVVALIDIDIF 910
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
572-907 3.28e-108

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: 343.55  E-value: 3.28e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLDAPklagiqefqdkrSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWA 651
Cdd:cd09074      1 VKIFVVTWNVGGGI------SPPENLENWLSPKG------------TEAPDIYAVGVQEVDMSVQGFVGNDDSAKAREWV 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAV--DTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:cd09074     63 DNIQEALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVegVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHL 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  730 AAGQSQVKERNEDFIEIARKLSFPMG----RMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNA 805
Cdd:cd09074    143 AAGQEEVERRNQDYRDILSKLKFYRGdpaiDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEK 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  806 GQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdeskilYTWTPGTL 885
Cdd:cd09074    223 GKVFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKS--------------------------KAGSEIQP 276
                          330       340
                   ....*....|....*....|...
gi 2462583457  886 LHYGRAEL-KTSDHRPVVALIDI 907
Cdd:cd09074    277 LSYTSVPLyKTSDHKPVRATFRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
572-903 4.66e-106

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae Inp51p, Inp52p, and Inp53p, and related proteins; This subfamily contains the INPP5c domain of three Saccharomyces cerevisiae synaptojanin-like inositol polyphosphate 5-phosphatases (INP51, INP52, and INP53), Schizosaccharomyces pombe synaptojanin (SPsynaptojanin), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, these proteins have an N-terminal catalytic Sac1-like domain (found in other proteins including the phophoinositide phosphatase Sac1p), and a C-terminal proline-rich domain (PRD). The Sac1 domain allows Inp52p and Inp53p to recognize and dephosphorylate a wider range of substrates including PI3P, PI4P, and PI(3,5)P2. The Sac1 domain of Inp51p is non-functional. Disruption of any two of INP51, INP52, and INP53, in S. cerevisiae leads to abnormal vacuolar and plasma membrane morphology. During hyperosmotic stress, Inp52p and Inp53p localize at actin patches, where they may facilitate the hydrolysis of PI(4,5)P2, and consequently promote actin rearrangement to regulate cell growth. SPsynaptojanin is also active against a range of soluble and lipid inositol phosphates, including I(1,4,5)P3, I(1,3,4,5)P4, I(1,4,5,6)P4, PI(4,5)P2, and PIP3. Transformation of S. cerevisiae with a plasmid expressing the SPsynaptojanin 5-phosphatase domain rescues inp51/inp52/inp53 triple-mutant strains.


Pssm-ID: 197324  Cd Length: 291  Bit Score: 337.39  E-value: 4.66e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGgkqfrsiAFKNQTLTDWLldapklagiqeFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWA 651
Cdd:cd09090      1 INIFVGTFNVNG-------KSYKDDLSSWL-----------FPEENDELPDIVVIGLQEVVELTAGQILNSDPSKSSFWE 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:cd09090     63 KKIKTTLNGrgGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHL 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  730 AAGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVF 809
Cdd:cd09090    143 AAGLTNYEERNNDYKTIARGLRFSRGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVF 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  810 RGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRrrkwpfdrsAEDLDLLNasfqdeskilytwtpgtllhYG 889
Cdd:cd09090    223 PGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYR---------GENLRQLS--------------------YN 273
                          330
                   ....*....|....
gi 2462583457  890 RAELKTSDHRPVVA 903
Cdd:cd09090    274 SAPLRFSDHRPVYA 287
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
572-907 3.25e-101

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: 324.27  E-value: 3.25e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKqfrsiafKNQTLTDWLldapklagiqefqDKRSKPTDIFAIGFEEmVELNAGNIVSASTTNQKLWA 651
Cdd:cd09093      1 FRIFVGTWNVNGQS-------PDESLRPWL-------------SCDEEPPDIYAIGFQE-LDLSAEAFLFNDSSREQEWV 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 731
Cdd:cd09093     60 KAVERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  732 GQSQVKERNEDFIEIARKLSFPMG----RMLFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQKNAG 806
Cdd:cd09093    140 HMEEVERRNQDYKDICARMKFEDPdgppLSISDHDVVFWLGDLNYRIqELPTEEVKELIEKNDLEELLKYDQLNIQRRAG 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  807 QVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedldllnasfqdESKIlytwtpgTLL 886
Cdd:cd09093    220 KVFEGFTEGEINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWR----------------------GTNI-------VQL 270
                          330       340
                   ....*....|....*....|..
gi 2462583457  887 HYGR-AELKTSDHRPVVALIDI 907
Cdd:cd09093    271 SYRShMELKTSDHKPVSALFDI 292
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
73-519 7.79e-93

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 311.25  E-value: 7.79e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   73 ESGAVAVLSSAEKEAIKGTYSKvldaYGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLR------ 146
Cdd:COG5329     39 ELVGVRFEPDEGFSSLSSAHKI----YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNnnkwdd 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  147 IDSSDEDRI---SEVRKVLNSGNFYFA--WSASGiSLDLSLNAHRSMQEQTTDNRFFWNQSL------HLHLKHYGVNCD 215
Cdd:COG5329    111 ELEEDEANYdklSELKKLLSNGTFYFSydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQF 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  216 D-WLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPL 294
Cdd:COG5329    190 DnFLTTVIRGFAETVDIKVGGNTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  295 FWEQPGLQVGShRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHaADIQMVNFDY 374
Cdd:COG5329    270 FWEQSNLLYGP-KIKVTRSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKK-PKIHYTEFDF 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  375 HQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFNGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAE 452
Cdd:COG5329    348 HKETSQDGFDDVKKLLYLIEQDLLEFGYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISD 427
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  453 KpqlVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKA----------KLKDGARSVTRTIQNNFFDSSKQEAIDVLL 519
Cdd:COG5329    428 G---YSPFLQIHRELWADNGDAISRLYTGTGALKSSFtrrgrrsfagALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
99-379 2.07e-87

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


Pssm-ID: 460545  Cd Length: 295  Bit Score: 286.01  E-value: 2.07e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457   99 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRIDSSD----------EDRI-SEVRKVLNSGNF 167
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGHPIYKITDVEFIPLNSSLSDtqlakkehpdEERLlKLLKLFLSSGSF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  168 YFAWSasgisLDLSlnahRSMQEQTT----------DNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQ 237
Cdd:pfam02383   77 YFSYD-----YDLT----NSLQRNLTrsrspsfdslDDRFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  238 AKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDS-----VSSFIQIRGSVPLFWEQPGLQVGSHRVRMSR 312
Cdd:pfam02383  148 VTLTLISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTSnsegkIFSFVQIRGSIPLFWSQDPNLKYKPKIQITR 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583457  313 gFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKAS--EHAADIQMVNFDYHQMVK 379
Cdd:pfam02383  228 -PEATQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEEAVKYLnqFLPDKLRYTAFDFHHECK 295
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
573-907 7.79e-72

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: 242.28  E-value: 7.79e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  573 RVCVGTWNVnggkqfrSIAFKNQTLTdwlldapKLAGIQEFQDKrskpTDIFAIGFEEmveLNAG---NIVSASTTNQkl 649
Cdd:cd09094      2 RVYVVTWNV-------ATAPPPIDVR-------SLLGLQSPEVA----PDIYIIGLQE---VNSKpvqFVSDLIFDDP-- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  650 WAvELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:cd09094     59 WS-DLFMDILSPKGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHL 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  730 AAGQSQVKERNEDFIEIARKLSFPMGRM--LFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQKNAG 806
Cdd:cd09094    138 PAHMEKWEQRIDDFETILSTQVFNECNTpsILDHDYVFWFGDLNFRIeDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKE 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  807 QVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedLDLLNASFQDESKIlytwtpgTLL 886
Cdd:cd09094    218 EAFQGFQEGPLNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWK------------VNPDASTEEKFLSI-------TQT 278
                          330       340
                   ....*....|....*....|..
gi 2462583457  887 HY-GRAELKTSDHRPVVALIDI 907
Cdd:cd09094    279 SYkSHMEYGISDHKPVTAQFRL 300
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
565-933 1.25e-71

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 247.39  E-value: 1.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  565 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVSA 642
Cdd:COG5411     23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  643 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 717
Cdd:COG5411     84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  718 HTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 795
Cdd:COG5411    163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  796 GDQLINQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 875
Cdd:COG5411    243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462583457  876 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIA--VQGPPDG 933
Cdd:COG5411    299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
906-1047 4.79e-68

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


Pssm-ID: 286093  Cd Length: 146  Bit Score: 225.46  E-value: 4.79e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  906 DIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKS-SLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEG 984
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583457  985 SSALNVLSLNGKELLNRTITIALKSPDWIKNLEEEM---SLEKISIAlpSSTSSTLLGEDAEVAAD 1047
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIilcTDNTIPVS--PCANSTLLAEDFDFGSP 144
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
570-907 2.38e-57

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol polyphosphate-5-phosphatase E and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase E (also called type IV or 72 kDa 5-phosphatase), rat pharbin, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5E hydrolyzes the 5-phosphate from PI(3,5)P2, PI(4,5)P2 and PI(3,4,5)P3, forming PI3P, PI4P, and PI(3,4)P2, respectively. It is a very potent PI(3,4,5)P3 5-phosphatase. Its intracellular localization is chiefly cytosolic, with pronounced perinuclear/Golgi localization. INPP5E also has an N-terminal proline rich domain (PRD) and a C-terminal CAAX motif. This protein is expressed in a variety of tissues, including the breast, brain, testis, and haemopoietic cells. It is differentially expressed in several cancers, for example, it is up-regulated in cervical cancer and down-regulated in stomach cancer. It is a candidate target for therapeutics of obesity and related disorders, as it is expressed in the hypothalamus, and following insulin stimulation, it undergoes tyrosine phosphorylation, associates with insulin receptor substrate-1, -2, and PI3-kinase, and become active as a 5-phosphatase. INPP5E may play a role, along with other 5-phosphatases SHIP2 and SKIP, in regulating glucose homoeostasis and energy metabolism. Mice deficient in INPPE5 develop a multi-organ disorder associated with structural defects of the primary cilium.


Pssm-ID: 197329  Cd Length: 298  Bit Score: 200.73  E-value: 2.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  570 KKIRVCVGTWNVNGGKQFrsiafkNQTLTDWLLdapklAGIQEFQdkrskpTDIFAIGFEEmvelnagnivsaSTTNQKL 649
Cdd:cd09095      3 RNVGIFVATWNMQGQKEL------PENLDDFLL-----PTSADFA------QDIYVIGVQE------------GCSDRRE 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  650 WAVELQKTISrdNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:cd09095     54 WEIRLQETLG--PSHVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHF 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  730 AAGQSQVKERNEDFIEIARKLSFPmgRMLFSHDY-------------VFWCGDFNYRIDLPNEEVKELIRQ---QNWDSL 793
Cdd:cd09095    132 TSGDGKVKERVLDYNKIIQALNLP--RNVPTNPYksesgdvttrfdeVFWFGDFNFRLSGPRHLVDALINQgqeVDVSAL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  794 IAGDQLINQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRkwpfdrsaedldllnasfqde 873
Cdd:cd09095    210 LQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSR--------------------- 268
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2462583457  874 skilytwTPGTL--LHYGRAE-LKTSDHRPVVALIDI 907
Cdd:cd09095    269 -------QKGDVccLKYNSCPsIKTSDHRPVFALFRV 298
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
663-915 8.59e-51

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 190.89  E-value: 8.59e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  663 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 740
Cdd:PLN03191   363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  741 EDFIEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLE 814
Cdd:PLN03191   443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  815 GKVTFAPTYKYDLFSDDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 889
Cdd:PLN03191   523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                          250       260
                   ....*....|....*....|....*.
gi 2462583457  890 RAELKTSDHRPVVAlididIFEVEAE 915
Cdd:PLN03191   574 RSEIRLSDHRPVSS-----MFLVEVE 594
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
932-1008 8.78e-42

RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup corresponds to the RRM of synaptojanin-1, also termed synaptojanin, or synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1, originally identified as one of the major Grb2-binding proteins that may participate in synaptic vesicle endocytosis. It also acts as a Src homology 3 (SH3) domain-binding brain-specific inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Synaptojanin-1 contains an N-terminal domain homologous to the cytoplasmic portion of the yeast protein Sac1p, a central inositol 5-phosphatase domain followed by a putative RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal proline-rich region mediating the binding of synaptojanin-1 to various SH3 domain-containing proteins including amphiphysin, SH3p4, SH3p8, SH3p13, and Grb2. Synaptojanin-1 has two tissue-specific alternative splicing isoforms, synaptojanin-145 expressed in brain and synaptojanin-170 expressed in peripheral tissues. Synaptojanin-145 is very abundant in nerve terminals and may play an essential role in the clathrin-mediated endocytosis of synaptic vesicles. In contrast to synaptojanin-145, synaptojanin-170 contains three unique asparagine-proline-phenylalanine (NPF) motifs in the C-terminal region and may functions as a potential binding partner for Eps15, a clathrin coat-associated protein acting as a major substrate for the tyrosine kinase activity of the epidermal growth factor receptor.


Pssm-ID: 410118  Cd Length: 77  Bit Score: 147.55  E-value: 8.78e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  932 DGTVLVSIKSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITIALK 1008
Cdd:cd12719      1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
572-850 8.99e-41

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: 153.22  E-value: 8.99e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivsaSTTNQKL 649
Cdd:cd09100      1 ITIFIGTWNMGNAPPPKKI-------TSWFQCK----GQGKTRDDTADyiPHDIYVIGTQE------------DPLGEKE 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  650 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 727
Cdd:cd09100     58 WLDTLKHSLREitSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNS 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  728 HFAAGQSQVKERNEDFIEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKEL---IRQQNWDSLIAGDQL 799
Cdd:cd09100    138 HLTSGSEKKLRRNQNYFNILRFLVLgdkKLSPFNITHrfTHLFWLGDLNYRVELPNTEAENIiqkIKQQQYQELLPHDQL 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583457  800 INQKNAGQVFRGFLEGKVTFAPTYKYD-------LFSDDYDTSEKCRTPAWTDRVLWR 850
Cdd:cd09100    218 LIERKESKVFLQFEEEEITFAPTYRFErgtreryAYTKQKATGMKYNLPSWCDRVLWK 275
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
572-907 2.04e-40

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: 152.02  E-value: 2.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDAPKLAGIQEFQDkrSKPTDIFAIGFEEmvelnagnivsaSTTNQKLWA 651
Cdd:cd09091      1 ISIFIGTWNMGSAPPPKNI-------TSWFTSKGQGKTRDDVAD--YIPHDIYVIGTQE------------DPLGEKEWL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  652 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 729
Cdd:cd09091     60 DLLRHSLKEltSLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  730 AAGQSQVKERNEDFIEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKELI---RQQNWDSLIAGDQLIN 801
Cdd:cd09091    140 TSGSEKKLRRNQNYLNILRFLSLgdkKLSAFNITHrfTHLFWLGDLNYRLDLPIQEAENIIqkiEQQQFEPLLRHDQLNL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  802 QKNAGQVFRGFLEGKVTFAPTYKYDLFSDDY-------DTSEKCRTPAWTDRVLWrrrkwpfdRSAEDLDLLNASFQDES 874
Cdd:cd09091    220 EREEHKVFLRFSEEEITFPPTYRYERGSRDTyaytkqkATGVKYNLPSWCDRILW--------KSYPETHIICQSYGCTD 291
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2462583457  875 KILytwtpgtllhygraelkTSDHRPVVALIDI 907
Cdd:cd09091    292 DIV-----------------TSDHSPVFGTFEV 307
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
572-850 4.23e-39

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol 5-phosphatase-2 and related proteins; This subfamily contains the INPP5c domain of SHIP2 (SH2 domain containing inositol 5-phosphatase-2, also called INPPL1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP2 catalyzes the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. SHIP2 is an inhibitor of the insulin signaling pathway. It is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. Its interacting partners include filamin/actin, p130Cas, Shc, Vinexin, Interesectin 1, and c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1). A large variety of extracellular stimuli appear to lead to the tyrosine phosphorylation of SHIP2, including epidermal growth factor (EGF), platelet-derived growth factor (PDGF), insulin, macrophage colony-stimulating factor (M-CSF) and hepatocyte growth factor (HGF). SHIP2 is localized to the cytosol in quiescent cells; following growth factor stimulation and /or cell adhesion, it relocalizes to membrane ruffles. In addition to this INPP5c domain, SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate for conferring a predisposition for type 2 diabetes; it has been suggested that suppression of SHIP2 may be of benefit in the treatment of obesity and thereby prevent type 2 diabetes. SHIP2 and SHIP1 have little overlap in their in vivo functions.


Pssm-ID: 197335  Cd Length: 304  Bit Score: 148.20  E-value: 4.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  572 IRVCVGTWNVNGGKQFRSiafknqtLTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivsaSTTNQKL 649
Cdd:cd09101      1 ISIFIGTWNMGSVPPPKS-------LASWLTSR----GLGKTLDETTVtiPHDIYVFGTQE------------NSVGDRE 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  650 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 727
Cdd:cd09101     58 WVDFLRASLKEltDIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNC 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  728 HFAAGQSQVKERNEDFIEIARKLSFPMGR-------MLFSHdyVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLI 800
Cdd:cd09101    138 HLTSGNEKTHRRNQNYLDILRSLSLGDKQlnafdisLRFTH--LFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLN 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  801 NQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRT-------PAWTDRVLWR 850
Cdd:cd09101    216 LEREKNKVFLRFREEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILWK 272
RRM_SYNJ cd12440
RNA recognition motif (RRM) found in synaptojanin-1, synaptojanin-2 and similar proteins; This ...
932-1008 1.69e-34

RNA recognition motif (RRM) found in synaptojanin-1, synaptojanin-2 and similar proteins; This subfamily corresponds to the RRM of two active phosphatidylinositol phosphate phosphatases, synaptojanin-1 and synaptojanin-2. They have different interaction partners and are likely to have different biological functions. Synaptojanin-1 was originally identified as one of the major Grb2-binding proteins that may participate in synaptic vesicle endocytosis. It also acts as a Src homology 3 (SH3) domain-binding brain-specific inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Synaptojanin-2 is a ubiquitously expressed homolog of synaptojanin-1. It is a novel Rac1 effector regulating the early step of clathrin-mediated endocytosis. Synaptojanin-2 directly and specifically interacts with Rac1 in a GTP-dependent manner. It mediates the inhibitory effect of Rac1 on endocytosis and plays an important role in the Rac1-mediated control of cell growth. Both, synaptojanin-1 and synaptojanin-2, have two tissue-specific alternative splicing isoforms, a shorter isoform expressed in brain and a longer isoform in peripheral tissues. Synaptojanin-1 contains an N-terminal domain homologous to the cytoplasmic portion of the yeast protein Sac1p, a central inositol 5-phosphatase domain followed by a putative RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal proline-rich region mediating the binding of synaptojanin-1 to various SH3 domain-containing proteins including amphiphysin, SH3p4, SH3p8, SH3p13, and Grb2. Synaptojanin-2 shows high sequence homology to the N-terminal Sac1p homology domain, the central inositol 5-phosphatase domain, the putative RNA recognition motif (RRM) of synaptojanin-1, but differs in the proline-rich region.


Pssm-ID: 409874 [Multi-domain]  Cd Length: 77  Bit Score: 126.77  E-value: 1.69e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  932 DGTVLVSIKSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITIALK 1008
Cdd:cd12440      1 DATVVVSLDSKSEEWNEFEDALIGELLRVLASYGDVVLVRFAHEGMLVTFRDGRSALAALALNGKQILGRTLKIRLK 77
RRM_SYNJ2 cd12720
RNA recognition motif (RRM) found in synaptojanin-2 and similar proteins; This subgroup ...
932-1005 2.50e-13

RNA recognition motif (RRM) found in synaptojanin-2 and similar proteins; This subgroup corresponds to the RRM of synaptojanin-2, also termed synaptic inositol-1,4,5-trisphosphate 5-phosphatase 2, an ubiquitously expressed central regulatory enzyme in the phosphoinositide-signaling cascade. As a novel Rac1 effector regulating the early step of clathrin-mediated endocytosis, synaptojanin-2 acts as a polyphosphoinositide phosphatase directly and specifically interacting with Rac1 in a GTP-dependent manner. It mediates the inhibitory effect of Rac1 on endocytosis and plays an important role in the Rac1-mediated control of cell growth. Synaptojanin-2 shows high sequence homology to the N-terminal Sac1p homology domain, the central inositol 5-phosphatase domain, the putative RNA recognition motif (RRM) of synaptojanin-1, but differs in the proline-rich region.


Pssm-ID: 410119 [Multi-domain]  Cd Length: 78  Bit Score: 66.34  E-value: 2.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583457  932 DGTVLVSIKS-SLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITI 1005
Cdd:cd12720      1 DATVVVNLLSpTLEEKNDFPEDLSTELVQCFQSYGTVILVRFNRGQMLVTFEDSRSALRVLDLDGIKVNGRAVKI 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
1093-1301 1.21e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.42  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1093 PTISEGPV-PSLPIRPSRAPS----RTPGPPSAQSSPidAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPP 1167
Cdd:PHA03247  2742 PAVPAGPAtPGGPARPARPPTtagpPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP 2819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1168 PSGARSPAPTRKEFGAPKSPGTTRkdniGRSQPS-PQAGLAGPG-------PAGYSTARPTIP--PRAGVISAPQSHARA 1237
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPP----GPPPPSlPLGGSVAPGgdvrrrpPSRSPAAKPAAParPPVRRLARPAVSRST 2895
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457 1238 SAGRLTPESQSKTSETSkgstfLPEPLKPQAAFPPQSSL---PPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQ-----APPPPQPQPQPPPPPQPqppPPPPPRPQPPLAPTTDPAGAGEPSG 2957
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1049-1329 1.22e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 62.86  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1049 DMEGDVDDySAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPSAQSSPID-- 1126
Cdd:pfam03154  153 DNESDSDS-SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTli 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1127 AQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTR------KEFGAPKSPGTTRKDNIGRSQP 1200
Cdd:pfam03154  232 QQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQtgpshmQHPVPPQPFPLTPQSSQSQVPP 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1201 SPQAGLAGPG------PAGYSTARPTIPPRAGVIS-APQSHARASAGRLTPESQSKTSETSKG-------STF-----LP 1261
Cdd:pfam03154  312 GPSPAAPGQSqqrihtPPSQSQLQSQQPPREQPLPpAPLSMPHIKPPPTTPIPQLPNPQSHKHpphlsgpSPFqmnsnLP 391
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462583457 1262 EP--LKPQAAFP---PQSSLPPPAQrlqepLVPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQQ 1329
Cdd:pfam03154  392 PPpaLKPLSSLSthhPPSAHPPPLQ-----LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQ 459
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1106-1301 3.47e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 61.54  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1106 RPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTRKEFGAPK 1185
Cdd:PRK07764   592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1186 SPGttrkDNIGRSQPSPQAGLAGPGPAGYSTARPTiPPRAGVISAPQSHARASAGRLTPESQSKTSETSKGSTFLP-EPL 1264
Cdd:PRK07764   672 KAG----GAAPAAPPPAPAPAAPAAPAGAAPAQPA-PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPpEPD 746
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462583457 1265 KPQAAFPPQSSlPPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PRK07764   747 DPPDPAGAPAQ-PPPPPAPAPAAAPAAAPPPSPPSEE 782
PHA03247 PHA03247
large tegument protein UL36; Provisional
1098-1332 6.40e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.11  E-value: 6.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1098 GPVPSLPIRPsrAPSRTPGPPsaqssPIDAQPATPLP-------QKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSG 1170
Cdd:PHA03247  2693 GSLTSLADPP--PPPPTPEPA-----PHALVSATPLPpgpaaarQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1171 ARSPAPTRKEFGAPKS----PGTTRKDNIGRSQPSPQ------AGLAGPGPAGYSTARP--TIPPRAGVISAPQSHARAS 1238
Cdd:PHA03247  2766 PPAPAPPAAPAAGPPRrltrPAVASLSESRESLPSPWdpadppAAVLAPAAALPPAASPagPLPPPTSAQPTAPPPPPGP 2845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1239 agrlTPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAA-PMPQSGPQPNLETPPQPPPRSRSSH 1317
Cdd:PHA03247  2846 ----PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTeSFALPPDQPERPPQPQAPPPPQPQP 2921
                          250
                   ....*....|....*
gi 2462583457 1318 SLPSEASSQPQQEQP 1332
Cdd:PHA03247  2922 QPPPPPQPQPPPPPP 2936
PHA03378 PHA03378
EBNA-3B; Provisional
1011-1300 1.45e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 59.31  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1011 DWIKNLEEEMSLEKISIALPSSTSSTLLGEDAEVA--ADFDMEGDvddysaEVEELLPQHLQPSSSSGLGTSPSSSPRts 1088
Cdd:PHA03378   507 DLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPCVytEDLDIESD------EPASTEPVHDQLLPAPGLGPLQIQPLT-- 578
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1089 pcqSPTISE--GPVPSLPIRPSRA--PSRTPGPPSAQSSPidaqPATPLPQKDPaqplepkrppPPRPVAPPTRPAPPQR 1164
Cdd:PHA03378   579 ---SPTTSQlaSSAPSYAQTPWPVphPSQTPEPPTTQSHI----PETSAPRQWP----------MPLRPIPMRPLRMQPI 641
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1165 PPPPSGARSPAPTRKEFGAPKSPGTTRKDNI-------------------GRSQPSPQAGLAGPGPAGYSTARPtiPPRA 1225
Cdd:PHA03378   642 TFNVLVFPTPHQPPQVEITPYKPTWTQIGHIpyqpsptgantmlpiqwapGTMQPPPRAPTPMRPPAAPPGRAQ--RPAA 719
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1226 GVISAPQSHA--------RASAGRLTPESQSKTSETSKGSTflPEPLKPQAAFP------PQSSLPP-PAQRlqeplvPV 1290
Cdd:PHA03378   720 ATGRARPPAAapgrarppAAAPGRARPPAAAPGRARPPAAA--PGRARPPAAAPgaptpqPPPQAPPaPQQR------PR 791
                          330
                   ....*....|
gi 2462583457 1291 AAPMPQSGPQ 1300
Cdd:PHA03378   792 GAPTPQPPPQ 801
PHA03247 PHA03247
large tegument protein UL36; Provisional
1093-1334 3.39e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1093 PTISEGPVPSLP-IRPSRAPSRTPGPPSAQSSPidAQPATPLPqKDPAqplepkrppppRPVAPPTRPAPPQRPPPPSGA 1171
Cdd:PHA03247  2761 PTTAGPPAPAPPaAPAAGPPRRLTRPAVASLSE--SRESLPSP-WDPA-----------DPPAAVLAPAAALPPAASPAG 2826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1172 RSPAPTRkefGAPKSPGTTRkdniGRSQPS-PQAGLAGPG-------PAGYSTARPTIP--PRAGVISAPQSHARASAGR 1241
Cdd:PHA03247  2827 PLPPPTS---AQPTAPPPPP----GPPPPSlPLGGSVAPGgdvrrrpPSRSPAAKPAAParPPVRRLARPAVSRSTESFA 2899
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1242 LTPESQSKTSETSkgstfLPEPLKPQAAFPPQSSL---PPPAQRLQEPLVPVAAPMPQSGPQPN--------LETPPQPP 1310
Cdd:PHA03247  2900 LPPDQPERPPQPQ-----APPPPQPQPQPPPPPQPqppPPPPPRPQPPLAPTTDPAGAGEPSGAvpqpwlgaLVPGRVAV 2974
                          250       260
                   ....*....|....*....|....
gi 2462583457 1311 PRSRSSHSLPSEASSQPQQEQPSG 1334
Cdd:PHA03247  2975 PRFRVPQPAPSREAPASSTPPLTG 2998
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
679-776 5.14e-07

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


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 52.48  E-value: 5.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  679 VFIRPqhaPFIRDVAVDTVKTGMGgATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERnedFIEIARKLSFPMGRML 758
Cdd:cd08372     71 ILSKT---PKFKIVEKHQYKFGEG-DSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVR---DAQLKEVLEFLKRLRQ 143
                           90
                   ....*....|....*...
gi 2462583457  759 FSHDYVFWCGDFNYRIDL 776
Cdd:cd08372    144 PNSAPVVICGDFNVRPSE 161
PHA03247 PHA03247
large tegument protein UL36; Provisional
1100-1321 1.04e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1100 VPSLPIRPsRAPSRTPGPPSAQSSPIDAQPATPLPqkDPAqplepkrpppprpvapptrpappqrPPPPSGARSPAPTRK 1179
Cdd:PHA03247  2591 APPQSARP-RAPVDDRGDPRGPAPPSPLPPDTHAP--DPP-------------------------PPSPSPAANEPDPHP 2642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1180 EFGAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYST--------ARPTI--------PPRAGVISAPQSHARASAGRLT 1243
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPpqrprrraARPTVgsltsladPPPPPPTPEPAPHALVSATPLP 2722
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583457 1244 PESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQE-PLVPVAAPMPQSGPQPNLeTPPQPPPRSRSSHSLPS 1321
Cdd:PHA03247  2723 PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGPPRRL-TRPAVASLSESRESLPS 2800
PHA03247 PHA03247
large tegument protein UL36; Provisional
1071-1301 1.85e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1071 PSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRApsRTPGPPSAQSSPID-----AQPATPLPQKDPAQPLEPK 1145
Cdd:PHA03247  2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA--RRLGRAAQASSPPQrprrrAARPTVGSLTSLADPPPPP 2705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1146 RPPPprpvapptrpappqrppppsgarsPAPTRKEFGAPKSPGTTRKDniGRSQPSPQAGLAGPGPAGYST-ARPTIPPR 1224
Cdd:PHA03247  2706 PTPE------------------------PAPHALVSATPLPPGPAAAR--QASPALPAAPAPPAVPAGPATpGGPARPAR 2759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1225 AGVISAPQSHA--RASAG----RLTPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSG 1298
Cdd:PHA03247  2760 PPTTAGPPAPAppAAPAAgpprRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                   ...
gi 2462583457 1299 PQP 1301
Cdd:PHA03247  2840 PPP 2842
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1169-1302 2.88e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1169 SGARSPAPTRKEFGAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTiPPRAGVISAPQSHARASAGRLTPESQS 1248
Cdd:PHA03307   795 AFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPP-PARSSESSKSKPAAAGGRARGKNGRRR 873
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462583457 1249 KTSETSKGSTFLPEPLKPQAAFPPQsslPPPAQRLQEPLVPVAAPMPQSGPQPN 1302
Cdd:PHA03307   874 PRPPEPRARPGAAAPPKAAAAAPPA---GAPAPRPRPAPRVKLGPMPPGGPDPR 924
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1030-1302 3.50e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1030 PSSTSSTLLGEDAEVAADFDMEGDVDDYSAEVEEllpqhlQPSSSSGLGTSPSSSPRTSPCQSPtisegPVPSLPIRPSr 1109
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS------DAASSRQAALPLSSPEETARAPSS-----PPAEPPPSTP- 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1110 aPSRTPGPPSAQSSPI--DAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTRKEFGAPKSP 1187
Cdd:PHA03307   199 -PAAASPRPPRRSSPIsaSASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1188 GTTRKdnigrSQPSPQAGLAGPGPagystarPTIPPRAGVISAPQSH-ARASAGRLTPESQSKTSETSKGSTFLPEPLKP 1266
Cdd:PHA03307   278 PSSRP-----GPASSSSSPRERSP-------SPSPSSPGSGPAPSSPrASSSSSSSRESSSSSTSSSSESSRGAAVSPGP 345
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462583457 1267 QAAFPPQSSLPPPaqrlqeplvPVAAPMPQSGPQPN 1302
Cdd:PHA03307   346 SPSRSPSPSRPPP---------PADPSSPRKRPRPS 372
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
1092-1333 3.80e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 51.11  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1092 SPTISEGPVPSLPIR---------PSRAPSRTP----GPPS-AQSSPIDAQPATPLPQKDPAqpLEPKRPPPPRPVAPPT 1157
Cdd:pfam17823   99 EPATREGAADGAASRalaaaasssPSSAAQSLPaaiaALPSeAFSAPRAAACRANASAAPRA--AIAAASAPHAASPAPR 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1158 RPAPPQRPPPPSGARSPAPTRkefGAPKSPGTtrkdnIGRSQPSPQAGLAGPGPA-GYSTAR-PTIPPRAG-VISAPQSH 1234
Cdd:pfam17823  177 TAASSTTAASSTTAASSAPTT---AASSAPAT-----LTPARGISTAATATGHPAaGTALAAvGNSSPAAGtVTAAVGTV 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1235 ARASAGRLTPESQSKTSETSKGSTFLPEP--LKPQAAFPPQSS----LPPPAQRLQEPLV------PVAAPMPQSGPQPN 1302
Cdd:pfam17823  249 TPAALATLAAAAGTVASAAGTINMGDPHArrLSPAKHMPSDTMarnpAAPMGAQAQGPIIqvstdqPVHNTAGEPTPSPS 328
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462583457 1303 LETPPQPPPRSRSSHSLPSEASSQPQQEQPS 1333
Cdd:pfam17823  329 NTTLEPNTPKSVASTNLAVVTTTKAQAKEPS 359
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1057-1334 4.09e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 51.62  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1057 YSAEVEELLPQHLQPSSSSGLgtspsssprtspcQSPTISEGPVPSlPIRPSraPSRTPGPPSAQSSPIDAQPATPL--P 1134
Cdd:PRK10263   333 WAAPVEPVTQTPPVASVDVPP-------------AQPTVAWQPVPG-PQTGE--PVIAPAPEGYPQQSQYAQPAVQYneP 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1135 QKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTRKEFGAPKSPgtTRKDNIGRSQPSPQAGLAGPGPAG- 1213
Cdd:PRK10263   397 LQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQA--EEQQSTFAPQSTYQTEQTYQQPAAq 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1214 --YSTARPTIPPRAGVISAPQSH----ARASAGRLTPESQSKTSETSKGSTF---LPEPLKpqAAFPPQSSLPPPAQRLQ 1284
Cdd:PRK10263   475 epLYQQPQPVEQQPVVEPEPVVEetkpARPPLYYFEEVEEKRAREREQLAAWyqpIPEPVK--EPEPIKSSLKAPSVAAV 552
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462583457 1285 EPLVPVAAPMP-QSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQQEQPSG 1334
Cdd:PRK10263   553 PPVEAAAAVSPlASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIG 603
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1099-1333 1.49e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.77  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1099 PVPSLPIRPSRAPS-RTPGPP---SAQSSPIDAQ-PATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARS 1173
Cdd:pfam03154  257 PPSQVSPQPLPQPSlHGQMPPmphSLQTGPSHMQhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1174 PAPTRKEFGAP--------KSPGTTRKDNIgrsqPSPQAG-----LAGPGPAGYSTARPTiPPRAGVISAPQSHARASAG 1240
Cdd:pfam03154  337 QQPPREQPLPPaplsmphiKPPPTTPIPQL----PNPQSHkhpphLSGPSPFQMNSNLPP-PPALKPLSSLSTHHPPSAH 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1241 ----RLTPESQSktsetskgstFLPEPLKP------QAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNLETPPQPP 1310
Cdd:pfam03154  412 ppplQLMPQSQQ----------LPPPPAQPpvltqsQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGP 481
                          250       260
                   ....*....|....*....|...
gi 2462583457 1311 PrsrsshslPSEASSQPQQEQPS 1333
Cdd:pfam03154  482 P--------TSTSSAMPGIQPPS 496
PHA02682 PHA02682
ORF080 virion core protein; Provisional
1199-1299 1.67e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 48.32  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1199 QPSPQAGLAgPGPAgYSTARPTIPPRAGVISAPQSHARASAgrltPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPP 1278
Cdd:PHA02682    75 RPSGQSPLA-PSPA-CAAPAPACPACAPAAPAPAVTCPAPA----PACPPATAPTCPPPAVCPAPARPAPACPPSTRQCP 148
                           90       100
                   ....*....|....*....|.
gi 2462583457 1279 PAqrlqePLVPVAAPMPQSGP 1299
Cdd:PHA02682   149 PA-----PPLPTPKPAPAAKP 164
PTZ00249 PTZ00249
variable surface protein Vir28; Provisional
1169-1330 2.14e-05

variable surface protein Vir28; Provisional


Pssm-ID: 140276 [Multi-domain]  Cd Length: 516  Bit Score: 48.87  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1169 SGARSPaPTRKEFGAPKS----PGTTRKDNiGRSQPSPQAGLAGPGPagystarpTIPPRagVISAPQSHA--RASAGRL 1242
Cdd:PTZ00249   234 SGEARP-PKHISFSSPHAhgrpPVETRPPN-PVSVSSPQAHGRHPGE--------THTPP--LVTVPSSKAhdRNPVQTP 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1243 TPESQSKTSETSKGstflpepLKPQAAFPPQSSLPPPAQRLQEPLvPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSE 1322
Cdd:PTZ00249   302 TPTSVSGYSSQAKG-------LEKQAGGESERTSSVPSEQFPLPL-PVLLPLGQSGPLESSESEETDEYAGPKGLPEPEL 373

                   ....*...
gi 2462583457 1323 ASSQPQQE 1330
Cdd:PTZ00249   374 ELVELQEE 381
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1066-1301 3.60e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 48.22  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1066 PQHLQPSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPSAQSSP-IDAQPATPLPQ-------KD 1137
Cdd:pfam03154  295 PQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhIKPPPTTPIPQlpnpqshKH 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1138 PAQPLEPK--RPPPPRPVAPPTRPAPPQRPPPPSGARSPA----PTRKEFGAP--KSPGTTRKDNI---GRSQPSPQAGL 1206
Cdd:pfam03154  375 PPHLSGPSpfQMNSNLPPPPALKPLSSLSTHHPPSAHPPPlqlmPQSQQLPPPpaQPPVLTQSQSLpppAASHPPTSGLH 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1207 AGPGPAGYSTaRPTIPPRAGVISAPqSHARASAGRLTPESQSKTSETSKGStfLPEPLKPQAAFPPQSSLPPPAQRLQEP 1286
Cdd:pfam03154  455 QVPSQSPFPQ-HPFVPGGPPPITPP-SGPPTSTSSAMPGIQPPSSASVSSS--GPVPAAVSCPLPPVQIKEEALDEAEEP 530
                          250
                   ....*....|....*
gi 2462583457 1287 LVPvaaPMPQSGPQP 1301
Cdd:pfam03154  531 ESP---PPPPRSPSP 542
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1098-1301 5.40e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 5.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1098 GPVPSLPIRPSRAPSRTPGPPSAQSSPI--DAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPA 1175
Cdd:PHA03307   186 PSSPPAEPPPSTPPAAASPRPPRRSSPIsaSASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITL 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1176 PTRKEFGAPKSPGTTRK--------DNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSHARASAGRLTPESQ 1247
Cdd:PHA03307   266 PTRIWEASGWNGPSSRPgpasssssPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP 345
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462583457 1248 S-----KTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPM--PQSGPQP 1301
Cdd:PHA03307   346 SpsrspSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRarRRDATGR 406
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
716-901 6.60e-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: 46.69  E-value: 6.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  716 LFHTTSLCFVCSHFAAGQSQVKERNEDFIeIARKLSFPMGRMLFshdYVFwcGDFNYRIDL------------------- 776
Cdd:cd09092    176 LFHDASNLAACESSPSVYSQNRHRALGYV-LERLTDERFEKVPF---FVF--GDFNFRLDTksvvetlcakatmqtvrka 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  777 -PNEEVKELIRQQNWD----------SLIAGDQLINQKNAGQVFRGF-----------LEGKVTFAPTYKYdlfSDDYDT 834
Cdd:cd09092    250 dSNIVVKLEFREKDNDnkvvlqiekkKFDYFNQDVFRDNNGKALLKFdkelevfkdvlYELDISFPPSYPY---SEDPEQ 326
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457  835 SE---KCRTPAWTDRVLwrrrkwpFDRSAEDLDLLNasfqDESKILYTwtpgtllHYGRaELKTSDHRPV 901
Cdd:cd09092    327 GTqymNTRCPAWCDRIL-------MSHSARELKSEN----EEKSVTYD-------MIGP-NVCMGDHKPV 377
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1196-1302 8.22e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1196 GRSQPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSHARASAGRLTPE-SQSKTSETSKGSTFLPEPlKPQAAFPPQS 1274
Cdd:PRK07764   400 SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPaGGAPSPPPAAAPSAQPAP-APAAAPEPTA 478
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462583457 1275 SLPPPAQRLQEPLVPVAAPM---PQSGPQPN 1302
Cdd:PRK07764   479 APAPAPPAAPAPAAAPAAPAapaAPAGADDA 509
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1104-1301 1.09e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1104 PIRPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAqplepkrpppprPVAPPTRPAPPQRPPPPSGARSPAPTRKEFGA 1183
Cdd:PRK12323   374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAA------------PAAAAAARAVAAAPARRSPAPEALAAARQASA 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1184 PKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRAgvisAPQSHARASAGRLTPesqsktSETSKGSTFLPEP 1263
Cdd:PRK12323   442 RGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARA----APAAAPAPADDDPPP------WEELPPEFASPAP 511
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462583457 1264 LKPQAAFPP--QSSLPPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PRK12323   512 AQPDAAPAGwvAESIPDPATADPDDAFETLAPAPAAAPAP 551
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
947-1005 1.98e-04

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


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 41.11  E-value: 1.98e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  947 NFFDDALIDELLQQFASFGEVILIRFVEDKM-------WVTFLEGSSALNVLS-LNGKELLNRTITI 1005
Cdd:cd00590      5 NLPPDTTEEDLRELFSKFGEVVSVRIVRDRDgkskgfaFVEFESPEDAEKALEaLNGTELGGRPLKV 71
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1169-1301 2.70e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1169 SGARSPAPTRKEFGAPKSPGTTRKDNIGRsQPSPqAGLAGPGPAGYSTARPTIPPRagvisaPQSHARASAGRLTPESQS 1248
Cdd:PTZ00449   531 EGEHEDSKESDEPKEGGKPGETKEGEVGK-KPGP-AKEHKPSKIPTLSKKPEFPKD------PKHPKDPEEPKKPKRPRS 602
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583457 1249 KTSETSKGSTFLPEPLK-PQAAFPPQSSL----PPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PTZ00449   603 AQRPTRPKSPKLPELLDiPKSPKRPESPKspkrPPPPQRPSSPERPEGPKIIKSPKPP 660
RRM3_Prp24 cd12298
RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar ...
954-1007 3.40e-04

RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins; This subfamily corresponds to the RRM3 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation.


Pssm-ID: 409739 [Multi-domain]  Cd Length: 78  Bit Score: 40.32  E-value: 3.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583457  954 IDELLQQFASFGEV---ILIRFVEDKM--------WVTFLEGSSALNVLSLNGKELLNRTITIAL 1007
Cdd:cd12298     14 EEALRGIFEKFGEIesiNIPKKQKNRKgrhnngfaFVTFEDADSAESALQLNGTLLDNRKISVSL 78
PHA03379 PHA03379
EBNA-3A; Provisional
1066-1301 4.16e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 45.05  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1066 PQHLQPSSSSGLGTSPSSSPRTSPCQSP-----TISEGPVPSL---PIRPSRAPSRTPGPPSaqsspiDAQPAtPLPQKD 1137
Cdd:PHA03379   428 PQSLETATSHGSAQVPEPPPVHDLEPGPlhdqhSMAPCPVAQLppgPLQDLEPGDQLPGVVQ------DGRPA-CAPVPA 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1138 PAqplepkrpppprpvapPTRPAPPQRPPPPSGARSPAPTRKEF--GAPKSPGTTRKDNIGRSQPsPQAGLAGPG-PAGY 1214
Cdd:PHA03379   501 PA----------------GPIVRPWEASLSQVPGVAFAPVMPQPmpVEPVPVPTVALERPVCPAP-PLIAMQGPGeTSGI 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1215 STAR---------PTiPPRagviSAPQSHARASAGRLTPESQSKTSETSKGSTFLPE---------PLKPQAAFPPQSSL 1276
Cdd:PHA03379   564 VRVRerwrpapwtPN-PPR----SPSQMSVRDRLARLRAEAQPYQASVEVQPPQLTQvspqqpmeyPLEPEQQMFPGSPF 638
                          250       260
                   ....*....|....*....|....*..
gi 2462583457 1277 PPPAQRLQEPLVPVAAPMPQSGP--QP 1301
Cdd:PHA03379   639 SQVADVMRAGGVPAMQPQYFDLPlqQP 665
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1202-1334 6.40e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.00  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1202 PQAGLAGPGPAGysTARPTIPPRAGVISAPQsharASAGRLTPESQSKTSETSKGSTflPEPLKPQAAFPPQSSLPPPAQ 1281
Cdd:PRK14971   363 TQKGDDASGGRG--PKQHIKPVFTQPAAAPQ----PSAAAAASPSPSQSSAAAQPSA--PQSATQPAGTPPTVSVDPPAA 434
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462583457 1282 rlqEPLVPVAAPMPQSGPQPNLETPPQPPPRSRSShSLPSEASSQPQQEQPSG 1334
Cdd:PRK14971   435 ---VPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSL-GPSTLRPIQEKAEQATG 483
PHA03378 PHA03378
EBNA-3B; Provisional
1100-1293 7.20e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1100 VPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAP--- 1176
Cdd:PHA03378   669 IGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARppa 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1177 -----TRKEFGAPkSPGTTRKDNIGRSQPSPQAGlAGPGPAGYSTARPT-IPPRAGVISAPQSHARASAGRLTPES---- 1246
Cdd:PHA03378   749 aapgrARPPAAAP-GRARPPAAAPGAPTPQPPPQ-APPAPQQRPRGAPTpQPPPQAGPTSMQLMPRAAPGQQGPTKqilr 826
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583457 1247 QSKTSETSKG--STFLPEPLKPQAAFPPQsslPPP-----AQRLQEPLV--PVAAP 1293
Cdd:PHA03378   827 QLLTGGVKRGrpSLKKPAALERQAAAGPT---PSPgsgtsDKIVQAPVFypPVLQP 879
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1171-1334 8.32e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 8.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1171 ARSPAPtrkefGAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSHARASAGRLTPESQSKT 1250
Cdd:PRK07003   357 AFEPAV-----TGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPA 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1251 SETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQQE 1330
Cdd:PRK07003   432 PPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDAR 511

                   ....
gi 2462583457 1331 QPSG 1334
Cdd:PRK07003   512 APAA 515
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1091-1301 1.06e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1091 QSPTISEGPVPSLPIRPSRAP----SRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPP 1166
Cdd:PHA03307    69 TGPPPGPGTEAPANESRSTPTwslsTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPP 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1167 PPSGARSPAPTRKEFGAPKSPGTTrKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSH---------ARA 1237
Cdd:PHA03307   149 AASPPAAGASPAAVASDAASSRQA-ALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISAsasspapapGRS 227
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583457 1238 SAGRLTPESQSKTSETSKGSTFLPEPLKPqAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PHA03307   228 AADDAGASSSDSSSSESSGCGWGPENECP-LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1196-1301 1.12e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1196 GRSQPSPQA-----GLAGPGPAGYSTARPTIPPRAGVISAPQSHARASAGRLTPE-SQSKTSETSKGSTFLPEPlKPQAA 1269
Cdd:PRK07764   395 AAAAPSAAAaapaaAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPaGGAPSPPPAAAPSAQPAP-APAAA 473
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462583457 1270 FPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQP 1301
Cdd:PRK07764   474 PEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAG 505
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1091-1301 1.53e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1091 QSPTISEGPVPSLPiRPSRAPSrtPGPPSAQSSPidaQPATPLPQKDPAqplepkrpppprpvapptrpappqrppppsg 1170
Cdd:NF033839   282 DTPKEPGNKKPSAP-KPGMQPS--PQPEKKEVKP---EPETPKPEVKPQ------------------------------- 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1171 ARSPAPTRKEfgAPKSPGTTRKDNIGRSQPSPQAGLAGPGPA---GYSTARPTIPPRAGViSAPQSHARASagrlTPESQ 1247
Cdd:NF033839   325 LEKPKPEVKP--QPEKPKPEVKPQLETPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQPET-PKPEVKPQPE----KPKPE 397
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462583457 1248 SKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPlvpvaAPMPQSGPQP 1301
Cdd:NF033839   398 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-----KPKPEVKPQP 446
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1095-1331 1.59e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1095 ISEGPVPSLPIRPSRAP--SRTPGPPSAQSSPIDaqPATPLPQKDPAQPLEPKRPppprpvapptrpappqrppppsgar 1172
Cdd:PTZ00449   557 VGKKPGPAKEHKPSKIPtlSKKPEFPKDPKHPKD--PEEPKKPKRPRSAQRPTRP------------------------- 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1173 sPAPTRKEFGA-PKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRA-GVISAPQSHARASAGRLTPESQSKT 1250
Cdd:PTZ00449   610 -KSPKLPELLDiPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSpKPPFDPKFKEKFYDDYLDAAAKSKE 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1251 SETS-----KGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNletppqppprsrsshslPSEASS 1325
Cdd:PTZ00449   689 TKTTvvldeSFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPD-----------------DIEFFT 751

                   ....*.
gi 2462583457 1326 QPQQEQ 1331
Cdd:PTZ00449   752 PPEEER 757
RRM smart00360
RNA recognition motif;
947-1005 1.80e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.80e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583457   947 NFFDDALIDELLQQFASFGEVILIRFVEDKMW--------VTFLEGSSALNVLS-LNGKELLNRTITI 1005
Cdd:smart00360    6 NLPPDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
1096-1234 3.16e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 40.06  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1096 SEGPVPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATP---------LPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPP 1166
Cdd:cd21975     27 GAGLAAGLDVRATREVAKGPGPPGPAWKPDGADSPGLvtaaphllaANVLAPLRGPSVEGSSLESGDADMGSDSDVAPAS 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583457 1167 PPSGARSPApTRKEFGAPKSPGttrkdnigrsqPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSH 1234
Cdd:cd21975    107 GAAASTSPE-SSSDAASSPSPL-----------SLLHPGEAGLEPERPRPRVRRGVRRRGVTPAAKRH 162
RRM2_SREK1 cd12260
RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 ...
955-1005 3.80e-03

RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins; This subfamily corresponds to the RRM2 of SREK1, also termed serine/arginine-rich-splicing regulatory protein 86-kDa (SRrp86), or splicing factor arginine/serine-rich 12 (SFRS12), or splicing regulatory protein 508 amino acid (SRrp508). SREK1 belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family), which is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. It is a unique SR family member and it may play a crucial role in determining tissue specific patterns of alternative splicing. SREK1 can alter splice site selection by both positively and negatively modulating the activity of other SR proteins. For instance, SREK1 can activate SRp20 and repress SC35 in a dose-dependent manner both in vitro and in vivo. In addition, SREK1 contains two (some contain only one) RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and two serine-arginine (SR)-rich domains (SR domains) separated by an unusual glutamic acid-lysine (EK) rich region. The RRM and SR domains are highly conserved among other members of the SR superfamily. However, the EK domain is unique to SREK1. It plays a modulatory role controlling SR domain function by involvement in the inhibition of both constitutive and alternative splicing and in the selection of splice-site.


Pssm-ID: 409705 [Multi-domain]  Cd Length: 85  Bit Score: 37.67  E-value: 3.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583457  955 DELLQQFASFGEVILIRFVEDK------MWVTFLEGSSALNVLSLNGKELLNRTITI 1005
Cdd:cd12260     19 DQLLEFFSQAGEVKYVRMAGDEtqptryAFVEFAEQTSVINALKLNGKMFGGRPLKV 75
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1169-1332 4.36e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1169 SGARSPAPTRKEFGAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPP-----------RAGVISAPQSHARA 1237
Cdd:PHA03307    73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPpspapdlsemlRPVGSPGPPPAASP 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1238 SAGRLTPESQSKTSETSKGSTFL--------PEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNLETPP-Q 1308
Cdd:PHA03307   153 PAAGASPAAVASDAASSRQAALPlsspeetaRAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADdA 232
                          170       180
                   ....*....|....*....|....
gi 2462583457 1309 PPPRSRSSHSLPSEASSQPQQEQP 1332
Cdd:PHA03307   233 GASSSDSSSSESSGCGWGPENECP 256
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1093-1237 4.90e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583457 1093 PTISEGPVPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPvapptrpAPPQRPPPPSGAR 1172
Cdd:PRK07764   386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPA-------GNAPAGGAPSPPP 458
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583457 1173 SPAPTRKEFGAPKSPGTTrkdnIGRSQPSPQAGLAGPGPAGystarptiPPRAGVISAPQSHARA 1237
Cdd:PRK07764   459 AAAPSAQPAPAPAAAPEP----TAAPAPAPPAAPAPAAAPA--------APAAPAAPAGADDAAT 511
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH