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Conserved domains on  [gi|256773218|ref|NP_001038980|]
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synaptojanin-1 isoform b [Mus musculus]

Protein Classification

INPP5c_Synj1 and RRM_SYNJ1 domain-containing protein( domain architecture ID 13429246)

protein containing domains COG5329, INPP5c_Synj1, RRM_SYNJ1, and PHA03378

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
533-868 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: 766.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 612
Cdd:cd09098     1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 692
Cdd:cd09098    81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  693 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 772
Cdd:cd09098   161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  773 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 852
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                         330
                  ....*....|....*.
gi 256773218  853 ELKTSDHRPVVALIDI 868
Cdd:cd09098   321 ELKTSDHRPVVALIDI 336
COG5329 super family cl34984
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
60-480 4.98e-94

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: 314.33  E-value: 4.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   60 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 130
Cdd:COG5329    61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  131 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 201
Cdd:COG5329   137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  202 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 281
Cdd:COG5329   216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  282 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 361
Cdd:COG5329   295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  362 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 439
Cdd:COG5329   374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256773218  440 YAGTGALEGKA----------KLKDGARSVTRTIQNNFFDSSKQEAIDVLL 480
Cdd:COG5329   451 YTGTGALKSSFtrrgrrsfagALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
867-1008 5.69e-63

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


The actual alignment was detected with superfamily member pfam08952:

Pssm-ID: 450164  Cd Length: 146  Bit Score: 210.82  E-value: 5.69e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   867 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 945
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256773218   946 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEM---SLEKISVTlpSSASSTLLGEDAEVAAD 1008
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIilcTDNTIPVS--PCANSTLLAEDFDFGSP 144
PHA03378 super family cl33729
EBNA-3B; Provisional
972-1276 8.54e-10

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 63.55  E-value: 8.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  972 DWIKHLEEEMSLEKISVTLPSSASSTLLGEDAEVA--ADFDMEGDvddysaEVEELLPQHLQPSSSSGLGTSPSSSPRts 1049
Cdd:PHA03378  507 DLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPCVytEDLDIESD------EPASTEPVHDQLLPAPGLGPLQIQPLT-- 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1050 pcqSPTVPEY--SAPSLPIRPSRA--PSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPP 1125
Cdd:PHA03378  579 ---SPTTSQLasSAPSYAQTPWPVphPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPP 655
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1126 PSGARSPAPARKEFGGVGAPPSPGVARREIEAPKSPGTArkdnigrnQPSPQAGLAGPGPAGY-GAARP--TIPARAGVI 1202
Cdd:PHA03378  656 QVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTM--------QPPPRAPTPMRPPAAPpGRAQRpaAATGRARPP 727
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218 1203 SAPQSQARVCAGRPTPDSQSKPSET-LKGPAVLPEPLKPQAAfpqQPSLPTPAQKLQDPLVPIAAPTMPPSgPQP 1276
Cdd:PHA03378  728 AAAPGRARPPAAAPGRARPPAAAPGrARPPAAAPGRARPPAA---APGAPTPQPPPQAPPAPQQRPRGAPT-PQP 798
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
533-868 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: 766.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 612
Cdd:cd09098     1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 692
Cdd:cd09098    81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  693 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 772
Cdd:cd09098   161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  773 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 852
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                         330
                  ....*....|....*.
gi 256773218  853 ELKTSDHRPVVALIDI 868
Cdd:cd09098   321 ELKTSDHRPVVALIDI 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
531-871 5.85e-129

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 399.04  E-value: 5.85e-129
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    531 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKL 610
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    611 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 690
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    691 AAGQSQVKERNEDFVEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 767
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    768 QIFRGFLEGKVTFAPTYKYDLF-SEDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 846
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 256773218    847 lHYGRAELKTSDHRPVVALIDIDIF 871
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
60-480 4.98e-94

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 314.33  E-value: 4.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   60 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 130
Cdd:COG5329    61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  131 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 201
Cdd:COG5329   137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  202 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 281
Cdd:COG5329   216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  282 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 361
Cdd:COG5329   295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  362 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 439
Cdd:COG5329   374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256773218  440 YAGTGALEGKA----------KLKDGARSVTRTIQNNFFDSSKQEAIDVLL 480
Cdd:COG5329   451 YTGTGALKSSFtrrgrrsfagALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
60-340 3.73e-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: 426748  Cd Length: 295  Bit Score: 285.24  E-value: 3.73e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    60 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISL---------RVDASDEDRI-SEVRKVLNSGNFY 129
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGGPIYKITDVEFIPLnsslydsssKSKSPDEARLlKLLKLFLSSGSFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   130 FAWSasgvsLDLS------LNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACL 203
Cdd:pfam02383   77 FSYD-----YDLTnslqrnSTTSRSPSFDSLDERFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   204 ISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDC-----VSSFIQIRGSVPLFWEQ-PGLQVGSHRVRMSRgFEA 277
Cdd:pfam02383  152 ISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTGnsegkIFSFVQIRGSIPLFWSQdPNLKYSKPKIQITR-PEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218   278 NAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKAS--EHASDIHMVSFDYHQMVK 340
Cdd:pfam02383  231 TQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEKAVKYLnqFLPDKLRYTAFDFHHECK 295
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
526-894 5.32e-70

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 242.77  E-value: 5.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  526 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVNA 603
Cdd:COG5411    23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  604 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 678
Cdd:COG5411    84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  679 HTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 756
Cdd:COG5411   163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  757 GDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 836
Cdd:COG5411   243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218  837 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIA--VQGPPDG 894
Cdd:COG5411   299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
867-1008 5.69e-63

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


Pssm-ID: 286093  Cd Length: 146  Bit Score: 210.82  E-value: 5.69e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   867 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 945
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256773218   946 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEM---SLEKISVTlpSSASSTLLGEDAEVAAD 1008
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIilcTDNTIPVS--PCANSTLLAEDFDFGSP 144
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
624-883 2.49e-50

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 189.35  E-value: 2.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  624 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 701
Cdd:PLN03191  363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  702 EDFVEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLE 775
Cdd:PLN03191  443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  776 GKVTFAPTYKYDLFSEDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 850
Cdd:PLN03191  523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                         250       260       270
                  ....*....|....*....|....*....|...
gi 256773218  851 RAELKTSDHRPVVALIDIdifEVEAEERQKIYK 883
Cdd:PLN03191  574 RSEIRLSDHRPVSSMFLV---EVEVFDHRKLQR 603
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
893-969 7.04e-39

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: 139.08  E-value: 7.04e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256773218  893 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 969
Cdd:cd12719     1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
PHA03378 PHA03378
EBNA-3B; Provisional
972-1276 8.54e-10

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 63.55  E-value: 8.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  972 DWIKHLEEEMSLEKISVTLPSSASSTLLGEDAEVA--ADFDMEGDvddysaEVEELLPQHLQPSSSSGLGTSPSSSPRts 1049
Cdd:PHA03378  507 DLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPCVytEDLDIESD------EPASTEPVHDQLLPAPGLGPLQIQPLT-- 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1050 pcqSPTVPEY--SAPSLPIRPSRA--PSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPP 1125
Cdd:PHA03378  579 ---SPTTSQLasSAPSYAQTPWPVphPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPP 655
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1126 PSGARSPAPARKEFGGVGAPPSPGVARREIEAPKSPGTArkdnigrnQPSPQAGLAGPGPAGY-GAARP--TIPARAGVI 1202
Cdd:PHA03378  656 QVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTM--------QPPPRAPTPMRPPAAPpGRAQRpaAATGRARPP 727
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218 1203 SAPQSQARVCAGRPTPDSQSKPSET-LKGPAVLPEPLKPQAAfpqQPSLPTPAQKLQDPLVPIAAPTMPPSgPQP 1276
Cdd:PHA03378  728 AAAPGRARPPAAAPGRARPPAAAPGrARPPAAAPGRARPPAA---APGAPTPQPPPQAPPAPQQRPRGAPT-PQP 798
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
1129-1268 1.78e-08

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 59.01  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1129 A------RSPAPArkefggVGAPPSPGVARREIEAPKSPGTarkdnigrnqPSPQAGLAGPGPAGYGAARPTIPARAGVI 1202
Cdd:pfam15685  400 AhpipgpRRPAPA------LLAPPMFIFPAPTNGEPVRPGP----------PAPQALLPRPPPPTPPATPPPVPPPIPQL 463
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218  1203 SAPQSQARVCAGRPTPDSQSKPSETLKGP---AVLPEPL------KPQAAFPQQPSlPTPAQKLQDPLVPIAAPT 1268
Cdd:pfam15685  464 PALQPMPLAAARPPTPRPCPGHGESALAPaptAPLPPALaadqapAPALAAAPAPS-PAPAPATADPLPPAPAPI 537
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1052-1277 3.63e-05

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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 47.84  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1052 QSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPpsgaRS 1131
Cdd:NF033839  285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQP----EK 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1132 PAPARK---EFGGVGAPPSPGVARREIEA-PKSPGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARagvisAPQS 1207
Cdd:NF033839  361 PKPEVKpqpEKPKPEVKPQPETPKPEVKPqPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV-----KPQP 435
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1208 qarvcagrPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQdplvpIAAPTMPPSGPQPN 1277
Cdd:NF033839  436 --------EKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQ-----PEKPKPDNSKPQAD 492
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1032-1280 2.10e-04

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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 45.53  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1032 PSSSSGLGTSPSSSPRtspcqSPTVPEYSAPSLPiRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPV 1111
Cdd:NF033839  147 SSSSSSSGSSTKPETP-----QPENPEHQKPTTP-APDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKH 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1112 APPARPAPPQRPPPPSGARSPAPARKEFGGvgapPSPGVarrEIEAPKSPGTARKDNIgrnQPSPQAGLAGPGPAGYGAA 1191
Cdd:NF033839  221 HLQKEKHRQIVALIKELDELKKQALSEIDN----VNTKV---EIENTVHKIFADMDAV---VTKFKKGLTQDTPKEPGNK 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1192 RPTIPaRAGVISAPQSQARVCAGRP-TPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQdplvpiaaPTMP 1270
Cdd:NF033839  291 KPSAP-KPGMQPSPQPEKKEVKPEPeTPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQ--------PEKP 361
                         250
                  ....*....|
gi 256773218 1271 PSGPQPNLET 1280
Cdd:NF033839  362 KPEVKPQPEK 371
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1131-1280 2.24e-04

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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 45.53  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1131 SPAPARKEFGGVGAPPSPGVaRREIEAPK--------SPGTARKDNIGRNQPSPQAGLAGPGPA---GYGAARPTIPARA 1199
Cdd:NF033839  302 SPQPEKKEVKPEPETPKPEV-KPQLEKPKpevkpqpeKPKPEVKPQLETPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQP 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1200 GvisAPQSQARVCAGRPTPDSQSKPsETLKgPAVLPEPLKPQAAFPQQPSLPTPAQKLQdPLVPIAAPTMPPSGPQPNL- 1278
Cdd:NF033839  381 E---TPKPEVKPQPEKPKPEVKPQP-EKPK-PEVKPQPEKPKPEVKPQPEKPKPEVKPQ-PEKPKPEVKPQPEKPKPEVk 454
                         170
                  ....*....|
gi 256773218 1279 --------ET 1280
Cdd:NF033839  455 pqpetpkpEV 464
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
1129-1275 8.28e-04

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225689 [Multi-domain]  Cd Length: 226  Bit Score: 42.57  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1129 ARSPAPARK-EFGGVGAPPSPGVARREIEApkspgtarkdnigrnQPSPQAGLAGPGPAGYGAArptiparagvisaPQS 1207
Cdd:COG3147    27 LDGKKKHRQdEVAAIPLPPKPQGDRDEPRV---------------LPAVVQVVALPTQPPEGVA-------------QEI 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256773218 1208 QARVCAGRPtpdsqSKPSETLKGPAVLPEPLKPQAAfPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQ 1275
Cdd:COG3147    79 QDAGDAAAA-----SVDPQPVAQPPVESTPAGVPVA-AQTPKPVKPPKQPPAGAVPAKPTPKPEPKPV 140
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1179-1279 1.24e-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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1179 GLAGPGPAGYGAARPTIPaRAGVISAPQSQARVCAGRP-TPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKL 1257
Cdd:NF033839  278 GLTQDTPKEPGNKKPSAP-KPGMQPSPQPEKKEVKPEPeTPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKP 356
                          90       100
                  ....*....|....*....|..
gi 256773218 1258 QdPLVPiaAPTMPPSGPQPNLE 1279
Cdd:NF033839  357 Q-PEKP--KPEVKPQPEKPKPE 375
RRM smart00360
RNA recognition motif;
911-966 1.41e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.41e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218    911 DDALIDELLRQFAHFGEVILIRFVEDKMW--------VTFLEGSSALNALS-LNGKELLNRTITI 966
Cdd:smart00360    9 PDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
1193-1278 2.14e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.16  E-value: 2.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   1193 PTIPARAGVIsaPQSQARVCAGRP--TPDSQSKPSetLKGPAvlPEPLKPQAAFPQQPSLPTPAQKLQDPLVPI----AA 1266
Cdd:smart00818   59 PVLPAQQPVV--PQQPLMPVPGQHsmTPTQHHQPN--LPQPA--QQPFQPQPLQPPQPQQPMQPQPPVHPIPPLppqpPL 132
                            90
                    ....*....|..
gi 256773218   1267 PTMPPSGPQPNL 1278
Cdd:smart00818  133 PPMFPMQPLPPL 144
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
533-868 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: 766.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 612
Cdd:cd09098     1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 692
Cdd:cd09098    81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  693 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 772
Cdd:cd09098   161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  773 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 852
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                         330
                  ....*....|....*.
gi 256773218  853 ELKTSDHRPVVALIDI 868
Cdd:cd09098   321 ELKTSDHRPVVALIDI 336
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
533-868 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: 685.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQ-EFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLW 611
Cdd:cd09089     1 LRVFVGTWNVNGGKHFRSIAFKHQSMTDWLLDNPKLAGQCsNDSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKEW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  612 AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFA 691
Cdd:cd09089    81 GEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  692 AGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFR 771
Cdd:cd09089   161 AGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  772 GFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDllnasfqdeSKILYTWTPGTLLHYGR 851
Cdd:cd09089   241 GFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPSDKTEESLV---------ETNDPTWNPGTLLYYGR 311
                         330
                  ....*....|....*..
gi 256773218  852 AELKTSDHRPVVALIDI 868
Cdd:cd09089   312 AELKTSDHRPVVAIIDI 328
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
533-868 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: 566.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 612
Cdd:cd09099     1 TRVAMGTWNVNGGKQFRSNILGTSELTDWLLDSPKLSGTPDFQDDESNPPDIFAVGFEEMVELSAGNIVNASTTNRKMWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 692
Cdd:cd09099    81 EQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  693 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 772
Cdd:cd09099   161 GQNQVKERNEDYKEITQKLSFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  773 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 852
Cdd:cd09099   241 FHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWRKKWPFEKTAGEINLLDSDLDFDTKIRHTWTPGALMYYGRA 320
                         330
                  ....*....|....*.
gi 256773218  853 ELKTSDHRPVVALIDI 868
Cdd:cd09099   321 ELQASDHRPVLAIVEV 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
531-871 5.85e-129

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


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 399.04  E-value: 5.85e-129
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    531 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKL 610
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    611 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 690
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    691 AAGQSQVKERNEDFVEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 767
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    768 QIFRGFLEGKVTFAPTYKYDLF-SEDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 846
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 256773218    847 lHYGRAELKTSDHRPVVALIDIDIF 871
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
533-868 1.06e-107

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: 341.62  E-value: 1.06e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLDAPklagiqefqdkrSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 612
Cdd:cd09074     1 VKIFVVTWNVGGGI------SPPENLENWLSPKG------------TEAPDIYAVGVQEVDMSVQGFVGNDDSAKAREWV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAV--DTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 690
Cdd:cd09074    63 DNIQEALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVegVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  691 AAGQSQVKERNEDFVEIARKLSFPMG----RMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNA 766
Cdd:cd09074   143 AAGQEEVERRNQDYRDILSKLKFYRGdpaiDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  767 GQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdeskilYTWTPGTL 846
Cdd:cd09074   223 GKVFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKS--------------------------KAGSEIQP 276
                         330       340
                  ....*....|....*....|...
gi 256773218  847 LHYGRAEL-KTSDHRPVVALIDI 868
Cdd:cd09074   277 LSYTSVPLyKTSDHKPVRATFRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
533-864 2.86e-105

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: 334.69  E-value: 2.86e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGgkqfrsiAFKNQTLTDWLldapklagiqeFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 612
Cdd:cd09090     1 INIFVGTFNVNG-------KSYKDDLSSWL-----------FPEENDELPDIVVIGLQEVVELTAGQILNSDPSKSSFWE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 690
Cdd:cd09090    63 KKIKTTLNGrgGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  691 AAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIF 770
Cdd:cd09090   143 AAGLTNYEERNNDYKTIARGLRFSRGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  771 RGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsAEDLDLLNasfqdeskilytwtpgtllhYG 850
Cdd:cd09090   223 PGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYR---------GENLRQLS--------------------YN 273
                         330
                  ....*....|....
gi 256773218  851 RAELKTSDHRPVVA 864
Cdd:cd09090   274 SAPLRFSDHRPVYA 287
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
533-868 3.51e-100

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: 320.80  E-value: 3.51e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKqfrsiafKNQTLTDWLldapklagiqefqDKRSKPTDIFAIGFEEmVELNAGNIVNASTTNQKLWA 612
Cdd:cd09093     1 FRIFVGTWNVNGQS-------PDESLRPWL-------------SCDEEPPDIYAIGFQE-LDLSAEAFLFNDSSREQEWV 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 692
Cdd:cd09093    60 KAVERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  693 GQSQVKERNEDFVEIARKLSFPMG----RMLFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQKNAG 767
Cdd:cd09093   140 HMEEVERRNQDYKDICARMKFEDPdgppLSISDHDVVFWLGDLNYRIqELPTEEVKELIEKNDLEELLKYDQLNIQRRAG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  768 QIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedldllnasfqdESKIlytwtpgTLL 847
Cdd:cd09093   220 KVFEGFTEGEINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWR----------------------GTNI-------VQL 270
                         330       340
                  ....*....|....*....|..
gi 256773218  848 HYGR-AELKTSDHRPVVALIDI 868
Cdd:cd09093   271 SYRShMELKTSDHKPVSALFDI 292
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
60-480 4.98e-94

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 314.33  E-value: 4.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   60 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 130
Cdd:COG5329    61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  131 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 201
Cdd:COG5329   137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  202 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 281
Cdd:COG5329   216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  282 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 361
Cdd:COG5329   295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  362 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 439
Cdd:COG5329   374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256773218  440 YAGTGALEGKA----------KLKDGARSVTRTIQNNFFDSSKQEAIDVLL 480
Cdd:COG5329   451 YTGTGALKSSFtrrgrrsfagALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
60-340 3.73e-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: 426748  Cd Length: 295  Bit Score: 285.24  E-value: 3.73e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218    60 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISL---------RVDASDEDRI-SEVRKVLNSGNFY 129
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGGPIYKITDVEFIPLnsslydsssKSKSPDEARLlKLLKLFLSSGSFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   130 FAWSasgvsLDLS------LNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACL 203
Cdd:pfam02383   77 FSYD-----YDLTnslqrnSTTSRSPSFDSLDERFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   204 ISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDC-----VSSFIQIRGSVPLFWEQ-PGLQVGSHRVRMSRgFEA 277
Cdd:pfam02383  152 ISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTGnsegkIFSFVQIRGSIPLFWSQdPNLKYSKPKIQITR-PEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218   278 NAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKAS--EHASDIHMVSFDYHQMVK 340
Cdd:pfam02383  231 TQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEKAVKYLnqFLPDKLRYTAFDFHHECK 295
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
534-868 6.67e-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: 6.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  534 RVCVGTWNVnggkqfrSIAFKNQTLTdwlldapKLAGIQEFQDKrskpTDIFAIGFEEmvelnagniVNASTTNQKL--- 610
Cdd:cd09094     2 RVYVVTWNV-------ATAPPPIDVR-------SLLGLQSPEVA----PDIYIIGLQE---------VNSKPVQFVSdli 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  611 ----WAvELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFV 686
Cdd:cd09094    55 fddpWS-DLFMDILSPKGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  687 CSHFAAGQSQVKERNEDFVEIARKLSFPMGRM--LFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQ 763
Cdd:cd09094   134 NCHLPAHMEKWEQRIDDFETILSTQVFNECNTpsILDHDYVFWFGDLNFRIeDVSIEFVRELVNSKKYHLLLEKDQLNMA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  764 KNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedLDLLNASFQDESKIlytwtp 843
Cdd:cd09094   214 KRKEEAFQGFQEGPLNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWK------------VNPDASTEEKFLSI------ 275
                         330       340
                  ....*....|....*....|....*.
gi 256773218  844 gTLLHY-GRAELKTSDHRPVVALIDI 868
Cdd:cd09094   276 -TQTSYkSHMEYGISDHKPVTAQFRL 300
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
526-894 5.32e-70

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 242.77  E-value: 5.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  526 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVNA 603
Cdd:COG5411    23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  604 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 678
Cdd:COG5411    84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  679 HTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 756
Cdd:COG5411   163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  757 GDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 836
Cdd:COG5411   243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218  837 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIA--VQGPPDG 894
Cdd:COG5411   299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
867-1008 5.69e-63

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


Pssm-ID: 286093  Cd Length: 146  Bit Score: 210.82  E-value: 5.69e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   867 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 945
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256773218   946 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEM---SLEKISVTlpSSASSTLLGEDAEVAAD 1008
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIilcTDNTIPVS--PCANSTLLAEDFDFGSP 144
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
531-868 6.92e-57

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


Pssm-ID: 197329  Cd Length: 298  Bit Score: 199.19  E-value: 6.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  531 KKIRVCVGTWNVNGGKQFrsiafkNQTLTDWLLdapklAGIQEFQdkrskpTDIFAIGFEEmvelnagnivnaSTTNQKL 610
Cdd:cd09095     3 RNVGIFVATWNMQGQKEL------PENLDDFLL-----PTSADFA------QDIYVIGVQE------------GCSDRRE 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  611 WAVELQKTISrdNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 690
Cdd:cd09095    54 WEIRLQETLG--PSHVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  691 AAGQSQVKERNEDFVEIARKLSFPmgRMLFSHDY-------------VFWCGDFNYRIDLPNEEVKELIRQ---QNWDSL 754
Cdd:cd09095   132 TSGDGKVKERVLDYNKIIQALNLP--RNVPTNPYksesgdvttrfdeVFWFGDFNFRLSGPRHLVDALINQgqeVDVSAL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  755 IAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRkwpfdrsaedldllnasfqde 834
Cdd:cd09095   210 LQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSR--------------------- 268
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 256773218  835 skilytwTPGTL--LHYGRAE-LKTSDHRPVVALIDI 868
Cdd:cd09095   269 -------QKGDVccLKYNSCPsIKTSDHRPVFALFRV 298
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
624-883 2.49e-50

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 189.35  E-value: 2.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  624 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 701
Cdd:PLN03191  363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  702 EDFVEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLE 775
Cdd:PLN03191  443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  776 GKVTFAPTYKYDLFSEDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 850
Cdd:PLN03191  523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                         250       260       270
                  ....*....|....*....|....*....|...
gi 256773218  851 RAELKTSDHRPVVALIDIdifEVEAEERQKIYK 883
Cdd:PLN03191  574 RSEIRLSDHRPVSSMFLV---EVEVFDHRKLQR 603
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
533-811 4.70e-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: 153.99  E-value: 4.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivnaSTTNQKL 610
Cdd:cd09100     1 ITIFIGTWNMGNAPPPKKI-------TSWFQCK----GQGKTRDDTADyiPHDIYVIGTQE------------DPLGEKE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  611 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 688
Cdd:cd09100    58 WLDTLKHSLREitSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  689 HFAAGQSQVKERNEDFVEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKEL---IRQQNWDSLIAGDQL 760
Cdd:cd09100   138 HLTSGSEKKLRRNQNYFNILRFLVLgdkKLSPFNITHrfTHLFWLGDLNYRVELPNTEAENIiqkIKQQQYQELLPHDQL 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 256773218  761 INQKNAGQIFRGFLEGKVTFAPTYKYD-------LFSEDYDTSEKCRTPAWTDRVLWR 811
Cdd:cd09100   218 LIERKESKVFLQFEEEEITFAPTYRFErgtreryAYTKQKATGMKYNLPSWCDRVLWK 275
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
533-868 1.74e-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: 1.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDAPKLAGIQEFQDkrSKPTDIFAIGFEEmvelnagnivnaSTTNQKLWA 612
Cdd:cd09091     1 ISIFIGTWNMGSAPPPKNI-------TSWFTSKGQGKTRDDVAD--YIPHDIYVIGTQE------------DPLGEKEWL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  613 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 690
Cdd:cd09091    60 DLLRHSLKEltSLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  691 AAGQSQVKERNEDFVEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKELI---RQQNWDSLIAGDQLIN 762
Cdd:cd09091   140 TSGSEKKLRRNQNYLNILRFLSLgdkKLSAFNITHrfTHLFWLGDLNYRLDLPIQEAENIIqkiEQQQFEPLLRHDQLNL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  763 QKNAGQIFRGFLEGKVTFAPTYKYDLFSEDY-------DTSEKCRTPAWTDRVLWrrrkwpfdRSAEDLDLLNASFQDES 835
Cdd:cd09091   220 EREEHKVFLRFSEEEITFPPTYRYERGSRDTyaytkqkATGVKYNLPSWCDRILW--------KSYPETHIICQSYGCTD 291
                         330       340       350
                  ....*....|....*....|....*....|...
gi 256773218  836 KILytwtpgtllhygraelkTSDHRPVVALIDI 868
Cdd:cd09091   292 DIV-----------------TSDHSPVFGTFEV 307
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
533-811 3.37e-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: 3.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  533 IRVCVGTWNVNGGKQFRSiafknqtLTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivnaSTTNQKL 610
Cdd:cd09101     1 ISIFIGTWNMGSVPPPKS-------LASWLTSR----GLGKTLDETTVtiPHDIYVFGTQE------------NSVGDRE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  611 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 688
Cdd:cd09101    58 WVDFLRASLKEltDIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNC 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  689 HFAAGQSQVKERNEDFVEIARKLSFPMGR-------MLFSHdyVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLI 761
Cdd:cd09101   138 HLTSGNEKTHRRNQNYLDILRSLSLGDKQlnafdisLRFTH--LFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLN 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 256773218  762 NQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRT-------PAWTDRVLWR 811
Cdd:cd09101   216 LEREKNKVFLRFREEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILWK 272
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
893-969 7.04e-39

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: 139.08  E-value: 7.04e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256773218  893 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 969
Cdd:cd12719     1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
RRM_SYNJ cd12440
RNA recognition motif (RRM) found in synaptojanin-1, synaptojanin-2 and similar proteins; This ...
893-969 5.52e-31

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  Cd Length: 77  Bit Score: 116.76  E-value: 5.52e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256773218  893 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 969
Cdd:cd12440     1 DATVVVSLDSKSEEWNEFEDALIGELLRVLASYGDVVLVRFAHEGMLVTFRDGRSALAALALNGKQILGRTLKIRLK 77
RRM_SYNJ2 cd12720
RNA recognition motif (RRM) found in synaptojanin-2 and similar proteins; This subgroup ...
893-966 1.06e-10

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: 59.03  E-value: 1.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218  893 DGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITI 966
Cdd:cd12720     1 DATVVVNLLSpTLEEKNDFPEDLSTELVQCFQSYGTVILVRFNRGQMLVTFEDSRSALRVLDLDGIKVNGRAVKI 75
PHA03378 PHA03378
EBNA-3B; Provisional
972-1276 8.54e-10

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 63.55  E-value: 8.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  972 DWIKHLEEEMSLEKISVTLPSSASSTLLGEDAEVA--ADFDMEGDvddysaEVEELLPQHLQPSSSSGLGTSPSSSPRts 1049
Cdd:PHA03378  507 DLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPCVytEDLDIESD------EPASTEPVHDQLLPAPGLGPLQIQPLT-- 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1050 pcqSPTVPEY--SAPSLPIRPSRA--PSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPP 1125
Cdd:PHA03378  579 ---SPTTSQLasSAPSYAQTPWPVphPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPP 655
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1126 PSGARSPAPARKEFGGVGAPPSPGVARREIEAPKSPGTArkdnigrnQPSPQAGLAGPGPAGY-GAARP--TIPARAGVI 1202
Cdd:PHA03378  656 QVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTM--------QPPPRAPTPMRPPAAPpGRAQRpaAATGRARPP 727
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218 1203 SAPQSQARVCAGRPTPDSQSKPSET-LKGPAVLPEPLKPQAAfpqQPSLPTPAQKLQDPLVPIAAPTMPPSgPQP 1276
Cdd:PHA03378  728 AAAPGRARPPAAAPGRARPPAAAPGrARPPAAAPGRARPPAA---APGAPTPQPPPQAPPAPQQRPRGAPT-PQP 798
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
1129-1268 1.78e-08

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 59.01  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1129 A------RSPAPArkefggVGAPPSPGVARREIEAPKSPGTarkdnigrnqPSPQAGLAGPGPAGYGAARPTIPARAGVI 1202
Cdd:pfam15685  400 AhpipgpRRPAPA------LLAPPMFIFPAPTNGEPVRPGP----------PAPQALLPRPPPPTPPATPPPVPPPIPQL 463
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218  1203 SAPQSQARVCAGRPTPDSQSKPSETLKGP---AVLPEPL------KPQAAFPQQPSlPTPAQKLQDPLVPIAAPT 1268
Cdd:pfam15685  464 PALQPMPLAAARPPTPRPCPGHGESALAPaptAPLPPALaadqapAPALAAAPAPS-PAPAPATADPLPPAPAPI 537
PHA03247 PHA03247
large tegument protein UL36; Provisional
1027-1277 1.97e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1027 PQHLQPSSSSGLGTSPSSSPRTSPCQSPTVPeySAPSLPIRPSrAPSRTPGPPSSQGSPVDTQPAAQKDSSQtlepkrpp 1106
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPALPAAPAPP--AVPAGPATPG-GPARPARPPTTAGPPAPAPPAAPAAGPP-------- 2780
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1107 pPRPVAPPARPAPPQRPPPPS-----GARSPAPARKEFGGVGAPPSPGVARREIEAPKSPGTARkdniGRNQPS-PQAGL 1180
Cdd:PHA03247 2781 -RRLTRPAVASLSESRESLPSpwdpaDPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP----GPPPPSlPLGGS 2855
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1181 AGPG-------PAGYGAARPTIPARAGV--ISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPqQPSLP 1251
Cdd:PHA03247 2856 VAPGgdvrrrpPSRSPAAKPAAPARPPVrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP-QPPPP 2934
                         250       260
                  ....*....|....*....|....*...
gi 256773218 1252 TPAQKlQDPLVPIA--APTMPPSGPQPN 1277
Cdd:PHA03247 2935 PPPRP-QPPLAPTTdpAGAGEPSGAVPQ 2961
PHA03247 PHA03247
large tegument protein UL36; Provisional
1054-1280 2.75e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.80  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1054 PTVPEYSAPSLPIRPSRAPSRTPgPPSSQGSPVDTQPAAQKDSS--QTLEPKRPPPPRPVAPPARPAPPQRPPPPSGARS 1131
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAP-HALVSATPLPPGPAAARQASpaLPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1132 PAPARkefGGVGAPP---------SPGVARREIEAPKSPGTARKDNIGRNQ------------PSPQAGLAGPGPAGYGA 1190
Cdd:PHA03247 2769 PAPPA---APAAGPPrrltrpavaSLSESRESLPSPWDPADPPAAVLAPAAalppaaspagplPPPTSAQPTAPPPPPGP 2845
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1191 ARPTIPARAGVISA--------PQSQARVCAGRPTPDSQ-------SKPSETLKGPAVLPEPLkPQAAFPQQPSLPTPAQ 1255
Cdd:PHA03247 2846 PPPSLPLGGSVAPGgdvrrrppSRSPAAKPAAPARPPVRrlarpavSRSTESFALPPDQPERP-PQPQAPPPPQPQPQPP 2924
                         250       260
                  ....*....|....*....|....*
gi 256773218 1256 KLQDPLVPIAAPTMPPSGPQPNLET 1280
Cdd:PHA03247 2925 PPPQPQPPPPPPPRPQPPLAPTTDP 2949
PHA03247 PHA03247
large tegument protein UL36; Provisional
1060-1278 1.55e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1060 SAPSLPIRPsRAPSRTPGPPSSQGSPVDTQPAAqkdssqtlepkrpppprpvapparpappqrPPPPSGARSPAPARKEF 1139
Cdd:PHA03247 2590 DAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDT------------------------------HAPDPPPPSPSPAANEP 2638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1140 GGVGAPPSPGVAR-REIEAPKSPGTARKDNIGRNQPSPQAGLAGPGPAgygAARPTIPARAGVISAPQsqarvcagrPTP 1218
Cdd:PHA03247 2639 DPHPPPTVPPPERpRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR---AARPTVGSLTSLADPPP---------PPP 2706
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256773218 1219 DSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNL 1278
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL 2783
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1127-1277 7.11e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1127 SGARSPAPARKEFGGVGAPPSPGVArreieAPKSPGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQ 1206
Cdd:PHA03307  784 AGSSPPVRAEAAFRRPGRLRRSGPA-----ADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKP 858
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218 1207 SQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPiaaptMPPSGPQPN 1277
Cdd:PHA03307  859 AAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGP-----MPPGGPDPR 924
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
640-737 9.60e-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: 51.33  E-value: 9.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  640 VFIRPqhaPFIRDVAVDTVKTGMGgATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFpmgRML 719
Cdd:cd08372    71 ILSKT---PKFKIVEKHQYKFGEG-DSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKR---LRQ 143
                          90
                  ....*....|....*...
gi 256773218  720 FSHDYVFWCGDFNYRIDL 737
Cdd:cd08372   144 PNSAPVVICGDFNVRPSE 161
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1064-1274 2.03e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 52.19  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1064 LPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVapparpappqrppppsgARSPAPARKEFGGVG 1143
Cdd:PRK12323  361 LAFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAA-----------------APAAAAAARAVAAAP 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1144 APPSPgvARREIEAPKSPGTARKdniGRNQPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSqSK 1223
Cdd:PRK12323  424 ARRSP--APEALAAARQASARGP---GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDD-PP 497
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256773218 1224 PSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGP 1274
Cdd:PRK12323  498 PWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA 548
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1067-1276 3.09e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.53  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1067 RPSRAPSRTPGPPSSQGSPVDTQPAAQkdssqtlepkrpppprpvappARPAPPQRPPPPSGARSPAPARKEFGGVGAPP 1146
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAP---------------------AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAP 650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1147 SPGVARREIEAPKSPGTARKDNIGRNQPS----PQAGLAGPGPAGyGAARPTIPARAGVISAPQSQARVCAGRPTPDSQS 1222
Cdd:PRK07764  651 EHHPKHVAVPDASDGGDGWPAKAGGAAPAapppAPAPAAPAAPAG-AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGAS 729
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 256773218 1223 KPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQP 1276
Cdd:PRK07764  730 APSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1057-1272 1.08e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.85  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1057 PEYSAPSLPIRPSRAPSRTPGPPSSQ--GSPVDTQPAAQKDSSQtlEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAP 1134
Cdd:PRK07003  412 PKAAAAAAATRAEAPPAAPAPPATADrgDDAADGDAPVPAKANA--RASADSRCDERDAQPPADSGSASAPASDAPPDAA 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1135 ARKEFGGVGAPPSPGVARREIEAPKSPgtARKDNIGRN-QPSPQAglAGPGPAgygAARPtiPARAGVISAPQSQARVCA 1213
Cdd:PRK07003  490 FEPAPRAAAPSAATPAAVPDARAPAAA--SREDAPAAAaPPAPEA--RPPTPA---AAAP--AARAGGAAAALDVLRNAG 560
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218 1214 GRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPsLPTPAQKLQDPLVPI--AAPTMPPS 1272
Cdd:PRK07003  561 MRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQ-VPTPRARAATGDAPPngAARAEQAA 620
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
677-862 1.68e-05

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


Pssm-ID: 197326  Cd Length: 383  Bit Score: 48.62  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  677 LFHTTSLCFVCSHFAAGQSQVKERNEDFVeIARKLSFPMGRMLFshdYVFwcGDFNYRIDL------------------- 737
Cdd:cd09092   176 LFHDASNLAACESSPSVYSQNRHRALGYV-LERLTDERFEKVPF---FVF--GDFNFRLDTksvvetlcakatmqtvrka 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  738 -PNEEVKELIRQQNWD----------SLIAGDQLINQKNAGQIFRGF-----------LEGKVTFAPTYKYdlfSEDYDT 795
Cdd:cd09092   250 dSNIVVKLEFREKDNDnkvvlqiekkKFDYFNQDVFRDNNGKALLKFdkelevfkdvlYELDISFPPSYPY---SEDPEQ 326
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  796 SE---KCRTPAWTDRVLwrrrkwpFDRSAEDLDLLNasfqDESKILYTwtpgtllHYGRaELKTSDHRPV 862
Cdd:cd09092   327 GTqymNTRCPAWCDRIL-------MSHSARELKSEN----EEKSVTYD-------MIGP-NVCMGDHKPV 377
PHA03378 PHA03378
EBNA-3B; Provisional
1053-1276 2.66e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.52  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1053 SPTVPEYSAPSLPIRPSRAPSRTPgPPssQGSPVDTQP---AAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGA 1129
Cdd:PHA03378  682 NTMLPIQWAPGTMQPPPRAPTPMR-PP--AAPPGRAQRpaaATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPA 758
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1130 RSPAPARKEFGGVGAP-PSPgvarreieAPKSPGTARKDNIG--RNQPSPQAG-----LAGPGPAGYGAARPTIPAR--- 1198
Cdd:PHA03378  759 AAPGRARPPAAAPGAPtPQP--------PPQAPPAPQQRPRGapTPQPPPQAGptsmqLMPRAAPGQQGPTKQILRQllt 830
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1199 AGVISA------PQSQARVCAGRPTPDSQSKPSE-TLKGPAVLPEPLKPqAAFPQQPSLPTPAQKLQDPLVPIAAP---- 1267
Cdd:PHA03378  831 GGVKRGrpslkkPAALERQAAAGPTPSPGSGTSDkIVQAPVFYPPVLQP-IQVMRQLGSVRAAAASTVTQAPTEYTgerr 909
                         250
                  ....*....|..
gi 256773218 1268 ---TMPPSGPQP 1276
Cdd:PHA03378  910 gvgPMHPTDIPP 921
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1052-1277 3.63e-05

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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 47.84  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1052 QSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPpsgaRS 1131
Cdd:NF033839  285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQP----EK 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1132 PAPARK---EFGGVGAPPSPGVARREIEA-PKSPGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARagvisAPQS 1207
Cdd:NF033839  361 PKPEVKpqpEKPKPEVKPQPETPKPEVKPqPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV-----KPQP 435
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1208 qarvcagrPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQdplvpIAAPTMPPSGPQPN 1277
Cdd:NF033839  436 --------EKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQ-----PEKPKPDNSKPQAD 492
RRM3_Prp24 cd12298
RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar ...
915-968 5.81e-05

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: 42.63  E-value: 5.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218  915 IDELLRQFAHFGEV---ILIRFVEDKM--------WVTFLEGSSALNALSLNGKELLNRTITITL 968
Cdd:cd12298    14 EEALRGIFEKFGEIesiNIPKKQKNRKgrhnngfaFVTFEDADSAESALQLNGTLLDNRKISVSL 78
MISS pfam15822
MAPK-interacting and spindle-stabilizing protein-like; MISS is a family of eukaryotic ...
1128-1275 7.47e-05

MAPK-interacting and spindle-stabilizing protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilizing protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 45.75  E-value: 7.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1128 GARSPAPARKEFGGVGAPPSPGVARREIE----APKSPGTARKDNIGRNQPSpqaGLAGPGPAGYGAArPTIPARA-GVI 1202
Cdd:pfam15822   95 GGPYPAPTVPGPGPIGPYPTPNMPFPELPrpygAPTDPAAAAPSGPWGSMSS---GPWAPGMGGQYPA-PNMPYPSpGPY 170
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256773218  1203 SAPQSQARVCAGRPTPDSQSKPsetlkGPAVLPEPL-KPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMpPSGPQ 1275
Cdd:pfam15822  171 PAVPPPQSPGAAPPVPWGTVPP-----GPWGPPAPYpDPTGSYPMPGLYPTPNNPFQVPSGPSGAPPM-PGGPH 238
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1060-1277 7.58e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1060 SAPSLPIRPSRAPSRTPGPPSSQGSPVD-TQPAAQKDSSQTLEpkrpppprpvapparpappqrppppsgARSPAPARKE 1138
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSSTHVPTNlTAPASTGPTVSTAD---------------------------VTSPTPAGTT 482
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1139 FGGVGAPPSPgvarreieAPKSPGTARKdniGRNQPSPQAGLAGPGPagyGAARPTiPAragvisapqsqarvcAGRPTP 1218
Cdd:pfam05109  483 SGASPVTPSP--------SPRDNGTESK---APDMTSPTSAVTTPTP---NATSPT-PA---------------VTTPTP 532
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 256773218  1219 DSQSkPSETLKGPAVLPEPLKPQAAFPqQPSLPTPAQKLQDPLVPIAAPTMPPSGPQPN 1277
Cdd:pfam05109  533 NATS-PTLGKTSPTSAVTTPTPNATSP-TPAVTTPTPNATIPTLGKTSPTSAVTTPTPN 589
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1174-1276 1.03e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1174 PSPQAGlAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTP 1253
Cdd:PRK07764  392 GAPAAA-APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAP 470
                          90       100
                  ....*....|....*....|...
gi 256773218 1254 AQKLQDPLVPIAAPTMPPSGPQP 1276
Cdd:PRK07764  471 AAAPEPTAAPAPAPPAAPAPAAA 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
1057-1280 1.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1057 PEYSAPSLPIRPSRAPsrtPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRP--------VAPPARPAPPQRPPPPSG 1128
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHA---PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvsrprrARRLGRAAQASSPPQRPR 2684
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1129 ARSPAPARKEFGGVGAPPSPGVA---RREIEAPKSPGTARKDNIGRNQPSPQAGLAGPGPAGyGAARPTIPARAGvisAP 1205
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTpepAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPA-GPATPGGPARPA---RP 2760
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1206 QSQARVCAGRPTPDSQSKPSETLKGPAV---------LPEPLKPQ-------AAFPQQPSLPTPAQKLQDPLVPIAAPTM 1269
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVaslsesresLPSPWDPAdppaavlAPAAALPPAASPAGPLPPPTSAQPTAPP 2840
                         250
                  ....*....|.
gi 256773218 1270 PPSGPQPNLET 1280
Cdd:PHA03247 2841 PPPGPPPPSLP 2851
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1053-1275 1.36e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1053 SPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSG---- 1128
Cdd:PRK07764  596 GGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAkagg 675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1129 ----ARSPAPARkefggvGAPPSPGVARREIEAPKSPGTARKdnigrnQPSPQAGLAGPGPAGYGAARPtiPARAGVISA 1204
Cdd:PRK07764  676 aapaAPPPAPAP------AAPAAPAGAAPAQPAPAPAATPPA------GQADDPAAQPPQAAQGASAPS--PAADDPVPL 741
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218 1205 PqsqarvcagrPTPDSQSKPSETlkgPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQ 1275
Cdd:PRK07764  742 P----------PEPDDPPDPAGA---PAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRR 799
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
916-966 1.40e-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: 41.50  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256773218  916 DELLRQFAHFGEVILIRFVEDKM-------WVTFLEGSSALNALS-LNGKELLNRTITI 966
Cdd:cd00590    13 EDLRELFSKFGEVVSVRIVRDRDgkskgfaFVEFESPEDAEKALEaLNGTELGGRPLKV 71
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1140-1279 1.55e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1140 GGVGAPPSPGVARREIEAPksPGTARKDNIGRNQPSPQAGLAGPGPAGY-----GAARPTIPARAGVISAPQSQARVCAG 1214
Cdd:PRK12323  369 GGGAGPATAAAAPVAQPAP--AAAAPAAAAPAPAAPPAAPAAAPAAAAAaravaAAPARRSPAPEALAAARQASARGPGG 446
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256773218 1215 RPTPDSQ--SKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPiAAPTMPPSGPQPNLE 1279
Cdd:PRK12323  447 APAPAPApaAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP-PWEELPPEFASPAPA 512
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1032-1280 2.10e-04

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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 45.53  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1032 PSSSSGLGTSPSSSPRtspcqSPTVPEYSAPSLPiRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPV 1111
Cdd:NF033839  147 SSSSSSSGSSTKPETP-----QPENPEHQKPTTP-APDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKH 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1112 APPARPAPPQRPPPPSGARSPAPARKEFGGvgapPSPGVarrEIEAPKSPGTARKDNIgrnQPSPQAGLAGPGPAGYGAA 1191
Cdd:NF033839  221 HLQKEKHRQIVALIKELDELKKQALSEIDN----VNTKV---EIENTVHKIFADMDAV---VTKFKKGLTQDTPKEPGNK 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1192 RPTIPaRAGVISAPQSQARVCAGRP-TPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQdplvpiaaPTMP 1270
Cdd:NF033839  291 KPSAP-KPGMQPSPQPEKKEVKPEPeTPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQ--------PEKP 361
                         250
                  ....*....|
gi 256773218 1271 PSGPQPNLET 1280
Cdd:NF033839  362 KPEVKPQPEK 371
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1131-1280 2.24e-04

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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 45.53  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1131 SPAPARKEFGGVGAPPSPGVaRREIEAPK--------SPGTARKDNIGRNQPSPQAGLAGPGPA---GYGAARPTIPARA 1199
Cdd:NF033839  302 SPQPEKKEVKPEPETPKPEV-KPQLEKPKpevkpqpeKPKPEVKPQLETPKPEVKPQPEKPKPEvkpQPEKPKPEVKPQP 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1200 GvisAPQSQARVCAGRPTPDSQSKPsETLKgPAVLPEPLKPQAAFPQQPSLPTPAQKLQdPLVPIAAPTMPPSGPQPNL- 1278
Cdd:NF033839  381 E---TPKPEVKPQPEKPKPEVKPQP-EKPK-PEVKPQPEKPKPEVKPQPEKPKPEVKPQ-PEKPKPEVKPQPEKPKPEVk 454
                         170
                  ....*....|
gi 256773218 1279 --------ET 1280
Cdd:NF033839  455 pqpetpkpEV 464
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1136-1276 3.43e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1136 RKEFGG------VGAPPSPGVARREIEAPKSPGTARKDNigrnQPSPQAGLAGPGPAGYGAA----RPTIPARAGVISAP 1205
Cdd:PRK07764  575 AEELGGdwqveaVVGPAPGAAGGEGPPAPASSGPPEEAA----RPAAPAAPAAPAAPAPAGAaaapAEASAAPAPGVAAP 650
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218 1206 QSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQP 1276
Cdd:PRK07764  651 EHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP 721
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1057-1277 6.61e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1057 PEYSAPSLPIRPSRAPSRTPGPPssQGS-PVDTQPAAQKDSSQTL-EPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAP 1134
Cdd:PHA03307  167 ASSRQAALPLSSPEETARAPSSP--PAEpPPSTPPAAASPRPPRRsSPISASASSPAPAPGRSAADDAGASSSDSSSSES 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1135 ARKEFGGVGAPPSPGVARreIEAPKSPGTArkdnIGRNQPSPQAGLAGPGPAGYGAARPTIPARAGV-ISAPQSQARVCA 1213
Cdd:PHA03307  245 SGCGWGPENECPLPRPAP--ITLPTRIWEA----SGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSgPAPSSPRASSSS 318
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256773218 1214 GRPTPDSQSKPSETLKGPAvlpeplkpQAAFPQQPSlPTPAQKLQDPlVPIAAPTMPPSGPQPN 1277
Cdd:PHA03307  319 SSSRESSSSSTSSSSESSR--------GAAVSPGPS-PSRSPSPSRP-PPPADPSSPRKRPRPS 372
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
1127-1227 7.19e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.90  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1127 SGARSPAPARkefGGVGAPPSPGVARREIEAPKSPGTARKDNIGRNQPS--PQAGL----AGPGPAGYGAARPTIPARAG 1200
Cdd:PRK14959  382 SGSAAEGPAS---GGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSaaPSPRVpwddAPPAPPRSGIPPRPAPRMPE 458
                          90       100
                  ....*....|....*....|....*..
gi 256773218 1201 VISAPQSQARVCAGRPTPDSQSKPSET 1227
Cdd:PRK14959  459 ASPVPGAPDSVASASDAPPTLGDPSDT 485
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
1129-1275 8.28e-04

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225689 [Multi-domain]  Cd Length: 226  Bit Score: 42.57  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1129 ARSPAPARK-EFGGVGAPPSPGVARREIEApkspgtarkdnigrnQPSPQAGLAGPGPAGYGAArptiparagvisaPQS 1207
Cdd:COG3147    27 LDGKKKHRQdEVAAIPLPPKPQGDRDEPRV---------------LPAVVQVVALPTQPPEGVA-------------QEI 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256773218 1208 QARVCAGRPtpdsqSKPSETLKGPAVLPEPLKPQAAfPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQ 1275
Cdd:COG3147    79 QDAGDAAAA-----SVDPQPVAQPPVESTPAGVPVA-AQTPKPVKPPKQPPAGAVPAKPTPKPEPKPV 140
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1124-1276 8.72e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1124 PPPSGARSPAPARKEFGGVGAPPSPGVARREIEAPKSPGTArkdnigRNQPSPQAGLAGPGPAGYGAARPTIPARAGVIS 1203
Cdd:PRK07003  388 AAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPA------APAPPATADRGDDAADGDAPVPAKANARASADS 461
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256773218 1204 APQSQARVCAGRPTPDS---QSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQP 1276
Cdd:PRK07003  462 RCDERDAQPPADSGSASapaSDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTP 537
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1179-1279 1.24e-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: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1179 GLAGPGPAGYGAARPTIPaRAGVISAPQSQARVCAGRP-TPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKL 1257
Cdd:NF033839  278 GLTQDTPKEPGNKKPSAP-KPGMQPSPQPEKKEVKPEPeTPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKP 356
                          90       100
                  ....*....|....*....|..
gi 256773218 1258 QdPLVPiaAPTMPPSGPQPNLE 1279
Cdd:NF033839  357 Q-PEKP--KPEVKPQPEKPKPE 375
RRM smart00360
RNA recognition motif;
911-966 1.41e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.41e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218    911 DDALIDELLRQFAHFGEVILIRFVEDKMW--------VTFLEGSSALNALS-LNGKELLNRTITI 966
Cdd:smart00360    9 PDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
1135-1274 1.57e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 42.24  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1135 ARKEFGGVGAPPSPGVARREIEAPKSPGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTI-PARAGVISAPQSQARVCA 1213
Cdd:PTZ00436  188 ARREDAAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAAAPAKAAAaPAKAAAPPAKAAAPPAKA 267
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256773218 1214 GRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPtPAQKLQDPLVPIAAPTMPPSGP 1274
Cdd:PTZ00436  268 AAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAA-PAKAAAAPAKAAAPPAKAAAPP 327
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1020-1269 1.59e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1020 AEVEELLPQHLQP--SSSSGLGTSPSSSPRTSPCQSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSS 1097
Cdd:PRK07003  420 ATRAEAPPAAPAPpaTADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAP 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1098 QTLEPKRPPPPRPVAPPARPAPPQRppppsgARSPAPArkefggvGAPPSPGVARreiEAPKSPGTARKDNIGRNqpspq 1177
Cdd:PRK07003  500 SAATPAAVPDARAPAAASREDAPAA------AAPPAPE-------ARPPTPAAAA---PAARAGGAAAALDVLRN----- 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1178 AGL---AGPGPAGYGAARPTIPARAGVISAPqsqARVCAGRPTPDSQSKPSETLKGPAVlpepLKPQAAfpQQPSLPTPA 1254
Cdd:PRK07003  559 AGMrvsSDRGARAAAAAKPAAAPAAAPKPAA---PRVAVQVPTPRARAATGDAPPNGAA----RAEQAA--ESRGAPPPW 629
                         250
                  ....*....|....*.
gi 256773218 1255 QKL-QDPLVPIAAPTM 1269
Cdd:PRK07003  630 EDIpPDDYVPLSADEG 645
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1051-1280 2.07e-03

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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 427171 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1051 CQSPTVPEYSAPslPIRPSRAPSRTPgPPSSQGSPVDTQPAaqkdssqtlepkrpppprpvapparpappQRPPPPSGAR 1130
Cdd:pfam03154  176 AQSGAASPPSPP--PPGTTQAATAGP-TPSAPSVPPQGSPA-----------------------------TSQPPNQTQS 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1131 SPAP-ARKEFGGVGAP---PSPGVARREIEAPKSPGTARKdnigrnQPSPQAGLAGPGP-------AGYGAARPTIPARA 1199
Cdd:pfam03154  224 TAAPhTLIQQTPTLHPqrlPSPHPPLQPMTQPPPPSQVSP------QPLPQPSLHGQMPpmphslqTGPSHMQHPVPPQP 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  1200 GVISAPQSQARVCAGrPTPDSQSKPSETLKGPAVLPEPLKPQAafPQQPSLPtPAqklqdplvPIAAPTM--PPSGPQPN 1277
Cdd:pfam03154  298 FPLTPQSSQSQVPPG-PSPAAPGQSQQRIHTPPSQSQLQSQQP--PREQPLP-PA--------PLSMPHIkpPPTTPIPQ 365

                   ...
gi 256773218  1278 LET 1280
Cdd:pfam03154  366 LPN 368
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
1193-1278 2.14e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.16  E-value: 2.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218   1193 PTIPARAGVIsaPQSQARVCAGRP--TPDSQSKPSetLKGPAvlPEPLKPQAAFPQQPSLPTPAQKLQDPLVPI----AA 1266
Cdd:smart00818   59 PVLPAQQPVV--PQQPLMPVPGQHsmTPTQHHQPN--LPQPA--QQPFQPQPLQPPQPQQPMQPQPPVHPIPPLppqpPL 132
                            90
                    ....*....|..
gi 256773218   1267 PTMPPSGPQPNL 1278
Cdd:smart00818  133 PPMFPMQPLPPL 144
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
991-1271 2.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  991 PSSASSTLLGEDAEVAADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGtspsssprtspcqSPTVPEYSAPSLPIRPSR 1070
Cdd:PHA03307  131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSP-------------EETARAPSSPPAEPPPST 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1071 APSRTPGPPSSQGSPV-----DTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAPARKEFGGVGAP 1145
Cdd:PHA03307  198 PPAAASPRPPRRSSPIsasasSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1146 P-------SPGVARREIEAPKSPGTARK-------DNIGRNQPSPQAGLA--------------GPGPAGYGAARPTIPA 1197
Cdd:PHA03307  278 PssrpgpaSSSSSPRERSPSPSPSSPGSgpapsspRASSSSSSSRESSSSstssssessrgaavSPGPSPSRSPSPSRPP 357
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773218 1198 RAGVISAPQSQARVCAGRPTPdSQSKPSETL-KGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPP 1271
Cdd:PHA03307  358 PPADPSSPRKRPRPSRAPSSP-AASAGRPTRrRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
RRM2_SREK1 cd12260
RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 ...
916-967 2.72e-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: 38.06  E-value: 2.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 256773218  916 DELLRQFAHFGEVILIRFVEDK------MWVTFLEGSSALNALSLNGKELLNRTITIT 967
Cdd:cd12260    19 DQLLEFFSQAGEVKYVRMAGDEtqptryAFVEFAEQTSVINALKLNGKMFGGRPLKVN 76
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1059-1271 3.33e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1059 YSAPSLPIRPSrAPSRTPGPPSSQGSpVDTQPAAqkdSSQTLEPKRpppprpvapparpappqrppppsgarSPAPArke 1138
Cdd:PRK10263  333 WAAPVEPVTQT-PPVASVDVPPAQPT-VAWQPVP---GPQTGEPVI--------------------------APAPE--- 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1139 fggvGAPPSPGVARREIE---------APKSPGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQsqa 1209
Cdd:PRK10263  379 ----GYPQQSQYAQPAVQyneplqqpvQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEE--- 451
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256773218 1210 rvcagrptPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPP 1271
Cdd:PRK10263  452 --------QQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPP 505
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1079-1272 3.67e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1079 PSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAPARKEFGGVGAPPSPGVARREIEAP 1158
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1159 KSPGtarkdnigrnqPSPQAGLAGPGPAGYGAARptiPARAGVISAPQSQARVCAGRPTPDSQSKPSEtlKGPAVLPEPL 1238
Cdd:PHA03307  124 ASPP-----------PSPAPDLSEMLRPVGSPGP---PPAASPPAAGASPAAVASDAASSRQAALPLS--SPEETARAPS 187
                         170       180       190
                  ....*....|....*....|....*....|....
gi 256773218 1239 KPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPS 1272
Cdd:PHA03307  188 SPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1173-1277 3.71e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1173 QPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSET-LKGPAVLPEPLKPQAAFPQQPSL- 1250
Cdd:PRK12323  364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAvAAAPARRSPAPEALAAARQASARg 443
                          90       100
                  ....*....|....*....|....*....
gi 256773218 1251 --PTPAQKLQDPLVPIAAPTMPPSGPQPN 1277
Cdd:PRK12323  444 pgGAPAPAPAPAAAPAAAARPAAAGPRPV 472
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1174-1271 3.99e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1174 PSPQAGLAGPGPAGYGAARPTIparagvisAPQSQARVCAGRPTPDSQSKPsETLKGPAVLPEPLKPQAAFPQQPSLPTP 1253
Cdd:PRK14950  362 PVPAPQPAKPTAAAPSPVRPTP--------APSTRPKAAAAANIPPKEPVR-ETATPPPVPPRPVAPPVPHTPESAPKLT 432
                          90
                  ....*....|....*...
gi 256773218 1254 AQKLQDPLVPIAAPTMPP 1271
Cdd:PRK14950  433 RAAIPVDEKPKYTPPAPP 450
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1176-1276 5.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.91  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1176 PQAGLAGPGPAGygAARPTIPARAGVISAPQSQARVCAgrptpdSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPtpaq 1255
Cdd:PRK14971  363 TQKGDDASGGRG--PKQHIKPVFTQPAAAPQPSAAAAA------SPSPSQSSAAAQPSAPQSATQPAGTPPTVSVD---- 430
                          90       100
                  ....*....|....*....|.
gi 256773218 1256 klqdplVPIAAPTMPPSGPQP 1276
Cdd:PRK14971  431 ------PPAAVPVNPPSTAPQ 445
PHA03301 PHA03301
envelope glycoprotein L; Provisional
1189-1276 5.62e-03

envelope glycoprotein L; Provisional


Pssm-ID: 223037 [Multi-domain]  Cd Length: 226  Bit Score: 39.85  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1189 GAARPTiPARAGVISAPQSQARVCAGRPTPDSQSKPSetLKGPAVLPEplkpQAAFPQQPSLPTPAqklqdplvPIAAPT 1268
Cdd:PHA03301  140 QAASHT-PVPPGCVNFEYSRTRRCVGRRTPGPANEPR--TRRPLSAPD----DEASPQPKSLATPP--------PVAAPS 204

                  ....*...
gi 256773218 1269 MPPSGPQP 1276
Cdd:PHA03301  205 RRTPRPRR 212
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1176-1276 7.37e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1176 PQAGLAGPGPAGygAARPTIPARAGVISAPQSQARVCAGR-----------PTPDSQSKPSETLKGPAVLPEPL--KPQA 1242
Cdd:PRK14951  366 PAAAAEAAAPAE--KKTPARPEAAAPAAAPVAQAAAAPAPaaapaaaasapAAPPAAAPPAPVAAPAAAAPAAApaAAPA 443
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 256773218 1243 AFPQQPSLPTPAQ--------KLQDPLVPIAAPTMPPSGPQP 1276
Cdd:PRK14951  444 AVALAPAPPAQAApetvaipvRVAPEPAVASAAPAPAAAPAA 485
PHA03247 PHA03247
large tegument protein UL36; Provisional
1054-1276 8.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1054 PTVPEYSAPSLPIRPSR---------APSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKrpppprpvapparpappqrpp 1124
Cdd:PHA03247  279 PPPPEAAAPNGAAAPPDgvwgaalagAPLALPAPPDPPPPAPAGDAEEEDDEDGAMEVV--------------------- 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218 1125 ppsgarSPAPARKEFGGVGAPPSpgvaRREIEAPksPGTARKDNIGRNQPsPQAGLagpgpagygaarPTIPARagviSA 1204
Cdd:PHA03247  338 ------SPLPRPRQHYPLGFPKR----RRPTWTP--PSSLEDLSAGRHHP-KRASL------------PTRKRR----SA 388
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256773218 1205 PQSQARVCAGrPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPlvpiAAPTMPPSGPQP 1276
Cdd:PHA03247  389 RHAATPFARG-PGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSD----DGPAPPPERQPP 455
RRM_II_PABPs cd12306
RNA recognition motif in type II polyadenylate-binding proteins; This subfamily corresponds to ...
916-967 9.12e-03

RNA recognition motif in type II polyadenylate-binding proteins; This subfamily corresponds to the RRM of type II polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 2 (PABP-2 or PABPN1), embryonic polyadenylate-binding protein 2 (ePABP-2 or PABPN1L) and similar proteins. PABPs are highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in the regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. ePABP-2 is predominantly located in the cytoplasm and PABP-2 is located in the nucleus. In contrast to the type I PABPs containing four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), the type II PABPs contains a single highly-conserved RRM. This subfamily also includes Saccharomyces cerevisiae RBP29 (SGN1, YIR001C) gene encoding cytoplasmic mRNA-binding protein Rbp29 that binds preferentially to poly(A). Although not essential for cell viability, Rbp29 plays a role in modulating the expression of cytoplasmic mRNA. Like other type II PABPs, Rbp29 contains one RRM only.


Pssm-ID: 409747 [Multi-domain]  Cd Length: 73  Bit Score: 36.13  E-value: 9.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773218  916 DELLRQFAHFGEVILIRFVEDKM--------WVTFLEGSSALNALSLNGKELLNRTITIT 967
Cdd:cd12306    14 EELQAHFKSCGTINRVTILCDKFtgqpkgfaYIEFVDKSSVENALLLNESEFRGRQIKVT 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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