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Conserved domains on  [gi|1907115283|ref|XP_036015603|]
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synaptojanin-1 isoform X11 [Mus musculus]

Protein Classification

INPP5c_Synj1 and RRM_SYNJ1 domain-containing protein( domain architecture ID 13429226)

protein containing domains COG5329, INPP5c_Synj1, RRM_SYNJ1, and PHA03247

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 ...
672-1007 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 1907115283  672 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 751
Cdd:cd09098      1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 831
Cdd:cd09098     81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  832 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 911
Cdd:cd09098    161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  912 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 991
Cdd:cd09098    241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                          330
                   ....*....|....*.
gi 1907115283  992 ELKTSDHRPVVALIDI 1007
Cdd:cd09098    321 ELKTSDHRPVVALIDI 336
COG5329 super family cl34984
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
204-627 1.80e-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: 317.79  E-value: 1.80e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 274
Cdd:COG5329     61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  275 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 345
Cdd:COG5329    137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  346 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 425
Cdd:COG5329    216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  426 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 505
Cdd:COG5329    295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  506 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 583
Cdd:COG5329    374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907115283  584 YAGTGALEGKAK-------AGKLKDGARSVTRTIQNNFFDSSKQEAIDVLL 627
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 ...
1006-1147 4.30e-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: 211.21  E-value: 4.30e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1006 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 1084
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907115283 1085 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEMSLEKIS-VTLPSSASSTLLGEDAEVAAD 1147
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIILCTDNtIPVSPCANSTLLAEDFDFGSP 144
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1193-1572 1.75e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1193 PTVPEYSA-PSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPArpappqrppPPSAPKSP 1271
Cdd:PHA03247  2589 PDAPPQSArPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER---------PRDDPAPG 2659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1272 GTARKDNIGRNQPSPQAG--LAGPGPAgygAARPTIPARAGVISAPQsqarvcagrPTPDSQSKPSETLKGPAVLPEPLK 1349
Cdd:PHA03247  2660 RVSRPRRARRLGRAAQASspPQRPRRR---AARPTVGSLTSLADPPP---------PPPTPEPAPHALVSATPLPPGPAA 2727
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1350 PQAAFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNLeTPPQPPPRSRSSQSLPSDSSPQL 1412
Cdd:PHA03247  2728 ARQASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL-TRPAVASLSESRESLPSPWDPAD 2806
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1413 QVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqLPSASQSQVNPLSSVSCMPTRPPGPEE 1492
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPAAKPAAPARPPV 2883
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1493 SK-SQESMGSSANPFPsLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPLShDTSKASSSLGGFE 1571
Cdd:PHA03247  2884 RRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTT-DPAGAGEPSGAVP 2960

                   .
gi 1907115283 1572 D 1572
Cdd:PHA03247  2961 Q 2961
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
672-1007 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 1907115283  672 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 751
Cdd:cd09098      1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 831
Cdd:cd09098     81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  832 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 911
Cdd:cd09098    161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  912 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 991
Cdd:cd09098    241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                          330
                   ....*....|....*.
gi 1907115283  992 ELKTSDHRPVVALIDI 1007
Cdd:cd09098    321 ELKTSDHRPVVALIDI 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
670-1010 4.68e-127

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: 4.68e-127
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   670 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKL 749
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   750 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 829
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   830 AAGQSQVKERNEDFVEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 906
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   907 QIFRGFLEGKVTFAPTYKYDLF-SEDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 985
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 1907115283   986 lHYGRAELKTSDHRPVVALIDIDIF 1010
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
204-627 1.80e-94

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 317.79  E-value: 1.80e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 274
Cdd:COG5329     61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  275 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 345
Cdd:COG5329    137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  346 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 425
Cdd:COG5329    216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  426 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 505
Cdd:COG5329    295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  506 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 583
Cdd:COG5329    374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907115283  584 YAGTGALEGKAK-------AGKLKDGARSVTRTIQNNFFDSSKQEAIDVLL 627
Cdd:COG5329    451 YTGTGALKSSFTrrgrrsfAGALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
204-484 1.10e-86

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: 1.10e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISL---------RVDASDEDRI-SEVRKVLNSGNFY 273
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGGPIYKITDVEFIPLnsslydsssKSKSPDEARLlKLLKLFLSSGSFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  274 FAWSasgvsLDLS------LNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACL 347
Cdd:pfam02383   77 FSYD-----YDLTnslqrnSTTSRSPSFDSLDERFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  348 ISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDC-----VSSFIQIRGSVPLFWEQ-PGLQVGSHRVRMSRgFEA 421
Cdd:pfam02383  152 ISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTGnsegkIFSFVQIRGSIPLFWSQdPNLKYSKPKIQITR-PEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907115283  422 NAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKAS--EHASDIHMVSFDYHQMVK 484
Cdd:pfam02383  231 TQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEKAVKYLnqFLPDKLRYTAFDFHHECK 295
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
665-1033 1.84e-68

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 238.91  E-value: 1.84e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  665 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVNA 742
Cdd:COG5411     23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  743 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 817
Cdd:COG5411     84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  818 HTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 895
Cdd:COG5411    163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  896 GDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 975
Cdd:COG5411    243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907115283  976 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIA--VQGPPDG 1033
Cdd:COG5411    299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
1006-1147 4.30e-63

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


Pssm-ID: 286093  Cd Length: 146  Bit Score: 211.21  E-value: 4.30e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1006 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 1084
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907115283 1085 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEMSLEKIS-VTLPSSASSTLLGEDAEVAAD 1147
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIILCTDNtIPVSPCANSTLLAEDFDFGSP 144
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
763-1022 1.59e-49

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 187.42  E-value: 1.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  763 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 840
Cdd:PLN03191   363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  841 EDFVEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLE 914
Cdd:PLN03191   443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  915 GKVTFAPTYKYDLFSEDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 989
Cdd:PLN03191   523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907115283  990 RAELKTSDHRPVVALIDIdifEVEAEERQKIYK 1022
Cdd:PLN03191   574 RSEIRLSDHRPVSSMFLV---EVEVFDHRKLQR 603
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
1032-1108 2.28e-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: 141.00  E-value: 2.28e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907115283 1032 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 1108
Cdd:cd12719      1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
1193-1572 1.75e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1193 PTVPEYSA-PSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPArpappqrppPPSAPKSP 1271
Cdd:PHA03247  2589 PDAPPQSArPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER---------PRDDPAPG 2659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1272 GTARKDNIGRNQPSPQAG--LAGPGPAgygAARPTIPARAGVISAPQsqarvcagrPTPDSQSKPSETLKGPAVLPEPLK 1349
Cdd:PHA03247  2660 RVSRPRRARRLGRAAQASspPQRPRRR---AARPTVGSLTSLADPPP---------PPPTPEPAPHALVSATPLPPGPAA 2727
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1350 PQAAFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNLeTPPQPPPRSRSSQSLPSDSSPQL 1412
Cdd:PHA03247  2728 ARQASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL-TRPAVASLSESRESLPSPWDPAD 2806
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1413 QVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqLPSASQSQVNPLSSVSCMPTRPPGPEE 1492
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPAAKPAAPARPPV 2883
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1493 SK-SQESMGSSANPFPsLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPLShDTSKASSSLGGFE 1571
Cdd:PHA03247  2884 RRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTT-DPAGAGEPSGAVP 2960

                   .
gi 1907115283 1572 D 1572
Cdd:PHA03247  2961 Q 2961
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1199-1569 1.57e-04

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: 46.45  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1199 SAPSLPIRPSRAPSRTPGPPSSQGSPVD-TQPAAQKDSSQTLEpkrpppPRPVAPPARPAPPQRPPPPSAPKSPGTARKd 1277
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSSTHVPTNlTAPASTGPTVSTAD------VTSPTPAGTTSGASPVTPSPSPRDNGTESK- 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1278 niGRNQPSPQAGLAGPGPagyGAARPTiPAragvisapqsqarvcAGRPTPDSQSkPSETLKGPAVLPEPLKPQAAFPqQ 1357
Cdd:pfam05109  503 --APDMTSPTSAVTTPTP---NATSPT-PA---------------VTTPTPNATS-PTLGKTSPTSAVTTPTPNATSP-T 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1358 PSLPTPAQKLQDPLVPIAAPTMPPSGPQPNLETppqppprsrssqSLPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLS 1437
Cdd:pfam05109  560 PAVTTPTPNATIPTLGKTSPTSAVTTPTPNATS------------PTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATS 627
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1438 lsvlAVSKAQPSVQISPV--LTPDPKMLIQLPSASQSQvNPLSSVSCMPTRPPGPEESKSQESMGSSANPFPSLPCRNP- 1514
Cdd:pfam05109  628 ----AVTTGQHNITSSSTssMSLRPSSISETLSPSTSD-NSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPr 702
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907115283 1515 --FTDRTAAPGNPfRVQSQESEATswLSKEEPvPNSPFPPLMPLSHDTS---------KASSSLGG 1569
Cdd:pfam05109  703 pgTTSQASGPGNS-STSTKPGEVN--VTKGTP-PKNATSPQAPSGQKTAvptvtstggKANSTTGG 764
RRM smart00360
RNA recognition motif;
1050-1105 1.81e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.81e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907115283  1050 DDALIDELLRQFAHFGEVILIRFVEDKMW--------VTFLEGSSALNALS-LNGKELLNRTITI 1105
Cdd:smart00360    9 PDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1171-1510 7.99e-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: 40.91  E-value: 7.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1171 PSSSSGLGTSPSSSPRtspcqSPTVPEYSAPSLP---IRPSRAPS-RTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPP 1246
Cdd:NF033839   147 SSSSSSSGSSTKPETP-----QPENPEHQKPTTPapdTKPSPQPEgKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHH 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1247 PRPVAPPARPAPPQRPPPPSAPKSP------------GTARK--DNIGRNQPSPQAGLAGPGPAGYGAARPTIPaRAGVI 1312
Cdd:NF033839   222 LQKEKHRQIVALIKELDELKKQALSeidnvntkveieNTVHKifADMDAVVTKFKKGLTQDTPKEPGNKKPSAP-KPGMQ 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1313 SAPQSQARVCAGRP-TPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQdplvpiaaPTMPPSGPQPNLETp 1391
Cdd:NF033839   301 PSPQPEKKEVKPEPeTPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQ--------PEKPKPEVKPQPEK- 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1392 pqppprsrssqslpsdssPQLQVKINgisGVKQEPTLKSDPfedlslsvlavSKAQPSVQISPVlTPDPKMLIQlPSASQ 1471
Cdd:NF033839   372 ------------------PKPEVKPQ---PETPKPEVKPQP-----------EKPKPEVKPQPE-KPKPEVKPQ-PEKPK 417
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907115283 1472 SQVNPlssvscmPTRPPGPEESKSQESMGSSANPFPSLP 1510
Cdd:NF033839   418 PEVKP-------QPEKPKPEVKPQPEKPKPEVKPQPEKP 449
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
672-1007 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 1907115283  672 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 751
Cdd:cd09098      1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 831
Cdd:cd09098     81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  832 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 911
Cdd:cd09098    161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  912 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 991
Cdd:cd09098    241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                          330
                   ....*....|....*.
gi 1907115283  992 ELKTSDHRPVVALIDI 1007
Cdd:cd09098    321 ELKTSDHRPVVALIDI 336
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
672-1007 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 1907115283  672 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQ-EFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLW 750
Cdd:cd09089      1 LRVFVGTWNVNGGKHFRSIAFKHQSMTDWLLDNPKLAGQCsNDSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKEW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  751 AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFA 830
Cdd:cd09089     81 GEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  831 AGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFR 910
Cdd:cd09089    161 AGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  911 GFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDllnasfqdeSKILYTWTPGTLLHYGR 990
Cdd:cd09089    241 GFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPSDKTEESLV---------ETNDPTWNPGTLLYYGR 311
                          330
                   ....*....|....*..
gi 1907115283  991 AELKTSDHRPVVALIDI 1007
Cdd:cd09089    312 AELKTSDHRPVVAIIDI 328
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
672-1007 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 1907115283  672 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 751
Cdd:cd09099      1 TRVAMGTWNVNGGKQFRSNILGTSELTDWLLDSPKLSGTPDFQDDESNPPDIFAVGFEEMVELSAGNIVNASTTNRKMWG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 831
Cdd:cd09099     81 EQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  832 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 911
Cdd:cd09099    161 GQNQVKERNEDYKEITQKLSFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKD 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  912 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 991
Cdd:cd09099    241 FHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWRKKWPFEKTAGEINLLDSDLDFDTKIRHTWTPGALMYYGRA 320
                          330
                   ....*....|....*.
gi 1907115283  992 ELKTSDHRPVVALIDI 1007
Cdd:cd09099    321 ELQASDHRPVLAIVEV 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
670-1010 4.68e-127

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: 4.68e-127
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   670 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKL 749
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   750 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 829
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   830 AAGQSQVKERNEDFVEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 906
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283   907 QIFRGFLEGKVTFAPTYKYDLF-SEDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 985
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 1907115283   986 lHYGRAELKTSDHRPVVALIDIDIF 1010
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
672-1007 1.56e-106

Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases.


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 341.62  E-value: 1.56e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  672 IRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLDAPklagiqefqdkrSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 751
Cdd:cd09074      1 VKIFVVTWNVGGGI------SPPENLENWLSPKG------------TEAPDIYAVGVQEVDMSVQGFVGNDDSAKAREWV 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAV--DTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 829
Cdd:cd09074     63 DNIQEALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVegVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHL 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  830 AAGQSQVKERNEDFVEIARKLSFPMG----RMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNA 905
Cdd:cd09074    143 AAGQEEVERRNQDYRDILSKLKFYRGdpaiDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEK 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  906 GQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdeskilYTWTPGTL 985
Cdd:cd09074    223 GKVFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKS--------------------------KAGSEIQP 276
                          330       340
                   ....*....|....*....|...
gi 1907115283  986 LHYGRAEL-KTSDHRPVVALIDI 1007
Cdd:cd09074    277 LSYTSVPLyKTSDHKPVRATFRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
672-1003 3.40e-104

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: 3.40e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  672 IRVCVGTWNVNGgkqfrsiAFKNQTLTDWLldapklagiqeFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 751
Cdd:cd09090      1 INIFVGTFNVNG-------KSYKDDLSSWL-----------FPEENDELPDIVVIGLQEVVELTAGQILNSDPSKSSFWE 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 829
Cdd:cd09090     63 KKIKTTLNGrgGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHL 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  830 AAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIF 909
Cdd:cd09090    143 AAGLTNYEERNNDYKTIARGLRFSRGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVF 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  910 RGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsAEDLDLLNasfqdeskilytwtpgtllhYG 989
Cdd:cd09090    223 PGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYR---------GENLRQLS--------------------YN 273
                          330
                   ....*....|....
gi 1907115283  990 RAELKTSDHRPVVA 1003
Cdd:cd09090    274 SAPLRFSDHRPVYA 287
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
672-1007 2.74e-99

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: 2.74e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  672 IRVCVGTWNVNGGKqfrsiafKNQTLTDWLldapklagiqefqDKRSKPTDIFAIGFEEmVELNAGNIVNASTTNQKLWA 751
Cdd:cd09093      1 FRIFVGTWNVNGQS-------PDESLRPWL-------------SCDEEPPDIYAIGFQE-LDLSAEAFLFNDSSREQEWV 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 831
Cdd:cd09093     60 KAVERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  832 GQSQVKERNEDFVEIARKLSFPMG----RMLFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQKNAG 906
Cdd:cd09093    140 HMEEVERRNQDYKDICARMKFEDPdgppLSISDHDVVFWLGDLNYRIqELPTEEVKELIEKNDLEELLKYDQLNIQRRAG 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  907 QIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedldllnasfqdESKIlytwtpgTLL 986
Cdd:cd09093    220 KVFEGFTEGEINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWR----------------------GTNI-------VQL 270
                          330       340
                   ....*....|....*....|..
gi 1907115283  987 HYGR-AELKTSDHRPVVALIDI 1007
Cdd:cd09093    271 SYRShMELKTSDHKPVSALFDI 292
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
204-627 1.80e-94

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 317.79  E-value: 1.80e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 274
Cdd:COG5329     61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  275 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 345
Cdd:COG5329    137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  346 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 425
Cdd:COG5329    216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  426 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 505
Cdd:COG5329    295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  506 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 583
Cdd:COG5329    374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907115283  584 YAGTGALEGKAK-------AGKLKDGARSVTRTIQNNFFDSSKQEAIDVLL 627
Cdd:COG5329    451 YTGTGALKSSFTrrgrrsfAGALNDFIKSFSRYYINNFTDGQRQDAIDLLL 501
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
204-484 1.10e-86

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: 1.10e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISL---------RVDASDEDRI-SEVRKVLNSGNFY 273
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGGPIYKITDVEFIPLnsslydsssKSKSPDEARLlKLLKLFLSSGSFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  274 FAWSasgvsLDLS------LNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACL 347
Cdd:pfam02383   77 FSYD-----YDLTnslqrnSTTSRSPSFDSLDERFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  348 ISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDC-----VSSFIQIRGSVPLFWEQ-PGLQVGSHRVRMSRgFEA 421
Cdd:pfam02383  152 ISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTGnsegkIFSFVQIRGSIPLFWSQdPNLKYSKPKIQITR-PEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907115283  422 NAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKAS--EHASDIHMVSFDYHQMVK 484
Cdd:pfam02383  231 TQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEKAVKYLnqFLPDKLRYTAFDFHHECK 295
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
673-1007 1.02e-71

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: 1.02e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  673 RVCVGTWNVnggkqfrSIAFKNQTLTdwlldapKLAGIQEFQDKrskpTDIFAIGFEEmvelnagniVNASTTNQKL--- 749
Cdd:cd09094      2 RVYVVTWNV-------ATAPPPIDVR-------SLLGLQSPEVA----PDIYIIGLQE---------VNSKPVQFVSdli 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  750 ----WAvELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFV 825
Cdd:cd09094     55 fddpWS-DLFMDILSPKGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFL 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  826 CSHFAAGQSQVKERNEDFVEIARKLSFPMGRM--LFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQ 902
Cdd:cd09094    134 NCHLPAHMEKWEQRIDDFETILSTQVFNECNTpsILDHDYVFWFGDLNFRIeDVSIEFVRELVNSKKYHLLLEKDQLNMA 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  903 KNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedLDLLNASFQDESKIlytwtp 982
Cdd:cd09094    214 KRKEEAFQGFQEGPLNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWK------------VNPDASTEEKFLSI------ 275
                          330       340
                   ....*....|....*....|....*.
gi 1907115283  983 gTLLHY-GRAELKTSDHRPVVALIDI 1007
Cdd:cd09094    276 -TQTSYkSHMEYGISDHKPVTAQFRL 300
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
665-1033 1.84e-68

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 238.91  E-value: 1.84e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  665 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVNA 742
Cdd:COG5411     23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  743 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 817
Cdd:COG5411     84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  818 HTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 895
Cdd:COG5411    163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  896 GDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 975
Cdd:COG5411    243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907115283  976 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIA--VQGPPDG 1033
Cdd:COG5411    299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
1006-1147 4.30e-63

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


Pssm-ID: 286093  Cd Length: 146  Bit Score: 211.21  E-value: 4.30e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1006 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 1084
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907115283 1085 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEMSLEKIS-VTLPSSASSTLLGEDAEVAAD 1147
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIILCTDNtIPVSPCANSTLLAEDFDFGSP 144
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
670-1007 1.95e-56

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: 198.42  E-value: 1.95e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  670 KKIRVCVGTWNVNGGKQFrsiafkNQTLTDWLLdapklAGIQEFQdkrskpTDIFAIGFEEmvelnagnivnaSTTNQKL 749
Cdd:cd09095      3 RNVGIFVATWNMQGQKEL------PENLDDFLL-----PTSADFA------QDIYVIGVQE------------GCSDRRE 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  750 WAVELQKTISrdNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 829
Cdd:cd09095     54 WEIRLQETLG--PSHVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHF 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  830 AAGQSQVKERNEDFVEIARKLSFPmgRMLFSHDY-------------VFWCGDFNYRIDLPNEEVKELIRQ---QNWDSL 893
Cdd:cd09095    132 TSGDGKVKERVLDYNKIIQALNLP--RNVPTNPYksesgdvttrfdeVFWFGDFNFRLSGPRHLVDALINQgqeVDVSAL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  894 IAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRkwpfdrsaedldllnasfqde 973
Cdd:cd09095    210 LQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSR--------------------- 268
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907115283  974 skilytwTPGTL--LHYGRAE-LKTSDHRPVVALIDI 1007
Cdd:cd09095    269 -------QKGDVccLKYNSCPsIKTSDHRPVFALFRV 298
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
763-1022 1.59e-49

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


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 187.42  E-value: 1.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  763 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 840
Cdd:PLN03191   363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  841 EDFVEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLE 914
Cdd:PLN03191   443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  915 GKVTFAPTYKYDLFSEDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 989
Cdd:PLN03191   523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907115283  990 RAELKTSDHRPVVALIDIdifEVEAEERQKIYK 1022
Cdd:PLN03191   574 RSEIRLSDHRPVSSMFLV---EVEVFDHRKLQR 603
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
672-950 6.31e-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: 6.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  672 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivnaSTTNQKL 749
Cdd:cd09100      1 ITIFIGTWNMGNAPPPKKI-------TSWFQCK----GQGKTRDDTADyiPHDIYVIGTQE------------DPLGEKE 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  750 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 827
Cdd:cd09100     58 WLDTLKHSLREitSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNS 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  828 HFAAGQSQVKERNEDFVEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKEL---IRQQNWDSLIAGDQL 899
Cdd:cd09100    138 HLTSGSEKKLRRNQNYFNILRFLVLgdkKLSPFNITHrfTHLFWLGDLNYRVELPNTEAENIiqkIKQQQYQELLPHDQL 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907115283  900 INQKNAGQIFRGFLEGKVTFAPTYKYD-------LFSEDYDTSEKCRTPAWTDRVLWR 950
Cdd:cd09100    218 LIERKESKVFLQFEEEEITFAPTYRFErgtreryAYTKQKATGMKYNLPSWCDRVLWK 275
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
672-1007 2.34e-40

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and -2, and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D), and SHIP2 (also known as INPPL1). It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Both SHIP1 and -2 catalyze the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP1 also converts inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4] to inositol-1,3,4-polyphosphate [I(1,3,4)P3]. SHIP1 and SHIP2 have little overlap in their in vivo functions. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. SHIP2 is as an inhibitor of the insulin signaling pathway, and is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD), while SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif, and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate gene for conferring a predisposition for type 2 diabetes.


Pssm-ID: 197325  Cd Length: 307  Bit Score: 152.02  E-value: 2.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  672 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDAPKLAGIQEFQDkrSKPTDIFAIGFEEmvelnagnivnaSTTNQKLWA 751
Cdd:cd09091      1 ISIFIGTWNMGSAPPPKNI-------TSWFTSKGQGKTRDDVAD--YIPHDIYVIGTQE------------DPLGEKEWL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  752 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 829
Cdd:cd09091     60 DLLRHSLKEltSLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  830 AAGQSQVKERNEDFVEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKELI---RQQNWDSLIAGDQLIN 901
Cdd:cd09091    140 TSGSEKKLRRNQNYLNILRFLSLgdkKLSAFNITHrfTHLFWLGDLNYRLDLPIQEAENIIqkiEQQQFEPLLRHDQLNL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  902 QKNAGQIFRGFLEGKVTFAPTYKYDLFSEDY-------DTSEKCRTPAWTDRVLWrrrkwpfdRSAEDLDLLNASFQDES 974
Cdd:cd09091    220 EREEHKVFLRFSEEEITFPPTYRYERGSRDTyaytkqkATGVKYNLPSWCDRILW--------KSYPETHIICQSYGCTD 291
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1907115283  975 KILytwtpgtllhygraelkTSDHRPVVALIDI 1007
Cdd:cd09091    292 DIV-----------------TSDHSPVFGTFEV 307
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
1032-1108 2.28e-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: 141.00  E-value: 2.28e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907115283 1032 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 1108
Cdd:cd12719      1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
672-950 4.52e-39

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


Pssm-ID: 197335  Cd Length: 304  Bit Score: 148.20  E-value: 4.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  672 IRVCVGTWNVNGGKQFRSiafknqtLTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivnaSTTNQKL 749
Cdd:cd09101      1 ISIFIGTWNMGSVPPPKS-------LASWLTSR----GLGKTLDETTVtiPHDIYVFGTQE------------NSVGDRE 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  750 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 827
Cdd:cd09101     58 WVDFLRASLKEltDIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNC 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  828 HFAAGQSQVKERNEDFVEIARKLSFPMGR-------MLFSHdyVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLI 900
Cdd:cd09101    138 HLTSGNEKTHRRNQNYLDILRSLSLGDKQlnafdisLRFTH--LFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLN 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907115283  901 NQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRT-------PAWTDRVLWR 950
Cdd:cd09101    216 LEREKNKVFLRFREEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILWK 272
RRM_SYNJ cd12440
RNA recognition motif (RRM) found in synaptojanin-1, synaptojanin-2 and similar proteins; This ...
1032-1108 2.51e-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: 117.91  E-value: 2.51e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907115283 1032 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 1108
Cdd:cd12440      1 DATVVVSLDSKSEEWNEFEDALIGELLRVLASYGDVVLVRFAHEGMLVTFRDGRSALAALALNGKQILGRTLKIRLK 77
RRM_SYNJ2 cd12720
RNA recognition motif (RRM) found in synaptojanin-2 and similar proteins; This subgroup ...
1032-1105 1.36e-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: 1.36e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907115283 1032 DGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITI 1105
Cdd:cd12720      1 DATVVVNLLSpTLEEKNDFPEDLSTELVQCFQSYGTVILVRFNRGQMLVTFEDSRSALRVLDLDGIKVNGRAVKI 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
1193-1572 1.75e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1193 PTVPEYSA-PSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPArpappqrppPPSAPKSP 1271
Cdd:PHA03247  2589 PDAPPQSArPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER---------PRDDPAPG 2659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1272 GTARKDNIGRNQPSPQAG--LAGPGPAgygAARPTIPARAGVISAPQsqarvcagrPTPDSQSKPSETLKGPAVLPEPLK 1349
Cdd:PHA03247  2660 RVSRPRRARRLGRAAQASspPQRPRRR---AARPTVGSLTSLADPPP---------PPPTPEPAPHALVSATPLPPGPAA 2727
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1350 PQAAFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNLeTPPQPPPRSRSSQSLPSDSSPQL 1412
Cdd:PHA03247  2728 ARQASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL-TRPAVASLSESRESLPSPWDPAD 2806
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1413 QVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqLPSASQSQVNPLSSVSCMPTRPPGPEE 1492
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPAAKPAAPARPPV 2883
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1493 SK-SQESMGSSANPFPsLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPLShDTSKASSSLGGFE 1571
Cdd:PHA03247  2884 RRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTT-DPAGAGEPSGAVP 2960

                   .
gi 1907115283 1572 D 1572
Cdd:PHA03247  2961 Q 2961
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
779-876 1.26e-06

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


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 51.33  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  779 VFIRPqhaPFIRDVAVDTVKTGMGgATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFpmgRML 858
Cdd:cd08372     71 ILSKT---PKFKIVEKHQYKFGEG-DSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKR---LRQ 143
                           90
                   ....*....|....*...
gi 1907115283  859 FSHDYVFWCGDFNYRIDL 876
Cdd:cd08372    144 PNSAPVVICGDFNVRPSE 161
PHA03247 PHA03247
large tegument protein UL36; Provisional
1284-1565 1.86e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 1.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1284 PSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVcAGRPTPDSQSKPSETlKGPAVLPEPLKPQAAF----PQQPS 1359
Cdd:PHA03247  2720 PLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP-ARPPTTAGPPAPAPP-AAPAAGPPRRLTRPAVaslsESRES 2797
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1360 LPTPAQKLQDPL-VPIAAPTMPPSG-PQPNLETPPQPPPRSRSSQSLPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLS 1437
Cdd:PHA03247  2798 LPSPWDPADPPAaVLAPAAALPPAAsPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1438 LSVLAVSK-AQPSVQISP---VLTPD-PKMLIQLPSASQSQVNPLSSVSCMPT---RPPGPEESKSQESMGSSANPFPSL 1509
Cdd:PHA03247  2878 PARPPVRRlARPAVSRSTesfALPPDqPERPPQPQAPPPPQPQPQPPPPPQPQpppPPPPRPQPPLAPTTDPAGAGEPSG 2957
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907115283 1510 PCRNPFTDrTAAPGNPFRVQSQESEATSwlSKEEPVPNSPFPPLMPLSHDTSKASS 1565
Cdd:PHA03247  2958 AVPQPWLG-ALVPGRVAVPRFRVPQPAP--SREAPASSTPPLTGHSLSRVSSWASS 3010
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
816-1001 2.19e-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: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  816 LFHTTSLCFVCSHFAAGQSQVKERNEDFVeIARKLSFPMGRMLFshdYVFwcGDFNYRIDL------------------- 876
Cdd:cd09092    176 LFHDASNLAACESSPSVYSQNRHRALGYV-LERLTDERFEKVPF---FVF--GDFNFRLDTksvvetlcakatmqtvrka 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  877 -PNEEVKELIRQQNWD----------SLIAGDQLINQKNAGQIFRGF-----------LEGKVTFAPTYKYdlfSEDYDT 934
Cdd:cd09092    250 dSNIVVKLEFREKDNDnkvvlqiekkKFDYFNQDVFRDNNGKALLKFdkelevfkdvlYELDISFPPSYPY---SEDPEQ 326
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283  935 SE---KCRTPAWTDRVLwrrrkwpFDRSAEDLDLLNasfqDESKILYTwtpgtllHYGRaELKTSDHRPV 1001
Cdd:cd09092    327 GTqymNTRCPAWCDRIL-------MSHSARELKSEN----EEKSVTYD-------MIGP-NVCMGDHKPV 377
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1192-1386 2.80e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1192 SPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSAPKSP 1271
Cdd:PRK07764   596 GGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1272 GTarkdniGRNQPSPQAGLAGPGPAGyGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQ 1351
Cdd:PRK07764   676 AA------PAAPPPAPAPAAPAAPAG-AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907115283 1352 AAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQP 1386
Cdd:PRK07764   749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PHA03378 PHA03378
EBNA-3B; Provisional
1111-1525 3.53e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.52  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1111 DWIKHLEEEMSLEKISVTLPSSASSTLLGEDAEVA--ADFDMEGDvddysaEVEELLPQHLQPSSSSGLGTSPSSSPRts 1188
Cdd:PHA03378   507 DLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPCVytEDLDIESD------EPASTEPVHDQLLPAPGLGPLQIQPLT-- 578
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1189 pcqSPTVPEY--SAPSLPIRPSRA--PSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPP------------------ 1246
Cdd:PHA03378   579 ---SPTTSQLasSAPSYAQTPWPVphPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRmqpitfnvlvfptphqpp 655
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1247 -PRPVAPPARPAPPQRPPPPSAPKSPGTARKDNI--GRNQPSPQAGLAGPGPAGY-GAARP--TIPARAGVISAPQSQAR 1320
Cdd:PHA03378   656 qVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWapGTMQPPPRAPTPMRPPAAPpGRAQRpaAATGRARPPAAAPGRAR 735
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1321 VCAGRPTPDSQSKPSET-LKGPAVLPEPLKPQAAFP------QQPSL-PTPAQKLQDPLVPIAAPTMPPSG-----PQPN 1387
Cdd:PHA03378   736 PPAAAPGRARPPAAAPGrARPPAAAPGRARPPAAAPgaptpqPPPQApPAPQQRPRGAPTPQPPPQAGPTSmqlmpRAAP 815
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1388 LETPPQPPPRSRSSQSLPSDSSPQLQVKingISGVKQEPT-LKSDPFEDLSLSVLavskaQPSVQISPVLTPdpkmlIQL 1466
Cdd:PHA03378   816 GQQGPTKQILRQLLTGGVKRGRPSLKKP---AALERQAAAgPTPSPGSGTSDKIV-----QAPVFYPPVLQP-----IQV 882
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907115283 1467 PSASQSqVNPLSSvscmPTRPPGPEESKSQESMGSSANPFPSLPCRNPFTDRTAAPGNP 1525
Cdd:PHA03378   883 MRQLGS-VRAAAA----STVTQAPTEYTGERRGVGPMHPTDIPPSKRAKTDAYVESQPP 936
PHA03247 PHA03247
large tegument protein UL36; Provisional
1193-1578 7.31e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 7.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1193 PTVPEYSAPSLPIRPSRAPSRTPgPPSSQGSPVDTQPAAQKDSS--QTLEPKRPPPPRPVAPPARPAPPQRPPPPSAPKS 1270
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAP-HALVSATPLPPGPAAARQASpaLPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1271 PGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKP 1350
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1351 QAAF--------------PQQPSLPTPAQKLQDPLVPIAAPTMPPSG---PQPNLEtppqppprsrssqslpsdssPQLQ 1413
Cdd:PHA03247  2849 SLPLggsvapggdvrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQ--------------------PERP 2908
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1414 vkingisgvkQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMLIQLPSASQSQVNPLSSVSCMPTRPPGPEES 1493
Cdd:PHA03247  2909 ----------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1494 KSQesmgssanPFPSLPcrnpftdrTAAPGNPFRVQSQESEATSWLSK----EEPVPnspfPPL-------MPLSHDTSK 1562
Cdd:PHA03247  2979 VPQ--------PAPSRE--------APASSTPPLTGHSLSRVSSWASSlalhEETDP----PPVslkqtlwPPDDTEDSD 3038
                          410
                   ....*....|....*.
gi 1907115283 1563 ASSSLGGFEDNFDLQS 1578
Cdd:PHA03247  3039 ADSLFDSDSERSDLEA 3054
RRM3_Prp24 cd12298
RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar ...
1054-1107 7.49e-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: 7.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907115283 1054 IDELLRQFAHFGEV---ILIRFVEDKM--------WVTFLEGSSALNALSLNGKELLNRTITITL 1107
Cdd:cd12298     14 EEALRGIFEKFGEIesiNIPKKQKNRKgrhnngfaFVTFEDADSAESALQLNGTLLDNRKISVSL 78
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1199-1569 1.57e-04

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: 46.45  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1199 SAPSLPIRPSRAPSRTPGPPSSQGSPVD-TQPAAQKDSSQTLEpkrpppPRPVAPPARPAPPQRPPPPSAPKSPGTARKd 1277
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSSTHVPTNlTAPASTGPTVSTAD------VTSPTPAGTTSGASPVTPSPSPRDNGTESK- 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1278 niGRNQPSPQAGLAGPGPagyGAARPTiPAragvisapqsqarvcAGRPTPDSQSkPSETLKGPAVLPEPLKPQAAFPqQ 1357
Cdd:pfam05109  503 --APDMTSPTSAVTTPTP---NATSPT-PA---------------VTTPTPNATS-PTLGKTSPTSAVTTPTPNATSP-T 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1358 PSLPTPAQKLQDPLVPIAAPTMPPSGPQPNLETppqppprsrssqSLPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLS 1437
Cdd:pfam05109  560 PAVTTPTPNATIPTLGKTSPTSAVTTPTPNATS------------PTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATS 627
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1438 lsvlAVSKAQPSVQISPV--LTPDPKMLIQLPSASQSQvNPLSSVSCMPTRPPGPEESKSQESMGSSANPFPSLPCRNP- 1514
Cdd:pfam05109  628 ----AVTTGQHNITSSSTssMSLRPSSISETLSPSTSD-NSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPr 702
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907115283 1515 --FTDRTAAPGNPfRVQSQESEATswLSKEEPvPNSPFPPLMPLSHDTS---------KASSSLGG 1569
Cdd:pfam05109  703 pgTTSQASGPGNS-STSTKPGEVN--VTKGTP-PKNATSPQAPSGQKTAvptvtstggKANSTTGG 764
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
1055-1105 1.80e-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: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907115283 1055 DELLRQFAHFGEVILIRFVEDKM-------WVTFLEGSSALNALS-LNGKELLNRTITI 1105
Cdd:cd00590     13 EDLRELFSKFGEVVSVRIVRDRDgkskgfaFVEFESPEDAEKALEaLNGTELGGRPLKV 71
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1204-1384 2.15e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1204 PIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSAPKSPGTArkdniGRNQ 1283
Cdd:PRK12323   374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP-----GGAP 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1284 PSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSqSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTP 1363
Cdd:PRK12323   449 APAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDD-PPPWEELPPEFASPAPAQPDAAPAGWVAESIP 527
                          170       180
                   ....*....|....*....|.
gi 1907115283 1364 AQKLQDPLVPIAAPTMPPSGP 1384
Cdd:PRK12323   528 DPATADPDDAFETLAPAPAAA 548
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1284-1386 2.19e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1284 PSPQAGlAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTP 1363
Cdd:PRK07764   392 GAPAAA-APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAP 470
                           90       100
                   ....*....|....*....|...
gi 1907115283 1364 AQKLQDPLVPIAAPTMPPSGPQP 1386
Cdd:PRK07764   471 AAAPEPTAAPAPAPPAAPAPAAA 493
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1190-1569 1.38e-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: 43.60  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1190 CQSPTVPEYSAPslPIRPSRAPSRTPgPPSSQGSPVDTQPAaqkdssqtlepkrpppprpvapparpappQRPPPPSAPK 1269
Cdd:pfam03154  176 AQSGAASPPSPP--PPGTTQAATAGP-TPSAPSVPPQGSPA-----------------------------TSQPPNQTQS 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1270 SPGTARKDNIGRNQPSPQagLAGPGPAGYGAARPTIPARAGVISAPQSQARvCAGRPTPDS-QSKPSETLKGPAVLPEPL 1348
Cdd:pfam03154  224 TAAPHTLIQQTPTLHPQR--LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLH-GQMPPMPHSlQTGPSHMQHPVPPQPFPL 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1349 KPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMP-PSGPQPNLEtppqppprsrssQSLPSDSSPQLQVKINGISGVKQEPT 1427
Cdd:pfam03154  301 TPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSqLQSQQPPRE------------QPLPPAPLSMPHIKPPPTTPIPQLPN 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1428 LKSDPFEDlslsvlAVSKAQPsVQISPVLTPDP--KMLIQL-----PSA--------SQSQVNPLSsvscmPTRPPGPEE 1492
Cdd:pfam03154  369 PQSHKHPP------HLSGPSP-FQMNSNLPPPPalKPLSSLsthhpPSAhppplqlmPQSQQLPPP-----PAQPPVLTQ 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1493 SKSQESMGSSANPFPSL---PCRNPFTDRTAAPGNPfrvqsqeseaTSWLSKEEPVPNSpfPPLMPLSHDTSKASSSLGG 1569
Cdd:pfam03154  437 SQSLPPPAASHPPTSGLhqvPSQSPFPQHPFVPGGP----------PPITPPSGPPTST--SSAMPGIQPPSSASVSSSG 504
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1284-1386 1.40e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1284 PSPQAGLAGPGPAGYGAARPtiPARAGVISAPQSQArvcagRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTP 1363
Cdd:PRK07764   406 PAAAPAPAAAAPAAAAAPAP--AAAPQPAPAPAPAP-----APPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTA 478
                           90       100
                   ....*....|....*....|...
gi 1907115283 1364 AQklqdplVPIAAPTMPPSGPQP 1386
Cdd:PRK07764   479 AP------APAPPAAPAPAAAPA 495
PHA03247 PHA03247
large tegument protein UL36; Provisional
1285-1672 1.51e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1285 SPQAGlaGPGPAGYGAARPTIPARagviSAPQSQarvCAGRPT-PDSQSKPSEtlkgPAVLPEPLKPQAafPQQPSLPTP 1363
Cdd:PHA03247  2545 SDDAG--DPPPPLPPAAPPAAPDR----SVPPPR---PAPRPSePAVTSRARR----PDAPPQSARPRA--PVDDRGDPR 2609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1364 AQKLQDPLVP-IAAPTMPPSGPQPnletppqpppRSRSSQSLPSDSSPQLQVKINGISGVKqeptlksdpfedLSLSVLA 1442
Cdd:PHA03247  2610 GPAPPSPLPPdTHAPDPPPPSPSP----------AANEPDPHPPPTVPPPERPRDDPAPGR------------VSRPRRA 2667
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1443 VSKAQPSVQISPVLTPDPKmliqlpsASQSQVNPLSSVSCMPTRPPGPEES-----------KSQESMGSSANPFPSLPC 1511
Cdd:PHA03247  2668 RRLGRAAQASSPPQRPRRR-------AARPTVGSLTSLADPPPPPPTPEPAphalvsatplpPGPAAARQASPALPAAPA 2740
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1512 RNPFTDRTAAPGNPFRVQSQESEATswlskeepvPNSPFPPLMPLSHDTSKASSSLGGfednfdlqSQSTVKTSNPKGWV 1591
Cdd:PHA03247  2741 PPAVPAGPATPGGPARPARPPTTAG---------PPAPAPPAAPAAGPPRRLTRPAVA--------SLSESRESLPSPWD 2803
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1592 TFDeddnfpttgksksvcPDLVGNAPASFDDDWSKGASVSfcvlparrpppppppvpllPPGTTSSAGPSTTLPSKAPST 1671
Cdd:PHA03247  2804 PAD---------------PPAAVLAPAAALPPAASPAGPL-------------------PPPTSAQPTAPPPPPGPPPPS 2849

                   .
gi 1907115283 1672 L 1672
Cdd:PHA03247  2850 L 2850
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1283-1516 1.80e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1283 QPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKP------SETLKGPAVLPEPLKPQAAFPQ 1356
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAaravaaAPARRSPAPEALAAARQASARG 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1357 QPSLPTPAQKLQDPLVPIAAPTMPPSGPQPNLETPPQPPPRSRSSQSLPSDSSPqlqvkingisgvkqeptlksdPFEDL 1436
Cdd:PRK12323   444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP---------------------PWEEL 502
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1437 SLSVLAVSKAQPSVQISPV---LTPDPKMLIQLPSASQSQVNPLSSVSCMPTRPPGPEESKSQESMGSSANP------FP 1507
Cdd:PRK12323   503 PPEFASPAPAQPDAAPAGWvaeSIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPdmfdgdWP 582

                   ....*....
gi 1907115283 1508 SLPCRNPFT 1516
Cdd:PRK12323   583 ALAARLPVR 591
RRM smart00360
RNA recognition motif;
1050-1105 1.81e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.81e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907115283  1050 DDALIDELLRQFAHFGEVILIRFVEDKMW--------VTFLEGSSALNALS-LNGKELLNRTITI 1105
Cdd:smart00360    9 PDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1283-1522 1.84e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1283 QPSPQAGLAGPGPAGYGAarptiPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPlkpqAAFPQQPSLPT 1362
Cdd:PRK10263   318 EPVAVAAAATTATQSWAA-----PVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAP----EGYPQQSQYAQ 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1363 PAQKLQDPLvpiaaptMPPSGPQPNLETPPQPPPRSRSSQSLPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLSLSVLA 1442
Cdd:PRK10263   389 PAVQYNEPL-------QQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQST 461
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1443 VSKAQPSVQisPVlTPDPKMLIQLPSASQSQVNPLSSV-SCMPTRPP-------GPEESKSQESMGSSANPFPSlPCRNP 1514
Cdd:PRK10263   462 YQTEQTYQQ--PA-AQEPLYQQPQPVEQQPVVEPEPVVeETKPARPPlyyfeevEEKRAREREQLAAWYQPIPE-PVKEP 537

                   ....*...
gi 1907115283 1515 FTDRTAAP 1522
Cdd:PRK10263   538 EPIKSSLK 545
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1271-1387 2.07e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1271 PGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKP 1350
Cdd:PHA03307   813 SRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAA 892
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907115283 1351 QAAFPQQPSLPTPAQKLQDPLVPiaaptMPPSGPQPN 1387
Cdd:PHA03307   893 AAAPPAGAPAPRPRPAPRVKLGP-----MPPGGPDPR 924
RRM2_SREK1 cd12260
RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 ...
1055-1106 3.51e-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: 3.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907115283 1055 DELLRQFAHFGEVILIRFVEDK------MWVTFLEGSSALNALSLNGKELLNRTITIT 1106
Cdd:cd12260     19 DQLLEFFSQAGEVKYVRMAGDEtqptryAFVEFAEQTSVINALKLNGKMFGGRPLKVN 76
PHA03247 PHA03247
large tegument protein UL36; Provisional
1193-1507 5.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1193 PTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTlepkrpppprpvapparpappqrPPPPSApkspg 1272
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP-----------------------PPGPPP----- 2847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1273 tarkdnigrnQPSPQAGLAGPG-------PAGYGAARPTIPARAGVISAPQSQArvcagRPTPDSQSKPSEtlkGPAVLP 1345
Cdd:PHA03247  2848 ----------PSLPLGGSVAPGgdvrrrpPSRSPAAKPAAPARPPVRRLARPAV-----SRSTESFALPPD---QPERPP 2909
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1346 EPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPP-SGPQPNLETPPQPPPRSRSSQSLPSDSSPQLQVKINGISgvKQ 1424
Cdd:PHA03247  2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPtTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS--RE 2987
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1425 EPTLKSDPFEDLSLSvlAVSKAQPSVQISPVLTPDPKMLIQ---LPS-----------ASQSQVNPLSSVSCMPTRP--- 1487
Cdd:PHA03247  2988 APASSTPPLTGHSLS--RVSSWASSLALHEETDPPPVSLKQtlwPPDdtedsdadslfDSDSERSDLEALDPLPPEPhdp 3065
                          330       340
                   ....*....|....*....|....*.
gi 1907115283 1488 ------PGPEESKSQESMGSSANPFP 1507
Cdd:PHA03247  3066 fahepdPATPEAGARESPSSQFGPPP 3091
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1284-1381 6.73e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1284 PSPQAGLAGPGPAGYGAARPTIparagvisAPQSQARVCAGRPTPDSQSKPsETLKGPAVLPEPLKPQAAFPQQPSLPTP 1363
Cdd:PRK14950   362 PVPAPQPAKPTAAAPSPVRPTP--------APSTRPKAAAAANIPPKEPVR-ETATPPPVPPRPVAPPVPHTPESAPKLT 432
                           90
                   ....*....|....*...
gi 1907115283 1364 AQKLQDPLVPIAAPTMPP 1381
Cdd:PRK14950   433 RAAIPVDEKPKYTPPAPP 450
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1286-1386 7.19e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.91  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1286 PQAGLAGPGPAGygAARPTIPARAGVISAPQSQARVCAgrptpdSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPtpaq 1365
Cdd:PRK14971   363 TQKGDDASGGRG--PKQHIKPVFTQPAAAPQPSAAAAA------SPSPSQSSAAAQPSAPQSATQPAGTPPTVSVD---- 430
                           90       100
                   ....*....|....*....|.
gi 1907115283 1366 klqdplVPIAAPTMPPSGPQP 1386
Cdd:PRK14971   431 ------PPAAVPVNPPSTAPQ 445
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1420-1565 7.80e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 7.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1420 SGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqlPSASQSQVNPlssvsCMPTRPPGPEESKSQESM 1499
Cdd:PTZ00449   551 ETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEE----PKKPKRPRSA-----QRPTRPKSPKLPELLDIP 621
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907115283 1500 GSSANP-FPSLPCRNPFTDRTAAPGNPfrvqsqesEATSWLSKEEPvPNSPFPPLMP-----LSHDTSKASS 1565
Cdd:PTZ00449   622 KSPKRPeSPKSPKRPPPPQRPSSPERP--------EGPKIIKSPKP-PKSPKPPFDPkfkekFYDDYLDAAA 684
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1171-1510 7.99e-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: 40.91  E-value: 7.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1171 PSSSSGLGTSPSSSPRtspcqSPTVPEYSAPSLP---IRPSRAPS-RTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPP 1246
Cdd:NF033839   147 SSSSSSSGSSTKPETP-----QPENPEHQKPTTPapdTKPSPQPEgKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHH 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1247 PRPVAPPARPAPPQRPPPPSAPKSP------------GTARK--DNIGRNQPSPQAGLAGPGPAGYGAARPTIPaRAGVI 1312
Cdd:NF033839   222 LQKEKHRQIVALIKELDELKKQALSeidnvntkveieNTVHKifADMDAVVTKFKKGLTQDTPKEPGNKKPSAP-KPGMQ 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1313 SAPQSQARVCAGRP-TPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQdplvpiaaPTMPPSGPQPNLETp 1391
Cdd:NF033839   301 PSPQPEKKEVKPEPeTPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQ--------PEKPKPEVKPQPEK- 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907115283 1392 pqppprsrssqslpsdssPQLQVKINgisGVKQEPTLKSDPfedlslsvlavSKAQPSVQISPVlTPDPKMLIQlPSASQ 1471
Cdd:NF033839   372 ------------------PKPEVKPQ---PETPKPEVKPQP-----------EKPKPEVKPQPE-KPKPEVKPQ-PEKPK 417
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907115283 1472 SQVNPlssvscmPTRPPGPEESKSQESMGSSANPFPSLP 1510
Cdd:NF033839   418 PEVKP-------QPEKPKPEVKPQPEKPKPEVKPQPEKP 449
 
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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