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Conserved domains on  [gi|755554757|ref|XP_011244383|]
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synaptojanin-1 isoform X13 [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 ...
680-1015 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 755554757  680 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 759
Cdd:cd09098     1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 839
Cdd:cd09098    81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  840 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 919
Cdd:cd09098   161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  920 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 999
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                         330
                  ....*....|....*.
gi 755554757 1000 ELKTSDHRPVVALIDI 1015
Cdd:cd09098   321 ELKTSDHRPVVALIDI 336
COG5329 super family cl34984
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
204-627 1.78e-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: 1.78e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 274
Cdd:COG5329    61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  275 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 345
Cdd:COG5329   137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  346 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 425
Cdd:COG5329   216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  426 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 505
Cdd:COG5329   295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  506 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 583
Cdd:COG5329   374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755554757  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 ...
1014-1155 5.41e-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: 5.41e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1014 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 1092
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755554757  1093 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEMSLEKIS-VTLPSSASSTLLGEDAEVAAD 1155
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIILCTDNtIPVSPCANSTLLAEDFDFGSP 144
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1207-1567 5.43e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1207 SAPSLPIRPsRAPSRTPGPPSSQGSPVDTQPAAqkdssqtlepkrpppprpvapparpappqrPPPPSGRNQPSPQAGLA 1286
Cdd:PHA03247 2590 DAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDT------------------------------HAPDPPPPSPSPAANEP 2638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1287 GPG--------------PAGYGAARP---TIPARAGVISAPQSQARVCAGRPT---------PDSQSKPSETLKGPAV-- 1338
Cdd:PHA03247 2639 DPHppptvppperprddPAPGRVSRPrraRRLGRAAQASSPPQRPRRRAARPTvgsltsladPPPPPPTPEPAPHALVsa 2718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1339 LPEPLKPQA---AFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNLeTPPQPPPRSRSSQS 1398
Cdd:PHA03247 2719 TPLPPGPAAarqASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL-TRPAVASLSESRES 2797
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1399 LPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqLPSASQSQVNPLSSVSCM 1478
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPAAK 2874
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1479 PTRPPGPEESK-SQESMGSSANPFPsLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPLShDTSK 1557
Cdd:PHA03247 2875 PAAPARPPVRRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTT-DPAG 2951
                         410
                  ....*....|
gi 755554757 1558 ASSSLGGFED 1567
Cdd:PHA03247 2952 AGEPSGAVPQ 2961
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
680-1015 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 755554757  680 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 759
Cdd:cd09098     1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 839
Cdd:cd09098    81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  840 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 919
Cdd:cd09098   161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  920 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 999
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                         330
                  ....*....|....*.
gi 755554757 1000 ELKTSDHRPVVALIDI 1015
Cdd:cd09098   321 ELKTSDHRPVVALIDI 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
678-1018 4.49e-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: 4.49e-127
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    678 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKL 757
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    758 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 837
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    838 AAGQSQVKERNEDFVEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 914
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    915 QIFRGFLEGKVTFAPTYKYDLF-SEDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 993
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 755554757    994 lHYGRAELKTSDHRPVVALIDIDIF 1018
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
204-627 1.78e-94

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 317.79  E-value: 1.78e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 274
Cdd:COG5329    61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  275 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 345
Cdd:COG5329   137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  346 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 425
Cdd:COG5329   216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  426 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 505
Cdd:COG5329   295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  506 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 583
Cdd:COG5329   374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755554757  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 1.09e-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: 1.09e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757   204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISL---------RVDASDEDRI-SEVRKVLNSGNFY 273
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGGPIYKITDVEFIPLnsslydsssKSKSPDEARLlKLLKLFLSSGSFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757   274 FAWSasgvsLDLS------LNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACL 347
Cdd:pfam02383   77 FSYD-----YDLTnslqrnSTTSRSPSFDSLDERFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757   348 ISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDC-----VSSFIQIRGSVPLFWEQ-PGLQVGSHRVRMSRgFEA 421
Cdd:pfam02383  152 ISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTGnsegkIFSFVQIRGSIPLFWSQdPNLKYSKPKIQITR-PEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755554757   422 NAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKAS--EHASDIHMVSFDYHQMVK 484
Cdd:pfam02383  231 TQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEKAVKYLnqFLPDKLRYTAFDFHHECK 295
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
673-1041 2.15e-68

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 238.53  E-value: 2.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  673 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVNA 750
Cdd:COG5411    23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  751 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 825
Cdd:COG5411    84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  826 HTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 903
Cdd:COG5411   163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  904 GDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 983
Cdd:COG5411   243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755554757  984 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIA--VQGPPDG 1041
Cdd:COG5411   299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
1014-1155 5.41e-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: 5.41e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1014 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 1092
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755554757  1093 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEMSLEKIS-VTLPSSASSTLLGEDAEVAAD 1155
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIILCTDNtIPVSPCANSTLLAEDFDFGSP 144
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
771-1030 1.82e-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: 1.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  771 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 848
Cdd:PLN03191  363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  849 EDFVEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLE 922
Cdd:PLN03191  443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  923 GKVTFAPTYKYDLFSEDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 997
Cdd:PLN03191  523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                         250       260       270
                  ....*....|....*....|....*....|...
gi 755554757  998 RAELKTSDHRPVVALIDIdifEVEAEERQKIYK 1030
Cdd:PLN03191  574 RSEIRLSDHRPVSSMFLV---EVEVFDHRKLQR 603
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
1040-1116 2.32e-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: 140.62  E-value: 2.32e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755554757 1040 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 1116
Cdd:cd12719     1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
1207-1567 5.43e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1207 SAPSLPIRPsRAPSRTPGPPSSQGSPVDTQPAAqkdssqtlepkrpppprpvapparpappqrPPPPSGRNQPSPQAGLA 1286
Cdd:PHA03247 2590 DAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDT------------------------------HAPDPPPPSPSPAANEP 2638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1287 GPG--------------PAGYGAARP---TIPARAGVISAPQSQARVCAGRPT---------PDSQSKPSETLKGPAV-- 1338
Cdd:PHA03247 2639 DPHppptvppperprddPAPGRVSRPrraRRLGRAAQASSPPQRPRRRAARPTvgsltsladPPPPPPTPEPAPHALVsa 2718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1339 LPEPLKPQA---AFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNLeTPPQPPPRSRSSQS 1398
Cdd:PHA03247 2719 TPLPPGPAAarqASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL-TRPAVASLSESRES 2797
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1399 LPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqLPSASQSQVNPLSSVSCM 1478
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPAAK 2874
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1479 PTRPPGPEESK-SQESMGSSANPFPsLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPLShDTSK 1557
Cdd:PHA03247 2875 PAAPARPPVRRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTT-DPAG 2951
                         410
                  ....*....|
gi 755554757 1558 ASSSLGGFED 1567
Cdd:PHA03247 2952 AGEPSGAVPQ 2961
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1157-1564 3.60e-07

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: 55.16  E-value: 3.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1157 DMEGDVDDySAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQ 1236
Cdd:pfam03154  153 DNESDSDS-SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLI 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1237 PAAQKDSSQTLEP---------KRPPPPRPVApparpappqrppppsgrnQPSPQAGLAGPGP-------AGYGAARPTI 1300
Cdd:pfam03154  232 QQTPTLHPQRLPSphpplqpmtQPPPPSQVSP------------------QPLPQPSLHGQMPpmphslqTGPSHMQHPV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1301 PARAGVISAPQSQARVCAGrPTPDSQSKPSETLKGPAVLPEPLKPQAafPQQPSLPtPAqklqdplvPIAAPTM--PPSG 1378
Cdd:pfam03154  294 PPQPFPLTPQSSQSQVPPG-PSPAAPGQSQQRIHTPPSQSQLQSQQP--PREQPLP-PA--------PLSMPHIkpPPTT 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1379 PQPNLETPPQPPPRSRSSQSLPSDSSpqlqvkingiSGVKQEPTLKsdPFEDLSlsvlavSKAQPSVQISPvltpdpkml 1458
Cdd:pfam03154  362 PIPQLPNPQSHKHPPHLSGPSPFQMN----------SNLPPPPALK--PLSSLS------THHPPSAHPPP--------- 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1459 IQLPSASQSQVNPlssvscmPTRPPGPEESKSQESMGSSANPFPSL---PCRNPFTDRTAAPGNPfrvqsqeseaTSWLS 1535
Cdd:pfam03154  415 LQLMPQSQQLPPP-------PAQPPVLTQSQSLPPPAASHPPTSGLhqvPSQSPFPQHPFVPGGP----------PPITP 477
                          410       420
                   ....*....|....*....|....*....
gi 755554757  1536 KEEPVPNSpfPPLMPLSHDTSKASSSLGG 1564
Cdd:pfam03154  478 PSGPPTST--SSAMPGIQPPSSASVSSSG 504
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1199-1381 3.25e-04

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


Pssm-ID: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 45.14  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1199 QSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGRNQ 1278
Cdd:NF033839  285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1279 PSPQagLAGPgpagygaaRPTIPARAGvisAPQSQARVCAGRPTPDSQSKPsETLKgPAVLPEPLKPQAAFPQQPSLPTP 1358
Cdd:NF033839  365 VKPQ--PEKP--------KPEVKPQPE---TPKPEVKPQPEKPKPEVKPQP-EKPK-PEVKPQPEKPKPEVKPQPEKPKP 429
                         170       180
                  ....*....|....*....|...
gi 755554757 1359 AQKLQdPLVPIAAPTMPPSGPQP 1381
Cdd:NF033839  430 EVKPQ-PEKPKPEVKPQPEKPKP 451
RRM smart00360
RNA recognition motif;
1058-1113 1.80e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.80e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755554757   1058 DDALIDELLRQFAHFGEVILIRFVEDKMW--------VTFLEGSSALNALS-LNGKELLNRTITI 1113
Cdd:smart00360    9 PDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
 
Name Accession Description Interval E-value
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
680-1015 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 755554757  680 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 759
Cdd:cd09098     1 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVSASTTNQKLWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 839
Cdd:cd09098    81 AELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  840 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 919
Cdd:cd09098   161 GQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  920 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 999
Cdd:cd09098   241 FLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRA 320
                         330
                  ....*....|....*.
gi 755554757 1000 ELKTSDHRPVVALIDI 1015
Cdd:cd09098   321 ELKTSDHRPVVALIDI 336
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
680-1015 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 755554757  680 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQ-EFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLW 758
Cdd:cd09089     1 LRVFVGTWNVNGGKHFRSIAFKHQSMTDWLLDNPKLAGQCsNDSEEDEKPVDIFAIGFEEMVDLNASNIVSASTTNQKEW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  759 AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFA 838
Cdd:cd09089    81 GEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  839 AGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFR 918
Cdd:cd09089   161 AGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  919 GFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDllnasfqdeSKILYTWTPGTLLHYGR 998
Cdd:cd09089   241 GFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPSDKTEESLV---------ETNDPTWNPGTLLYYGR 311
                         330
                  ....*....|....*..
gi 755554757  999 AELKTSDHRPVVALIDI 1015
Cdd:cd09089   312 AELKTSDHRPVVAIIDI 328
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
680-1015 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 755554757  680 IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 759
Cdd:cd09099     1 TRVAMGTWNVNGGKQFRSNILGTSELTDWLLDSPKLSGTPDFQDDESNPPDIFAVGFEEMVELSAGNIVNASTTNRKMWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 839
Cdd:cd09099    81 EQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  840 GQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRG 919
Cdd:cd09099   161 GQNQVKERNEDYKEITQKLSFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  920 FLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRA 999
Cdd:cd09099   241 FHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWRKKWPFEKTAGEINLLDSDLDFDTKIRHTWTPGALMYYGRA 320
                         330
                  ....*....|....*.
gi 755554757 1000 ELKTSDHRPVVALIDI 1015
Cdd:cd09099   321 ELQASDHRPVLAIVEV 336
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
678-1018 4.49e-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: 4.49e-127
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    678 KKIRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLdapklagiQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKL 757
Cdd:smart00128    1 RDIKVLIGTWNVGGLE------SPKVDVTSWLF--------QKIEVKQSEKPDIYVIGLQEVVGLAPGVILETIAGKERL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    758 WAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 837
Cdd:smart00128   67 WSDLLESSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHL 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    838 AAGQSQVKERNEDFVEIARKLSFPMGRML--FSHDYVFWCGDFNYRIDLP-NEEVKELIRQQNWDSLIAGDQLINQKNAG 914
Cdd:smart00128  147 AAGASNVEQRNQDYKTILRALSFPERALLsqFDHDVVFWFGDLNFRLDSPsYEEVRRKISKKEFDDLLEKDQLNRQREAG 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757    915 QIFRGFLEGKVTFAPTYKYDLF-SEDYDTSEKCRTPAWTDRVLWRrrkwpfdRSAEDLDLLNAsfqdeskilytwtpgtl 993
Cdd:smart00128  227 KVFKGFQEGPITFPPTYKYDSVgTETYDTSEKKRVPAWCDRILYR-------SNGPELIQLSE----------------- 282
                           330       340
                    ....*....|....*....|....*
gi 755554757    994 lHYGRAELKTSDHRPVVALIDIDIF 1018
Cdd:smart00128  283 -YHSGMEITTSDHKPVFATFRLKVT 306
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
680-1015 1.53e-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: 1.53e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  680 IRVCVGTWNVNGGKqfrsiaFKNQTLTDWLLDAPklagiqefqdkrSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 759
Cdd:cd09074     1 VKIFVVTWNVGGGI------SPPENLENWLSPKG------------TEAPDIYAVGVQEVDMSVQGFVGNDDSAKAREWV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAV--DTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 837
Cdd:cd09074    63 DNIQEALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVegVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  838 AAGQSQVKERNEDFVEIARKLSFPMG----RMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNA 913
Cdd:cd09074   143 AAGQEEVERRNQDYRDILSKLKFYRGdpaiDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKEK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  914 GQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdeskilYTWTPGTL 993
Cdd:cd09074   223 GKVFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKS--------------------------KAGSEIQP 276
                         330       340
                  ....*....|....*....|...
gi 755554757  994 LHYGRAEL-KTSDHRPVVALIDI 1015
Cdd:cd09074   277 LSYTSVPLyKTSDHKPVRATFRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
680-1011 3.34e-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: 3.34e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  680 IRVCVGTWNVNGgkqfrsiAFKNQTLTDWLldapklagiqeFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWA 759
Cdd:cd09090     1 INIFVGTFNVNG-------KSYKDDLSSWL-----------FPEENDELPDIVVIGLQEVVELTAGQILNSDPSKSSFWE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 837
Cdd:cd09090    63 KKIKTTLNGrgGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  838 AAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIF 917
Cdd:cd09090   143 AAGLTNYEERNNDYKTIARGLRFSRGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  918 RGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsAEDLDLLNasfqdeskilytwtpgtllhYG 997
Cdd:cd09090   223 PGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYR---------GENLRQLS--------------------YN 273
                         330
                  ....*....|....
gi 755554757  998 RAELKTSDHRPVVA 1011
Cdd:cd09090   274 SAPLRFSDHRPVYA 287
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
680-1015 2.70e-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: 2.70e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  680 IRVCVGTWNVNGGKqfrsiafKNQTLTDWLldapklagiqefqDKRSKPTDIFAIGFEEmVELNAGNIVNASTTNQKLWA 759
Cdd:cd09093     1 FRIFVGTWNVNGQS-------PDESLRPWL-------------SCDEEPPDIYAIGFQE-LDLSAEAFLFNDSSREQEWV 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAA 839
Cdd:cd09093    60 KAVERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  840 GQSQVKERNEDFVEIARKLSFPMG----RMLFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQKNAG 914
Cdd:cd09093   140 HMEEVERRNQDYKDICARMKFEDPdgppLSISDHDVVFWLGDLNYRIqELPTEEVKELIEKNDLEELLKYDQLNIQRRAG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  915 QIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedldllnasfqdESKIlytwtpgTLL 994
Cdd:cd09093   220 KVFEGFTEGEINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWR----------------------GTNI-------VQL 270
                         330       340
                  ....*....|....*....|..
gi 755554757  995 HYGR-AELKTSDHRPVVALIDI 1015
Cdd:cd09093   271 SYRShMELKTSDHKPVSALFDI 292
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
204-627 1.78e-94

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


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 317.79  E-value: 1.78e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRIS---------EVRKVLNSGNFYF 274
Cdd:COG5329    61 YGVIGLIKLKGD----IYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEdeanydklsELKKLLSNGTFYF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  275 A--WSASGvSLDLSLNAHRSMQEHTTDNRFFWNQSL------HLHLKHYGVNCDD-WLLRLMCGGVEIRTIYAAHKQAKA 345
Cdd:COG5329   137 SydFDITN-SLQKNLSEGLEASVDRADLIFMWNSFLleefinHRSKLSSLEKQFDnFLTTVIRGFAETVDIKVGGNTISL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  346 CLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGShRVRMSRGFEANAPA 425
Cdd:COG5329   216 TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP-KIKVTRSSEAAQSA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  426 FDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHAsDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDY 505
Cdd:COG5329   295 FDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKP-KIHYTEFDFHKETSQDGFDDVKKLLYLIEQDLLEF 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  506 GFFYFDGSEVQRC--QSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKpqlVTRFQEVFRSMWSVNGDSISKI 583
Cdd:COG5329   374 GYFAYDINEGKSIseQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFRSEGVISDG---YSPFLQIHRELWADNGDAISRL 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755554757  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 1.09e-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: 1.09e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757   204 YGLLGVLRLNLGdtmlHYLVLVTGCMSVGKIQESEVFRVTSTEFISL---------RVDASDEDRI-SEVRKVLNSGNFY 273
Cdd:pfam02383    1 YGILGLIRLLSG----YYLIVITKREQVGQIGGGPIYKITDVEFIPLnsslydsssKSKSPDEARLlKLLKLFLSSGSFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757   274 FAWSasgvsLDLS------LNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACL 347
Cdd:pfam02383   77 FSYD-----YDLTnslqrnSTTSRSPSFDSLDERFFWNRHLLKPLIDFQLDLDRWILPLIQGFVEQGKLSVFGRSVTLTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757   348 ISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDC-----VSSFIQIRGSVPLFWEQ-PGLQVGSHRVRMSRgFEA 421
Cdd:pfam02383  152 ISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTGnsegkIFSFVQIRGSIPLFWSQdPNLKYSKPKIQITR-PEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755554757   422 NAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKAS--EHASDIHMVSFDYHQMVK 484
Cdd:pfam02383  231 TQPAFKKHFDDLIERYGPVHIVNLVEKKGRESKLSEAYEKAVKYLnqFLPDKLRYTAFDFHHECK 295
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
681-1015 1.01e-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: 1.01e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  681 RVCVGTWNVnggkqfrSIAFKNQTLTdwlldapKLAGIQEFQDKrskpTDIFAIGFEEmvelnagniVNASTTNQKL--- 757
Cdd:cd09094     2 RVYVVTWNV-------ATAPPPIDVR-------SLLGLQSPEVA----PDIYIIGLQE---------VNSKPVQFVSdli 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  758 ----WAvELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFV 833
Cdd:cd09094    55 fddpWS-DLFMDILSPKGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  834 CSHFAAGQSQVKERNEDFVEIARKLSFPMGRM--LFSHDYVFWCGDFNYRI-DLPNEEVKELIRQQNWDSLIAGDQLINQ 910
Cdd:cd09094   134 NCHLPAHMEKWEQRIDDFETILSTQVFNECNTpsILDHDYVFWFGDLNFRIeDVSIEFVRELVNSKKYHLLLEKDQLNMA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  911 KNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRrrkwpfdrsaedLDLLNASFQDESKIlytwtp 990
Cdd:cd09094   214 KRKEEAFQGFQEGPLNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWK------------VNPDASTEEKFLSI------ 275
                         330       340
                  ....*....|....*....|....*.
gi 755554757  991 gTLLHY-GRAELKTSDHRPVVALIDI 1015
Cdd:cd09094   276 -TQTSYkSHMEYGISDHKPVTAQFRL 300
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
673-1041 2.15e-68

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 238.53  E-value: 2.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  673 KYSKPKKIRVCVGTWNVNGgkqfrsiafKNQT--LTDWLLdaPklagiqefQDKRSKPTDIFAIGFEEMVELNAGNIVNA 750
Cdd:COG5411    23 KYVIEKDVSIFVSTFNPPG---------KPPKasTKRWLF--P--------EIEATELADLYVVGLQEVVELTPGSILSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  751 STtNQKL--W---AVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLF 825
Cdd:COG5411    84 DP-YDRLriWeskVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  826 HTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNW--DSLIA 903
Cdd:COG5411   163 ERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGrlDKLFE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  904 GDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRrkwpfdrsaedldllnasfqdesk 983
Cdd:COG5411   243 YDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYDTSDKGRIPSWTDRILYKS------------------------ 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755554757  984 ilYTWTPGTllhYGRAE-LKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIA--VQGPPDG 1041
Cdd:COG5411   299 --EQLTPHS---YSSIPhLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAeyKTELGEA 354
DUF1866 pfam08952
Domain of unknown function (DUF1866); This domain, found in Synaptojanin, has no known ...
1014-1155 5.41e-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: 5.41e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1014 DIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEG 1092
Cdd:pfam08952    1 DVEIQEVDPEARRRVFKEVIRDQGPPDGTIVVSLCSgDLDEKNIFDENLMDELIQELTSFGEVTLVRFVEDTMWVTFRDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755554757  1093 SSALNALSLNGKELLNRTITITLKSPDWIKHLEEEMSLEKIS-VTLPSSASSTLLGEDAEVAAD 1155
Cdd:pfam08952   81 HSALNALSKDGMKVCGRALKIRLKSKDWIKGLEEEIILCTDNtIPVSPCANSTLLAEDFDFGSP 144
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
678-1015 2.08e-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: 2.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  678 KKIRVCVGTWNVNGGKQFrsiafkNQTLTDWLLdapklAGIQEFQdkrskpTDIFAIGFEEmvelnagnivnaSTTNQKL 757
Cdd:cd09095     3 RNVGIFVATWNMQGQKEL------PENLDDFLL-----PTSADFA------QDIYVIGVQE------------GCSDRRE 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  758 WAVELQKTISrdNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 837
Cdd:cd09095    54 WEIRLQETLG--PSHVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  838 AAGQSQVKERNEDFVEIARKLSFPmgRMLFSHDY-------------VFWCGDFNYRIDLPNEEVKELIRQ---QNWDSL 901
Cdd:cd09095   132 TSGDGKVKERVLDYNKIIQALNLP--RNVPTNPYksesgdvttrfdeVFWFGDFNFRLSGPRHLVDALINQgqeVDVSAL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  902 IAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRkwpfdrsaedldllnasfqde 981
Cdd:cd09095   210 LQHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSR--------------------- 268
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 755554757  982 skilytwTPGTL--LHYGRAE-LKTSDHRPVVALIDI 1015
Cdd:cd09095   269 -------QKGDVccLKYNSCPsIKTSDHRPVFALFRV 298
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
771-1030 1.82e-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: 1.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  771 KYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKE--RN 848
Cdd:PLN03191  363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEqrRN 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  849 EDFVEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLE 922
Cdd:PLN03191  443 ADVYEIIRRTRFSsvldtdQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKE 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  923 GKVTFAPTYKYDLFSEDY-----DTSEKCRTPAWTDRVLWrrrkwpfdrsaedldlLNASFQDESkilytwtpgtllhYG 997
Cdd:PLN03191  523 GPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------------LGKGIKQLC-------------YK 573
                         250       260       270
                  ....*....|....*....|....*....|...
gi 755554757  998 RAELKTSDHRPVVALIDIdifEVEAEERQKIYK 1030
Cdd:PLN03191  574 RSEIRLSDHRPVSSMFLV---EVEVFDHRKLQR 603
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
680-958 6.29e-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: 6.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  680 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivnaSTTNQKL 757
Cdd:cd09100     1 ITIFIGTWNMGNAPPPKKI-------TSWFQCK----GQGKTRDDTADyiPHDIYVIGTQE------------DPLGEKE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  758 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 835
Cdd:cd09100    58 WLDTLKHSLREitSISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  836 HFAAGQSQVKERNEDFVEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKEL---IRQQNWDSLIAGDQL 907
Cdd:cd09100   138 HLTSGSEKKLRRNQNYFNILRFLVLgdkKLSPFNITHrfTHLFWLGDLNYRVELPNTEAENIiqkIKQQQYQELLPHDQL 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755554757  908 INQKNAGQIFRGFLEGKVTFAPTYKYD-------LFSEDYDTSEKCRTPAWTDRVLWR 958
Cdd:cd09100   218 LIERKESKVFLQFEEEEITFAPTYRFErgtreryAYTKQKATGMKYNLPSWCDRVLWK 275
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
680-1015 2.33e-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: 2.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  680 IRVCVGTWNVNGGKQFRSIafknqtlTDWLLDAPKLAGIQEFQDkrSKPTDIFAIGFEEmvelnagnivnaSTTNQKLWA 759
Cdd:cd09091     1 ISIFIGTWNMGSAPPPKNI-------TSWFTSKGQGKTRDDVAD--YIPHDIYVIGTQE------------DPLGEKEWL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  760 VELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHF 837
Cdd:cd09091    60 DLLRHSLKEltSLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  838 AAGQSQVKERNEDFVEIARKLSF---PMGRMLFSH--DYVFWCGDFNYRIDLPNEEVKELI---RQQNWDSLIAGDQLIN 909
Cdd:cd09091   140 TSGSEKKLRRNQNYLNILRFLSLgdkKLSAFNITHrfTHLFWLGDLNYRLDLPIQEAENIIqkiEQQQFEPLLRHDQLNL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  910 QKNAGQIFRGFLEGKVTFAPTYKYDLFSEDY-------DTSEKCRTPAWTDRVLWrrrkwpfdRSAEDLDLLNASFQDES 982
Cdd:cd09091   220 EREEHKVFLRFSEEEITFPPTYRYERGSRDTyaytkqkATGVKYNLPSWCDRILW--------KSYPETHIICQSYGCTD 291
                         330       340       350
                  ....*....|....*....|....*....|...
gi 755554757  983 KILytwtpgtllhygraelkTSDHRPVVALIDI 1015
Cdd:cd09091   292 DIV-----------------TSDHSPVFGTFEV 307
RRM_SYNJ1 cd12719
RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins; This subgroup ...
1040-1116 2.32e-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: 140.62  E-value: 2.32e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755554757 1040 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 1116
Cdd:cd12719     1 DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGRTIIISLK 77
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
680-958 4.50e-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: 4.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  680 IRVCVGTWNVNGGKQFRSiafknqtLTDWLLDApklaGIQEFQDKRSK--PTDIFAIGFEEmvelnagnivnaSTTNQKL 757
Cdd:cd09101     1 ISIFIGTWNMGSVPPPKS-------LASWLTSR----GLGKTLDETTVtiPHDIYVFGTQE------------NSVGDRE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  758 WAVELQKTISR--DNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCS 835
Cdd:cd09101    58 WVDFLRASLKEltDIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNC 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  836 HFAAGQSQVKERNEDFVEIARKLSFPMGR-------MLFSHdyVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLI 908
Cdd:cd09101   138 HLTSGNEKTHRRNQNYLDILRSLSLGDKQlnafdisLRFTH--LFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLN 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755554757  909 NQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRT-------PAWTDRVLWR 958
Cdd:cd09101   216 LEREKNKVFLRFREEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILWK 272
RRM_SYNJ cd12440
RNA recognition motif (RRM) found in synaptojanin-1, synaptojanin-2 and similar proteins; This ...
1040-1116 2.50e-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: 2.50e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755554757 1040 DGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITITLK 1116
Cdd:cd12440     1 DATVVVSLDSKSEEWNEFEDALIGELLRVLASYGDVVLVRFAHEGMLVTFRDGRSALAALALNGKQILGRTLKIRLK 77
RRM_SYNJ2 cd12720
RNA recognition motif (RRM) found in synaptojanin-2 and similar proteins; This subgroup ...
1040-1113 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 755554757 1040 DGTVLVSIKS-SAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELLNRTITI 1113
Cdd:cd12720     1 DATVVVNLLSpTLEEKNDFPEDLSTELVQCFQSYGTVILVRFNRGQMLVTFEDSRSALRVLDLDGIKVNGRAVKI 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
1207-1567 5.43e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1207 SAPSLPIRPsRAPSRTPGPPSSQGSPVDTQPAAqkdssqtlepkrpppprpvapparpappqrPPPPSGRNQPSPQAGLA 1286
Cdd:PHA03247 2590 DAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDT------------------------------HAPDPPPPSPSPAANEP 2638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1287 GPG--------------PAGYGAARP---TIPARAGVISAPQSQARVCAGRPT---------PDSQSKPSETLKGPAV-- 1338
Cdd:PHA03247 2639 DPHppptvppperprddPAPGRVSRPrraRRLGRAAQASSPPQRPRRRAARPTvgsltsladPPPPPPTPEPAPHALVsa 2718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1339 LPEPLKPQA---AFPQQPSLPTPAQKLQDPLVPI-----------------AAPTMPPSGPQPNLeTPPQPPPRSRSSQS 1398
Cdd:PHA03247 2719 TPLPPGPAAarqASPALPAAPAPPAVPAGPATPGgparparppttagppapAPPAAPAAGPPRRL-TRPAVASLSESRES 2797
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1399 LPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqLPSASQSQVNPLSSVSCM 1478
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPAAK 2874
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1479 PTRPPGPEESK-SQESMGSSANPFPsLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPLShDTSK 1557
Cdd:PHA03247 2875 PAAPARPPVRRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTT-DPAG 2951
                         410
                  ....*....|
gi 755554757 1558 ASSSLGGFED 1567
Cdd:PHA03247 2952 AGEPSGAVPQ 2961
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1157-1564 3.60e-07

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: 55.16  E-value: 3.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1157 DMEGDVDDySAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQ 1236
Cdd:pfam03154  153 DNESDSDS-SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLI 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1237 PAAQKDSSQTLEP---------KRPPPPRPVApparpappqrppppsgrnQPSPQAGLAGPGP-------AGYGAARPTI 1300
Cdd:pfam03154  232 QQTPTLHPQRLPSphpplqpmtQPPPPSQVSP------------------QPLPQPSLHGQMPpmphslqTGPSHMQHPV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1301 PARAGVISAPQSQARVCAGrPTPDSQSKPSETLKGPAVLPEPLKPQAafPQQPSLPtPAqklqdplvPIAAPTM--PPSG 1378
Cdd:pfam03154  294 PPQPFPLTPQSSQSQVPPG-PSPAAPGQSQQRIHTPPSQSQLQSQQP--PREQPLP-PA--------PLSMPHIkpPPTT 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1379 PQPNLETPPQPPPRSRSSQSLPSDSSpqlqvkingiSGVKQEPTLKsdPFEDLSlsvlavSKAQPSVQISPvltpdpkml 1458
Cdd:pfam03154  362 PIPQLPNPQSHKHPPHLSGPSPFQMN----------SNLPPPPALK--PLSSLS------THHPPSAHPPP--------- 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1459 IQLPSASQSQVNPlssvscmPTRPPGPEESKSQESMGSSANPFPSL---PCRNPFTDRTAAPGNPfrvqsqeseaTSWLS 1535
Cdd:pfam03154  415 LQLMPQSQQLPPP-------PAQPPVLTQSQSLPPPAASHPPTSGLhqvPSQSPFPQHPFVPGGP----------PPITP 477
                          410       420
                   ....*....|....*....|....*....
gi 755554757  1536 KEEPVPNSpfPPLMPLSHDTSKASSSLGG 1564
Cdd:pfam03154  478 PSGPPTST--SSAMPGIQPPSSASVSSSG 504
PHA03247 PHA03247
large tegument protein UL36; Provisional
1174-1562 4.29e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1174 PQHLQPSSSSGLGTSPSSSPRTSPCQSPTVPeySAPSLPIRPSrAPSRTPGPPSSQGSPVDTQPAAQKDSSQtlepkrpp 1253
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPALPAAPAPP--AVPAGPATPG-GPARPARPPTTAGPPAPAPPAAPAAGPP-------- 2780
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1254 pPRPVAPPARPAPPQRPPPPSGRNQPSPQAGLAGPGPAGYGAARPTIParagvisAPQSQARVCAGRPTPDSQSKPSETL 1333
Cdd:PHA03247 2781 -RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------LPPPTSAQPTAPPPPPGPPPPSLPL 2852
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1334 KGpAVLP-------EPLKPQAAFPQQPSLPtPAQKLQDPLVPIAAPT--MPPSGPQPNLETPPQPPPRSRSSQSLPSDSS 1404
Cdd:PHA03247 2853 GG-SVAPggdvrrrPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESfaLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1405 PQLQvkingisgvkqePTLKSDPFEDLSLSVLAVSKAQPSV------QISPVLTPDPKMLIqlPSASQSQVNPLSSVSCm 1478
Cdd:PHA03247 2931 PPPP------------PPPRPQPPLAPTTDPAGAGEPSGAVpqpwlgALVPGRVAVPRFRV--PQPAPSREAPASSTPP- 2995
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1479 PTRPPGPEESKSQESMG----SSANPFPSLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPVPNSPF--PPLMPLS 1552
Cdd:PHA03247 2996 LTGHSLSRVSSWASSLAlheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFahEPDPATP 3075
                         410
                  ....*....|
gi 755554757 1553 HDTSKASSSL 1562
Cdd:PHA03247 3076 EAGARESPSS 3085
PHA03247 PHA03247
large tegument protein UL36; Provisional
1201-1560 8.27e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 8.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1201 PTVPEYSAPSLPIRPSRAPSRTPgPPSSQGSPVDTQPAAQKDSS--QTLEPKRPPPPRPVAPPARPAPPQRPPPPSGRNQ 1278
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAP-HALVSATPLPPGPAAARQASpaLPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1279 PSPQAGLAGPGPagygaarPTIPARAGvisAPQSQARVCAgrPTPDSQSKPSETLKGPAvlpePLKPQAAFPQQPSLPTP 1358
Cdd:PHA03247 2769 PAPPAAPAAGPP-------RRLTRPAV---ASLSESRESL--PSPWDPADPPAAVLAPA----AALPPAASPAGPLPPPT 2832
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1359 AqklqdplvPIAAPTMPPSGPQPNLETppqppprsrssqsLPSDSSPQLQVKINGISG-VKQEPTLKSDPfedlSLSVLA 1437
Cdd:PHA03247 2833 S--------AQPTAPPPPPGPPPPSLP-------------LGGSVAPGGDVRRRPPSRsPAAKPAAPARP----PVRRLA 2887
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1438 VSKAQPSVQISPVLTPDPKMLIQLPSASQSQVNPLSSVSCMPT---RPPGPEESKSQESMGSSANPFPSLPCRNPFTDrT 1514
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQpppPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLG-A 2966
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 755554757 1515 AAPGNPFRVQSQESEATSwlSKEEPVPNSPFPPLMPLSHDTSKASS 1560
Cdd:PHA03247 2967 LVPGRVAVPRFRVPQPAP--SREAPASSTPPLTGHSLSRVSSWASS 3010
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
787-884 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 755554757  787 VFIRPqhaPFIRDVAVDTVKTGMGgATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFpmgRML 866
Cdd:cd08372    71 ILSKT---PKFKIVEKHQYKFGEG-DSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKR---LRQ 143
                          90
                  ....*....|....*...
gi 755554757  867 FSHDYVFWCGDFNYRIDL 884
Cdd:cd08372   144 PNSAPVVICGDFNVRPSE 161
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1177-1379 5.09e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.42  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1177 LQPSSSSGlgtspsssprtspcQSPTVPEYSAPSLPIRPSRAPSRTPGPPSSqgSPVDTQPAAQKDSSQTLEPKRPPPPR 1256
Cdd:PRK12323  363 FRPGQSGG--------------GAGPATAAAAPVAQPAPAAAAPAAAAPAPA--APPAAPAAAPAAAAAARAVAAAPARR 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1257 PVAPPARPAPPQRPPPPSGRNQPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSqSKPSETLKGP 1336
Cdd:PRK12323  427 SPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDD-PPPWEELPPE 505
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 755554757 1337 AVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGP 1379
Cdd:PRK12323  506 FASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA 548
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1200-1381 5.38e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.14  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1200 SPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGR--- 1276
Cdd:PRK07764  596 GGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKagg 675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1277 ----NQPSPQAGLAGPGPAGyGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQ 1352
Cdd:PRK07764  676 aapaAPPPAPAPAAPAAPAG-AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGA 754
                         170       180
                  ....*....|....*....|....*....
gi 755554757 1353 PSLPTPAQKLQDPLVPIAAPTMPPSGPQP 1381
Cdd:PRK07764  755 PAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PHA03247 PHA03247
large tegument protein UL36; Provisional
1267-1551 6.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1267 PQRPPPPSGRNQPSPQAGLAGPGPA-GYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKP 1345
Cdd:PHA03247 2557 PAAPPAAPDRSVPPPRPAPRPSEPAvTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAAN 2636
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1346 QAAFPQQPSLPTPAQKLQDPLVP-------------IAAPTMPPSGPQP--------NLETPPQPPPRSRSSQSLPSDSS 1404
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDPAPGrvsrprrarrlgrAAQASSPPQRPRRraarptvgSLTSLADPPPPPPTPEPAPHALV 2716
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1405 PQLQVKINGISGVKQEPTLKSDPfedlslsvlaVSKAQPSVQISPVlTPDPKMLIQLPSASQSQVNPLSSVSCMPTRPPG 1484
Cdd:PHA03247 2717 SATPLPPGPAAARQASPALPAAP----------APPAVPAGPATPG-GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR 2785
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755554757 1485 PEESKSQESMGSSANPFPSLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPVPNSPFPPLMPL 1551
Cdd:PHA03247 2786 PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1207-1564 1.08e-05

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 50.30  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1207 SAPSLPIRPSRAPSRTPGPPSSQGSPVD-TQPAAQKDSSQTLEPKRPPPPRPVAPPARPAppqrppppsgrnqPSPQagl 1285
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSSTHVPTNlTAPASTGPTVSTADVTSPTPAGTTSGASPVT-------------PSPS--- 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1286 agPGPAGYGAARPTIPARAGVISAPQSQARV---CAGRPTPDSQSkPSETLKGPAVLPEPLKPQAAFPqQPSLPTPAQKL 1362
Cdd:pfam05109  494 --PRDNGTESKAPDMTSPTSAVTTPTPNATSptpAVTTPTPNATS-PTLGKTSPTSAVTTPTPNATSP-TPAVTTPTPNA 569
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1363 QDPLVPIAAPTMPPSGPQPNLETppqppprsrssqSLPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLSlsvlAVSKAQ 1442
Cdd:pfam05109  570 TIPTLGKTSPTSAVTTPTPNATS------------PTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATS----AVTTGQ 633
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  1443 PSVQISPV--LTPDPKMLIQLPSASQSQvNPLSSVSCMPTRPPGPEESKSQESMGSSANPFPSLPCRNP---FTDRTAAP 1517
Cdd:pfam05109  634 HNITSSSTssMSLRPSSISETLSPSTSD-NSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPrpgTTSQASGP 712
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755554757  1518 GNPfRVQSQESEATswLSKEEPvPNSPFPPLMPLSHDTS---------KASSSLGG 1564
Cdd:pfam05109  713 GNS-STSTKPGEVN--VTKGTP-PKNATSPQAPSGQKTAvptvtstggKANSTTGG 764
PHA03247 PHA03247
large tegument protein UL36; Provisional
1207-1502 2.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1207 SAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTlepkrpppprPVAPPARPAPPQRPPPPSGRNQPSPQAGLA 1286
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS----------AQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1287 GPGPAGYGAARPTIPARAGVISAPQSQArvcagRPTPDSQSKPSEtlkGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPL 1366
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAV-----SRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1367 VPIAAPTMPP-SGPQPNLETPPQPPPRSRSSQSLPSDSSPQLQVKINGISgvKQEPTLKSDPFEDLSLSvlAVSKAQPSV 1445
Cdd:PHA03247 2936 PPRPQPPLAPtTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS--REAPASSTPPLTGHSLS--RVSSWASSL 3011
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1446 QISPVLTPDPKMLIQ---LPS-----------ASQSQVNPLSSVSCMPTRP---------PGPEESKSQESMGSSANPFP 1502
Cdd:PHA03247 3012 ALHEETDPPPVSLKQtlwPPDdtedsdadslfDSDSERSDLEALDPLPPEPhdpfahepdPATPEAGARESPSSQFGPPP 3091
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
824-1009 2.36e-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: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  824 LFHTTSLCFVCSHFAAGQSQVKERNEDFVeIARKLSFPMGRMLFshdYVFwcGDFNYRIDL------------------- 884
Cdd:cd09092   176 LFHDASNLAACESSPSVYSQNRHRALGYV-LERLTDERFEKVPF---FVF--GDFNFRLDTksvvetlcakatmqtvrka 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  885 -PNEEVKELIRQQNWD----------SLIAGDQLINQKNAGQIFRGF-----------LEGKVTFAPTYKYdlfSEDYDT 942
Cdd:cd09092   250 dSNIVVKLEFREKDNDnkvvlqiekkKFDYFNQDVFRDNNGKALLKFdkelevfkdvlYELDISFPPSYPY---SEDPEQ 326
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757  943 SE---KCRTPAWTDRVLwrrrkwpFDRSAEDLDLLNasfqDESKILYTwtpgtllHYGRaELKTSDHRPV 1009
Cdd:cd09092   327 GTqymNTRCPAWCDRIL-------MSHSARELKSEN----EEKSVTYD-------MIGP-NVCMGDHKPV 377
RRM3_Prp24 cd12298
RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar ...
1062-1115 7.46e-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: 7.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755554757 1062 IDELLRQFAHFGEV---ILIRFVEDKM--------WVTFLEGSSALNALSLNGKELLNRTITITL 1115
Cdd:cd12298    14 EEALRGIFEKFGEIesiNIPKKQKNRKgrhnngfaFVTFEDADSAESALQLNGTLLDNRKISVSL 78
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1279-1473 7.66e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.56  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1279 PSPQAGLAGPGPAGYGAARPtiPARAGVISAPQSQARVCAGRPTPDSQ--SKPSETLKGPAVLPEPLKPQAAFPQQPSLP 1356
Cdd:PRK12323  408 AAPAAAAAARAVAAAPARRS--PAPEALAAARQASARGPGGAPAPAPApaAAPAAAARPAAAGPRPVAAAAAAAPARAAP 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1357 TPAQKLQDPLVPiAAPTMPPSGPQPNLETPPQPPPRSRSSQSLPSDSSPQlqvkingisgvkqeptlkSDPFEDLSLSVL 1436
Cdd:PRK12323  486 AAAPAPADDDPP-PWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADP------------------DDAFETLAPAPA 546
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 755554757 1437 AVSKAQPSVQISPVLTPDPkmliqlPSASQSQVNPLS 1473
Cdd:PRK12323  547 AAPAPRAAAATEPVVAPRP------PRASASGLPDMF 577
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
1063-1113 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 755554757 1063 DELLRQFAHFGEVILIRFVEDKM-------WVTFLEGSSALNALS-LNGKELLNRTITI 1113
Cdd:cd00590    13 EDLRELFSKFGEVVSVRIVRDRDgkskgfaFVEFESPEDAEKALEaLNGTELGGRPLKV 71
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1278-1381 2.65e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1278 QPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPT 1357
Cdd:PRK07764  398 APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPT 477
                          90       100
                  ....*....|....*....|....
gi 755554757 1358 PAQklqdplVPIAAPTMPPSGPQP 1381
Cdd:PRK07764  478 AAP------APAPPAAPAPAAAPA 495
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1199-1381 3.25e-04

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


Pssm-ID: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 45.14  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1199 QSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGRNQ 1278
Cdd:NF033839  285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1279 PSPQagLAGPgpagygaaRPTIPARAGvisAPQSQARVCAGRPTPDSQSKPsETLKgPAVLPEPLKPQAAFPQQPSLPTP 1358
Cdd:NF033839  365 VKPQ--PEKP--------KPEVKPQPE---TPKPEVKPQPEKPKPEVKPQP-EKPK-PEVKPQPEKPKPEVKPQPEKPKP 429
                         170       180
                  ....*....|....*....|...
gi 755554757 1359 AQKLQdPLVPIAAPTMPPSGPQP 1381
Cdd:NF033839  430 EVKPQ-PEKPKPEVKPQPEKPKP 451
PHA03247 PHA03247
large tegument protein UL36; Provisional
1201-1667 9.22e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1201 PTVPEYSA-PSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKrpppprpvapparpappqrppppSGRNQP 1279
Cdd:PHA03247 2589 PDAPPQSArPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPD-----------------------PHPPPT 2645
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1280 SPQAGLAGPGPAGYGAARP---TIPARAGVISAPQSQARVCAGRPTPDSQSKPSETlKGPAVLPEPlKPQAAFPQQPSLP 1356
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPrraRRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP-PPPPPTPEP-APHALVSATPLPP 2723
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1357 TPAQKLQDPLVPIAAPTMPPSGPQPNLETPPQPPPRSRSSQSLPSDSSPQLQVKingisgvKQEPTLKSDPFEDLSLSVL 1436
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-------GPPRRLTRPAVASLSESRE 2796
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1437 AV-SKAQPSVQISPVLTPDPKMLIQLPSASQSQvNPLSSVSCMPTRPPGPeeSKSQESMGSSANPFPSL----PCRNPFT 1511
Cdd:PHA03247 2797 SLpSPWDPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQPTAPPPPPGP--PPPSLPLGGSVAPGGDVrrrpPSRSPAA 2873
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1512 DRTAAPGNPFRVQSQESEATSWLSKEEPvPNSPFPPLMPlshdtskassslggfednfDLQSQSTVKTSNPkgwVTFDED 1591
Cdd:PHA03247 2874 KPAAPARPPVRRLARPAVSRSTESFALP-PDQPERPPQP-------------------QAPPPPQPQPQPP---PPPQPQ 2930
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1592 DNFPTTGKSKSVCPDLVGNAPAS-----FDDDWSKGASVSFCVLPARRPPPPPPPVPLLPPGTTSSAGPSTTLPSKAPST 1666
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGepsgaVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010

                  .
gi 755554757 1667 L 1667
Cdd:PHA03247 3011 L 3011
PHA03378 PHA03378
EBNA-3B; Provisional
1200-1382 1.47e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1200 SPTVPEYSAPSLPIRPSRAPSRTPGPpssQGSPVDTQPAAqkdssqtlepkrpppprpvappARPAPPQRPPPPSGRNQP 1279
Cdd:PHA03378  702 TPMRPPAAPPGRAQRPAAATGRARPP---AAAPGRARPPA----------------------AAPGRARPPAAAPGRARP 756
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1280 SPQAGLAGPGPAGY-GAARPTIPARAGviSAPQSQARvCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQpsLPTP 1358
Cdd:PHA03378  757 PAAAPGRARPPAAApGAPTPQPPPQAP--PAPQQRPR-GAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQ--LLTG 831
                         170       180
                  ....*....|....*....|....*.
gi 755554757 1359 AQKLQDPLV--PIAAPTMPPSGPQPN 1382
Cdd:PHA03378  832 GVKRGRPSLkkPAALERQAAAGPTPS 857
PHA03247 PHA03247
large tegument protein UL36; Provisional
1280-1667 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1280 SPQAGlaGPGPAGYGAARPTIPARagviSAPQSQarvCAGRPT-PDSQSKPSEtlkgPAVLPEPLKPQAafPQQPSLPTP 1358
Cdd:PHA03247 2545 SDDAG--DPPPPLPPAAPPAAPDR----SVPPPR---PAPRPSePAVTSRARR----PDAPPQSARPRA--PVDDRGDPR 2609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1359 AQKLQDPLVP-IAAPTMPPSGPQPnletppqpppRSRSSQSLPSDSSPQLQVKINGISGVKqeptlksdpfedLSLSVLA 1437
Cdd:PHA03247 2610 GPAPPSPLPPdTHAPDPPPPSPSP----------AANEPDPHPPPTVPPPERPRDDPAPGR------------VSRPRRA 2667
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1438 VSKAQPSVQISPVLTPDPKmliqlpsASQSQVNPLSSVSCMPTRPPGPEES-----------KSQESMGSSANPFPSLPC 1506
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRRR-------AARPTVGSLTSLADPPPPPPTPEPAphalvsatplpPGPAAARQASPALPAAPA 2740
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1507 RNPFTDRTAAPGNPFRVQSQESEATswlskeepvPNSPFPPLMPLSHDTSKASSSLGGfednfdlqSQSTVKTSNPKGWV 1586
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAG---------PPAPAPPAAPAAGPPRRLTRPAVA--------SLSESRESLPSPWD 2803
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1587 TFDeddnfpttgksksvcPDLVGNAPASFDDDWSKGASVSfcvlparrpppppppvpllPPGTTSSAGPSTTLPSKAPST 1666
Cdd:PHA03247 2804 PAD---------------PPAAVLAPAAALPPAASPAGPL-------------------PPPTSAQPTAPPPPPGPPPPS 2849

                  .
gi 755554757 1667 L 1667
Cdd:PHA03247 2850 L 2850
RRM smart00360
RNA recognition motif;
1058-1113 1.80e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.34  E-value: 1.80e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755554757   1058 DDALIDELLRQFAHFGEVILIRFVEDKMW--------VTFLEGSSALNALS-LNGKELLNRTITI 1113
Cdd:smart00360    9 PDTTEEELRELFSKFGKVESVRLVRDKETgkskgfafVEFESEEDAEKALEaLNGKELDGRPLKV 73
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1278-1511 1.82e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1278 QPSPQAGLAGPGPAGYGAARPTIPARAGVISAPQSQARVCAGRPTPDSQSKP------SETLKGPAVLPEPLKPQAAFPQ 1351
Cdd:PRK12323  364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAaravaaAPARRSPAPEALAAARQASARG 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1352 QPSLPTPAQKLQDPLVPIAAPTMPPSGPQPNLETPPQPPPRSRSSQSLPSDSSPqlqvkingisgvkqeptlksdPFEDL 1431
Cdd:PRK12323  444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP---------------------PWEEL 502
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1432 SLSVLAVSKAQPSVQISPV---LTPDPKMLIQLPSASQSQVNPLSSVSCMPTRPPGPEESKSQESMGSSANP------FP 1502
Cdd:PRK12323  503 PPEFASPAPAQPDAAPAGWvaeSIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPdmfdgdWP 582

                  ....*....
gi 755554757 1503 SLPCRNPFT 1511
Cdd:PRK12323  583 ALAARLPVR 591
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1278-1517 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 755554757 1278 QPSPQAGLAGPGPAGYGAarptiPARAGVISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPlkpqAAFPQQPSLPT 1357
Cdd:PRK10263  318 EPVAVAAAATTATQSWAA-----PVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAP----EGYPQQSQYAQ 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1358 PAQKLQDPLvpiaaptMPPSGPQPNLETPPQPPPRSRSSQSLPSDSSPQLQVKINGISGVKQEPTLKSDPFEDLSLSVLA 1437
Cdd:PRK10263  389 PAVQYNEPL-------QQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQST 461
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1438 VSKAQPSVQisPVlTPDPKMLIQLPSASQSQVNPLSSV-SCMPTRPP-------GPEESKSQESMGSSANPFPSlPCRNP 1509
Cdd:PRK10263  462 YQTEQTYQQ--PA-AQEPLYQQPQPVEQQPVVEPEPVVeETKPARPPlyyfeevEEKRAREREQLAAWYQPIPE-PVKEP 537

                  ....*...
gi 755554757 1510 FTDRTAAP 1517
Cdd:PRK10263  538 EPIKSSLK 545
RRM2_SREK1 cd12260
RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 ...
1063-1114 3.49e-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: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755554757 1063 DELLRQFAHFGEVILIRFVEDK------MWVTFLEGSSALNALSLNGKELLNRTITIT 1114
Cdd:cd12260    19 DQLLEFFSQAGEVKYVRMAGDEtqptryAFVEFAEQTSVINALKLNGKMFGGRPLKVN 76
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1279-1376 6.83e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1279 PSPQAGLAGPGPAGYGAARPTIparagvisAPQSQARVCAGRPTPDSQSKPsETLKGPAVLPEPLKPQAAFPQQPSLPTP 1358
Cdd:PRK14950  362 PVPAPQPAKPTAAAPSPVRPTP--------APSTRPKAAAAANIPPKEPVR-ETATPPPVPPRPVAPPVPHTPESAPKLT 432
                          90
                  ....*....|....*...
gi 755554757 1359 AQKLQDPLVPIAAPTMPP 1376
Cdd:PRK14950  433 RAAIPVDEKPKYTPPAPP 450
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1167-1377 6.86e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1167 AEVEELLPQHLQP--SSSSGLGTSPSSSPRTSPCQSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSS 1244
Cdd:PRK07003  420 ATRAEAPPAAPAPpaTADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAP 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1245 QTLEPKRPPPPRPVAPPARPAPPQRPPppsgrnQPSPQAglAGPGPAgygAARPtiPARAGVISAPQSQARVCAGRPTPD 1324
Cdd:PRK07003  500 SAATPAAVPDARAPAAASREDAPAAAA------PPAPEA--RPPTPA---AAAP--AARAGGAAAALDVLRNAGMRVSSD 566
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755554757 1325 SQSKPSETLKGPAVLPEPLKPQAAFPQQPsLPTPAQKLQDPLVPI--AAPTMPPS 1377
Cdd:PRK07003  567 RGARAAAAAKPAAAPAAAPKPAAPRVAVQ-VPTPRARAATGDAPPngAARAEQAA 620
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1281-1381 7.17e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.91  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1281 PQAGLAGPGPAGygAARPTIPARAGVISAPQSQARVCAgrptpdSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPtpaq 1360
Cdd:PRK14971  363 TQKGDDASGGRG--PKQHIKPVFTQPAAAPQPSAAAAA------SPSPSQSSAAAQPSAPQSATQPAGTPPTVSVD---- 430
                          90       100
                  ....*....|....*....|.
gi 755554757 1361 klqdplVPIAAPTMPPSGPQP 1381
Cdd:PRK14971  431 ------PPAAVPVNPPSTAPQ 445
PHA03379 PHA03379
EBNA-3A; Provisional
1214-1551 8.05e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.81  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1214 RPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGRNQPSP----QAGLAGPG 1289
Cdd:PHA03379  407 KASEPTYGTPRPPVEKPRPEVPQSLETATSHGSAQVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPlqdlEPGDQLPG 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1290 PAGYGAARPT-IPARAGVISAPQsqarvcagrptpdsQSKPSETlkgPAVLPEPLKPQaAFPQQPsLPTPAQKLQDPLVP 1368
Cdd:PHA03379  487 VVQDGRPACApVPAPAGPIVRPW--------------EASLSQV---PGVAFAPVMPQ-PMPVEP-VPVPTVALERPVCP 547
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1369 iAAPTMPPSGPQpnlETPPQPPPRSRSSQSLPSDSSPQLQVKI---NGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPsv 1445
Cdd:PHA03379  548 -APPLIAMQGPG---ETSGIVRVRERWRPAPWTPNPPRSPSQMsvrDRLARLRAEAQPYQASVEVQPPQLTQVSPQQP-- 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1446 qISPVLTPDPKML-------------------IQLPSASQSQVNPLSSVSC-------MPTRPPGPEESKS--------Q 1491
Cdd:PHA03379  622 -MEYPLEPEQQMFpgspfsqvadvmraggvpaMQPQYFDLPLQQPISQGAPlaplrasMGPVPPVPATQPQyfdiplteP 700
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755554757 1492 ESMGSSANPF--------PSLPCRNPFTDRTAAPG-NPFRVQSQESEATSWLSKEEPVPNSPFPPLMPL 1551
Cdd:PHA03379  701 INQGASAAHFlpqqpmegPLVPERWMFQGATLSQSvRPGVAQSQYFDLPLTQPINHGAPAAHFLHQPPM 769
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1415-1560 8.11e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554757 1415 SGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKMliqlPSASQSQVNPlssvsCMPTRPPGPEESKSQESM 1494
Cdd:PTZ00449  551 ETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEE----PKKPKRPRSA-----QRPTRPKSPKLPELLDIP 621
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755554757 1495 GSSANP-FPSLPCRNPFTDRTAAPGNPfrvqsqesEATSWLSKEEPvPNSPFPPLMP-----LSHDTSKASS 1560
Cdd:PTZ00449  622 KSPKRPeSPKSPKRPPPPQRPSSPERP--------EGPKIIKSPKP-PKSPKPPFDPkfkekFYDDYLDAAA 684
 
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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