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Conserved domains on  [gi|1858900856|ref|NP_001371319|]
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F-BAR domain only protein 1 isoform f [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AP_MHD_Cterm super family cl10970
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
 602-863 8.16e-167

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


The actual alignment was detected with superfamily member cd09268:

Pssm-ID: 472082  Cd Length: 265  Bit Score: 484.86  E-value: 8.16e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 680
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgATAVPTPL 760
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 761 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 837
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                         250       260
                  ....*....|....*....|....*.
gi 1858900856 838 DLELVGSGYRMSLVKRRFATGMYLVS 863
Cdd:cd09268   240 DIELVGSGYRMSLVKKRFATGKYLVC 265
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 10-245 1.39e-163

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07674:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 261  Bit Score: 476.36  E-value: 1.39e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  10 GEKNHGFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLALCHLELT 64
Cdd:cd07674     1 GEKNAGFDVLYHNMKHGQISTKELADFVRERaaieetysksmsklskmasngsplgTFAPMWEVFRVSSDKLALCHLELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  65 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 144
Cdd:cd07674    81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 145 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 224
Cdd:cd07674   161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                         250       260
                  ....*....|....*....|.
gi 1858900856 225 RKFAESKGTGREKPGPLDFEA 245
Cdd:cd07674   241 RKFAESKGTGKERPGPVGFEE 261
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 228-537 2.38e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  228 AESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTC-PEVDEEGFTVRPDV 306
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdPPPPPPTPEPAPHA 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  307 TQNSTAEPSRFSSSDSDFddeeprkfyvhikPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQR 386
Cdd:PHA03247  2715 LVSATPLPPGPAAARQAS-------------PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  387 PRSAPRTSSCAERLQSeeqvsknlfgppLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDS 466
Cdd:PHA03247  2782 RLTRPAVASLSESRES------------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  467 WVP-----------RPGTPQSPPSCRAPP--PEARGIRAPPLPDSPQPLASSPGPwgleaLAGGDLMPAPADPTAREGLA 533
Cdd:PHA03247  2850 LPLggsvapggdvrRRPPSRSPAAKPAAParPPVRRLARPAVSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPP 2924


                   ....
gi 1858900856  534 APPR 537
Cdd:PHA03247  2925 PPPQ 2928
 
Name Accession Description Interval E-value
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 602-863 8.16e-167

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 (FCH domain only 1 or FCHo1, also known as KIAA0290) and similar proteins; This family corresponds to the MHD found in ubiquitously expressed mammalian membrane-sculpting FCHo1 and similar proteins. FCHo1 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo1 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin. Unlike other F-BAR domain containing proteins, FCHo1 has neither the Src homology 3 (SH3) domain nor any other known domain for interaction with dynamin and actin cytoskeleton. However, it can periodically accumulate at the budding site of clathrin. FCHo1 may utilize a unique action mode for vesicle formation as compared with other F-BAR proteins.


Pssm-ID: 271173  Cd Length: 265  Bit Score: 484.86  E-value: 8.16e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 680
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgATAVPTPL 760
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 761 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 837
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                         250       260
                  ....*....|....*....|....*.
gi 1858900856 838 DLELVGSGYRMSLVKRRFATGMYLVS 863
Cdd:cd09268   240 DIELVGSGYRMSLVKKRFATGKYLVC 265
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 10-245 1.39e-163

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 476.36  E-value: 1.39e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  10 GEKNHGFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLALCHLELT 64
Cdd:cd07674     1 GEKNAGFDVLYHNMKHGQISTKELADFVRERaaieetysksmsklskmasngsplgTFAPMWEVFRVSSDKLALCHLELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  65 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 144
Cdd:cd07674    81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 145 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 224
Cdd:cd07674   161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                         250       260
                  ....*....|....*....|.
gi 1858900856 225 RKFAESKGTGREKPGPLDFEA 245
Cdd:cd07674   241 RKFAESKGTGKERPGPVGFEE 261
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 601-861 5.74e-76

Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that is conserved from yeast to humans.This C-terminal domain is structurally similar to mu homology domains, and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15. This interaction influences muniscin localization. The muniscins provide a combined adaptor-membrane-tubulation activity that is important for regulating endocytosis.


Pssm-ID: 463046  Cd Length: 255  Bit Score: 248.00  E-value: 5.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 601 LPIATAFTEYVHAYFRGHSPSClARVTGELTMTFPAGIVRVFsgtPPPPVLSFRLVHTTAIEHFQPNADLLFsDPSQSDP 680
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK-SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 EtkdFWLNMAALTEALQRQAeqnptasyynvvlLRYQFSR-PGPQSVPLQLSAHWQCGATLTQVSVEYGYRPG-ATAVPT 758
Cdd:pfam10291  76 E---FKVNPQFLASRTPLGA-------------LKYQVHIdPLSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 759 PLTNVQILLPVGEP-VTNVRLQPAATWNLEEKRLTWRLPDVSEA--GGSGRLSASWEPLSGPSTPSPVAAQFTSE-GTTL 834
Cdd:pfam10291 140 VLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTsdGDGGKLIARFMTEGGASKPGGVAVKFEIEtGDTL 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1858900856 835 SGVDLELV---------GSGYRMSLVKRRFATGMYL 861
Cdd:pfam10291 220 SGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-63 1.59e-07

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 49.65  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856    7 HFWGEKNHGFEVLYHSVKQGPISTKELADFIRER-----------------------------TFAPLWEVFRVSSDKLA 57
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERakieeeyakklqklskklravrdtepeygSLSKAWEVLLSETDALA 81


                   ....*.
gi 1858900856   58 LCHLEL 63
Cdd:smart00055  82 KQHLEL 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
 228-537 2.38e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  228 AESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTC-PEVDEEGFTVRPDV 306
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdPPPPPPTPEPAPHA 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  307 TQNSTAEPSRFSSSDSDFddeeprkfyvhikPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQR 386
Cdd:PHA03247  2715 LVSATPLPPGPAAARQAS-------------PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  387 PRSAPRTSSCAERLQSeeqvsknlfgppLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDS 466
Cdd:PHA03247  2782 RLTRPAVASLSESRES------------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  467 WVP-----------RPGTPQSPPSCRAPP--PEARGIRAPPLPDSPQPLASSPGPwgleaLAGGDLMPAPADPTAREGLA 533
Cdd:PHA03247  2850 LPLggsvapggdvrRRPPSRSPAAKPAAParPPVRRLARPAVSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPP 2924


                   ....
gi 1858900856  534 APPR 537
Cdd:PHA03247  2925 PPPQ 2928
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 15-62 6.17e-05

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 41.87  E-value: 6.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900856  15 GFEVLYHSVKQGPISTKELADFIRER------------------------------TFAPLWEVFRVSSDKLALCHLE 62
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERaeieeeyakklqklakkflkkkkkpeddggTLKKAWDELLTETEQLAKQHLK 78
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 452-536 2.89e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 43.76  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 452 LDSPSHAAPGPSPdswvPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAggdlmPAPADPTAREG 531
Cdd:pfam07174  33 LPAVAHADPEPAP----PPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPP-----PPPADPNAPPP 103


                  ....*
gi 1858900856 532 LAAPP 536
Cdd:pfam07174 104 PAVDP 108
 
Name Accession Description Interval E-value
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 602-863 8.16e-167

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 (FCH domain only 1 or FCHo1, also known as KIAA0290) and similar proteins; This family corresponds to the MHD found in ubiquitously expressed mammalian membrane-sculpting FCHo1 and similar proteins. FCHo1 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo1 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin. Unlike other F-BAR domain containing proteins, FCHo1 has neither the Src homology 3 (SH3) domain nor any other known domain for interaction with dynamin and actin cytoskeleton. However, it can periodically accumulate at the budding site of clathrin. FCHo1 may utilize a unique action mode for vesicle formation as compared with other F-BAR proteins.


Pssm-ID: 271173  Cd Length: 265  Bit Score: 484.86  E-value: 8.16e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 680
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgATAVPTPL 760
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 761 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 837
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                         250       260
                  ....*....|....*....|....*.
gi 1858900856 838 DLELVGSGYRMSLVKRRFATGMYLVS 863
Cdd:cd09268   240 DIELVGSGYRMSLVKKRFATGKYLVC 265
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 10-245 1.39e-163

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 476.36  E-value: 1.39e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  10 GEKNHGFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLALCHLELT 64
Cdd:cd07674     1 GEKNAGFDVLYHNMKHGQISTKELADFVRERaaieetysksmsklskmasngsplgTFAPMWEVFRVSSDKLALCHLELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  65 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 144
Cdd:cd07674    81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 145 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 224
Cdd:cd07674   161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                         250       260
                  ....*....|....*....|.
gi 1858900856 225 RKFAESKGTGREKPGPLDFEA 245
Cdd:cd07674   241 RKFAESKGTGKERPGPVGFEE 261
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 602-863 2.33e-159

Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to the MHD found in the metazoan counterparts of yeast Syp1, which includes two ubiquitously expressed membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCH domain only 1 and 2, or FCHo1/FCHo2), neuronal-specific SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. FCHo1/FCHo2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Both FCHo1/FCHo2 contain an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD responsible for the binding of eps15 and intersectin. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271171  Cd Length: 266  Bit Score: 465.43  E-value: 2.33e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 680
Cdd:cd09265     1 PVAAAFTETVHAYFKGADPSkCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPL 760
Cdd:cd09265    81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 761 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 837
Cdd:cd09265   161 LNVQFSVPVDGGVTNVQSEPPATWNAEQKRLLWKLPDISQNsegGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSGV 240

                         250       260
                  ....*....|....*....|....*.
gi 1858900856 838 DLELVGSGYRMSLVKRRFATGMYLVS 863
Cdd:cd09265   241 DIELVGSGYRLSLIKKRFAAGKYLCD 266
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 10-244 6.53e-134

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 399.79  E-value: 6.53e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  10 GEKNHGFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLALCHLELT 64
Cdd:cd07648     1 GEKNNGFDVLYHNMKHGQIAVKELADFLRERatieetyskalnklakqasnssqlgTFAPLWLVLRVSTEKLSELHLQLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  65 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 144
Cdd:cd07648    81 QKLQELIKDVQKYGEEQHKKHKKVKEEESGTAEAVQAIQTTTAALQKAKEAYHARCLELERLRRENASPKEIEKAEAKLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 145 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 224
Cdd:cd07648   161 KAQDEYKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVLSENHSAVGQVHEEFKRQVDELTVDKLL 240

                         250       260
                  ....*....|....*....|
gi 1858900856 225 RKFAESKGTGREKPGPLDFE 244
Cdd:cd07648   241 RQFVESKGTGTEKPELIEFE 260
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 3-244 2.43e-121

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 367.85  E-value: 2.43e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856   3 YFGEHFWGEKNHGFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLA 57
Cdd:cd07673     1 YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERatieeaysrsmtklaksasnysqlgTFAPVWDVFKTSTEKLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  58 LCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMD 137
Cdd:cd07673    81 NCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEGATQREIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 138 KAETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIEN 217
Cdd:cd07673   161 KAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQIGQVHEEFINNMAN 240

                         250       260
                  ....*....|....*....|....*..
gi 1858900856 218 VSVEMLLRKFAESKGTGREKPGPLDFE 244
Cdd:cd07673   241 TTVESLIQKFAESKGTGKERPGPIEFE 267
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 602-864 1.27e-113

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 (FCH domain only 2 or FCHo2) and similar proteins; This family corresponds to the MHD found in the ubiquitously expressed mammalian membrane-sculpting FCHo2 and similar proteins. FCHo2 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engages the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo2 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin.


Pssm-ID: 211378  Cd Length: 267  Bit Score: 347.78  E-value: 1.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 680
Cdd:cd09267     1 PVAVALTESVNAYFKGADPTkCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPL 760
Cdd:cd09267    81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 761 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 837
Cdd:cd09267   161 SNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKsenGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSGV 240

                         250       260
                  ....*....|....*....|....*..
gi 1858900856 838 DLELVGSGYRMSLVKRRFATGMYLVSC 864
Cdd:cd09267   241 DMELVGTGYRLSLNKKRFATGRYMADC 267
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 602-861 3.51e-96

mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 (also known as endophilin-3-interacting protein, SGIP1) and similar proteins; This family corresponds to the MHD found in mammalian neuronal-specific transcript SGIP1 and similar proteins. Unlike other members in this family, SGIP1 does not contain EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis, and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271172  Cd Length: 267  Bit Score: 301.98  E-value: 3.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 680
Cdd:cd09266     1 PVAAAFTETVNAYFKGADPSkCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPL 760
Cdd:cd09266    81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 761 TNVQILLPVGEPVTNVR-LQPAATWNLEEKRLTWRLPDV---SEAGGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSG 836
Cdd:cd09266   161 NNVQFLVPIDGGVTKLQaVLPPAVWNAEQQRILWKIPDIsqkSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                         250       260
                  ....*....|....*....|....*
gi 1858900856 837 VDLELVGSGYRMSLVKRRFATGMYL 861
Cdd:cd09266   241 CDIELVGPGYRFSLIKKRFAAGKYL 265
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 601-861 5.74e-76

Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that is conserved from yeast to humans.This C-terminal domain is structurally similar to mu homology domains, and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15. This interaction influences muniscin localization. The muniscins provide a combined adaptor-membrane-tubulation activity that is important for regulating endocytosis.


Pssm-ID: 463046  Cd Length: 255  Bit Score: 248.00  E-value: 5.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 601 LPIATAFTEYVHAYFRGHSPSClARVTGELTMTFPAGIVRVFsgtPPPPVLSFRLVHTTAIEHFQPNADLLFsDPSQSDP 680
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK-SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 681 EtkdFWLNMAALTEALQRQAeqnptasyynvvlLRYQFSR-PGPQSVPLQLSAHWQCGATLTQVSVEYGYRPG-ATAVPT 758
Cdd:pfam10291  76 E---FKVNPQFLASRTPLGA-------------LKYQVHIdPLSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 759 PLTNVQILLPVGEP-VTNVRLQPAATWNLEEKRLTWRLPDVSEA--GGSGRLSASWEPLSGPSTPSPVAAQFTSE-GTTL 834
Cdd:pfam10291 140 VLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTsdGDGGKLIARFMTEGGASKPGGVAVKFEIEtGDTL 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1858900856 835 SGVDLELV---------GSGYRMSLVKRRFATGMYL 861
Cdd:pfam10291 220 SGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 602-863 1.30e-43

Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family corresponds to the MHD found in muniscins, a novel family of endocytic adaptor proteins. The term, muniscins, has been assigned to name the MHD of proteins with both EFC/F-BAR domain and MHD. These two domains are responsible for the membrane-tubulation activity associated with transmembrane cargo proteins. Members in this family include an endocytic adaptor Syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. Syp1 contains an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD that can directly binds to the endocytic adaptor/scaffold protein Ede1 or a transmembrane stress sensor cargo protein Mid2. Thus, Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress response. Syp1 shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, the membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCHo1/2). FCHo1/2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271165  Cd Length: 244  Bit Score: 158.30  E-value: 1.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 602 PIATAFTEYVHAYFRGHSPSCLArVTGELTMTFPAGIVrvfsgTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDPe 681
Cdd:cd09257     1 GVKAALTEELNAEFKGSSLQSVG-VEGEVQLAVPSSDA-----KPKPAPFNLRLNDASSLEKAAPNVAFLNSVPSGSSP- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 682 tKDFWLNMAALTealqrqaeqnptASYYNVVLLRYQFSrPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgatAVPTPLT 761
Cdd:cd09257    74 -GEFLVNTKAIR------------ASEVGSPILKYSCS-SKLRPVPLRVQTVWRCESHQTSVMLQYVSNP---SLPGPLQ 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 762 NVQILLPV-GEPVTNVRLQPAATWNLEEKRLTWRLPDVSEAGGSGRLSASWEPLSGPST---PSPVAAQFTSEGTTLSGV 837
Cdd:cd09257   137 DVTVIVNVpPGAGENLKSSPGAVWNEEKRRLTWKLPELGVNGEGGELRARFQIDAGQTAekvPFPVLVRCLSEGSTLSGL 216

                         250       260
                  ....*....|....*....|....*...
gi 1858900856 838 DLELVGSGYRM--SLVKRRFATGMYLVS 863
Cdd:cd09257   217 GLEVVALEEEWafIEVKVTRRFGVYHAE 244
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 15-213 5.94e-20

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 88.55  E-value: 5.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  15 GFEVLYHSVKQGPISTKELADFIRER---------------------------TFAPLWEVFRVSSDKLALCHLELTRKL 67
Cdd:cd07610     1 GFELLEKRTELGLDLLKDLREFLKKRaaieeeyaknlqklakkfskkpesgktSLGTSWNSLREETESAATVHEELSEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  68 QDLIKDVLRYGEEQLKTHKKckEEVVSTLDAVQvlsgvsqllpksrenylnrcmdqerLRRESTSQKEmdkaetktKKAA 147
Cdd:cd07610    81 SQLIREPLEKVKEDKEQARK--KELAEGEKLKK-------------------------KLQELWAKLA--------KKAD 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858900856 148 ESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 213
Cdd:cd07610   126 EEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN 191
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-213 2.20e-14

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 73.66  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  15 GFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLALCHLELTRKLQD 69
Cdd:cd07647     6 GFDTLLQRLKEGKKMCKELEDFLKQRakaeedygkallklsksagpgdeigTLKSSWDSLRKETENVANAHIQLAQSLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  70 LIKDVLRYGEEQLKTHKKCKEEVvstlDAVQVLSGVS-QLLPKSRENYLNRCMD----QERLRRES--TSQKEMDKAETK 142
Cdd:cd07647    86 EAEKLEEFREKQKEERKKTEDIM----KRSQKNKKELyKKTMKAKKSYEQKCREkdkaEQAYEKSSsgAQPKEAEKLKKK 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900856 143 TKKAAESL-------RRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 213
Cdd:cd07647   162 AAQCKTSAeeadsayKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCNLGSMQCVKLDEMYEDVRK 239
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 15-200 2.24e-14

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 73.51  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  15 GFEVLYHSVKQGPISTKELADFIRER-------------------------TFAPLWEVFRVSSDKLALCHLELTRKLQD 69
Cdd:cd07649     6 GFEILLQKQLKGKQMQKEMAEFIRERikieeeyaknlsklsqsslaaqeegTLGEAWAQVKKSLADEAEVHLKFSSKLQS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  70 LI-KDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKS---RENYLNRCMDQERLRRESTSQKEMDKAETKTKK 145
Cdd:cd07649    86 EVeKPLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKAlleRQKDLEGKTQQLEIKLSNKTEEDIKKARRKSTQ 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1858900856 146 AAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDT 200
Cdd:cd07649   166 AGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQLRHET 220
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-63 1.59e-07

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 49.65  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856    7 HFWGEKNHGFEVLYHSVKQGPISTKELADFIRER-----------------------------TFAPLWEVFRVSSDKLA 57
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERakieeeyakklqklskklravrdtepeygSLSKAWEVLLSETDALA 81


                   ....*.
gi 1858900856   58 LCHLEL 63
Cdd:smart00055  82 KQHLEL 87
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-213 1.87e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 53.03  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  15 GFEVLYHSVKQGPISTKELADFIRER--------------------------TFAPLWEVFRVSSDKLALCHLELTRKLQ 68
Cdd:cd07672     6 GYDCIIQHLNDGRKNCKEFEDFLKERasieekygkellnlskkkpcgqteinTLKRSLDVFKQQIDNVGQSHIQLAQTLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  69 DLIKDVLRYGEEQlKTHKKCKEEVVSTLDAVQVLSGVSQLlpKSRENYLNRCMDQERL-----RRESTS-QKEMDKAETK 142
Cdd:cd07672    86 DEAKKMEDFRERQ-KLARKKIELIMDAIHKQRAMQFKKTM--ESKKNYEQKCRDKDEAeqavnRNANLVnVKQQEKLFAK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900856 143 ---TKKAAESLRRS----VEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 213
Cdd:cd07672   163 laqSKQNAEDADRLymqnISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDEMYEEVRK 240
PHA03247 PHA03247
large tegument protein UL36; Provisional
 228-537 2.38e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  228 AESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTC-PEVDEEGFTVRPDV 306
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdPPPPPPTPEPAPHA 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  307 TQNSTAEPSRFSSSDSDFddeeprkfyvhikPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQR 386
Cdd:PHA03247  2715 LVSATPLPPGPAAARQAS-------------PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  387 PRSAPRTSSCAERLQSeeqvsknlfgppLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDS 466
Cdd:PHA03247  2782 RLTRPAVASLSESRES------------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  467 WVP-----------RPGTPQSPPSCRAPP--PEARGIRAPPLPDSPQPLASSPGPwgleaLAGGDLMPAPADPTAREGLA 533
Cdd:PHA03247  2850 LPLggsvapggdvrRRPPSRSPAAKPAAParPPVRRLARPAVSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPP 2924


                   ....
gi 1858900856  534 APPR 537
Cdd:PHA03247  2925 PPPQ 2928
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 8-195 5.12e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization.


Pssm-ID: 153342 [Multi-domain]  Cd Length: 239  Bit Score: 51.61  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856   8 FWGEKnhGFEVLYHSVKQGPISTKELADFIRER------------------------TFAPLWEVFRVSSDKLALcHLEL 63
Cdd:cd07658     1 FMGQK--GFEELRRYVKQGGDFCKELATVLQERaelelnyakglsklsgklskasksVSGTLSSAWTCVAEEMES-EADI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  64 TRKL-----QDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAV-----QVLSGVSQLLPKSREN---------YLNRCMDQE 124
Cdd:cd07658    78 HRNLgsaltEEAIKPLRQVLDEQHKTRKPVENEVDKAAKLLtdwrsEQIKVKKKLHGLARENeklqdqvedNKQSCTKQK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 125 RLRRES----TSQKEMDKAETKTKKAAESLRRS-VEKYNS------ARADFEQKMLDSALRFQAMEETHLRHMKALLGSY 193
Cdd:cd07658   158 MLNKLKksaeVQDKEDEKLEAKRKKGEESRLKAeNEYYTCcvrlerLRLEWESALRKGLNQYESLEEERLQHLKHSLSQY 237


                  ..
gi 1858900856 194 AH 195
Cdd:cd07658   238 LR 239
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 225-551 2.32e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  225 RKFAESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTCPEVDEEGFTVRP 304
Cdd:PHA03307    64 RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGS 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  305 DVTQNST-AEPSRFSSSDSDFDDEEPRKFYVHIKPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGK 383
Cdd:PHA03307   144 PGPPPAAsPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPA 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  384 PQRPRSAPRTSScaerlqseeqVSKNLFGPPLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPS 463
Cdd:PHA03307   224 PGRSAADDAGAS----------SSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRE 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  464 PDSwVPRPGTPQSPPsCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAGGDLMPAPADPTAREGLAAPPRRLRSRK 543
Cdd:PHA03307   294 RSP-SPSPSSPGSGP-APSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRP 371


                   ....*...
gi 1858900856  544 VSCPLTRS 551
Cdd:PHA03307   372 SRAPSSPA 379
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
 710-847 4.65e-06

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 49.12  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 710 NVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgatAVPTPLTNVQILLPVGEPVTNVRLQPA---ATWNL 786
Cdd:cd09252    92 KFTLMSYRVDLNSLVSLPVYVKPQISFSGSSGRFEITVGSRQ---NLGKSIENVVVEIPLPKGVKSLRLTAShgsFSFDS 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1858900856 787 EEKRLTWRLPDVSeAGGSGRLSASWEPLSG---PSTPSPVAAQFTSEGTTLSG--VD-LELVGSGYR 847
Cdd:cd09252   169 STKTLVWNIGKLT-PGKTPTLRGSVSLSSGleaPSESPSISVQFKIPGYTPSGlkVDsLDIYNEKYK 234
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 15-62 6.17e-05

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 41.87  E-value: 6.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900856  15 GFEVLYHSVKQGPISTKELADFIRER------------------------------TFAPLWEVFRVSSDKLALCHLE 62
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERaeieeeyakklqklakkflkkkkkpeddggTLKKAWDELLTETEQLAKQHLK 78
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 452-536 2.89e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 43.76  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 452 LDSPSHAAPGPSPdswvPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAggdlmPAPADPTAREG 531
Cdd:pfam07174  33 LPAVAHADPEPAP----PPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPP-----PPPADPNAPPP 103


                  ....*
gi 1858900856 532 LAAPP 536
Cdd:pfam07174 104 PAVDP 108
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
 713-836 3.85e-04

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271157  Cd Length: 245  Bit Score: 43.16  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 713 LLRYQFSRPgPQSVPLQLSAHWQCGATLTQVSVEYGYRPGataVPTPLTNVQILLPVGEPVTNVRLQPA---ATWNLEEK 789
Cdd:cd07954    85 LMSYRTVEP-WSILPITIFPVVSEEGSQLEVVITLKLSES---LQLTAENVEVHIPLPSGVTSLKSKPSdgqAKFDPEKN 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1858900856 790 RLTWRLPDVSEAGGSGRLSASWEPLSGPSTPS----PVAAQFTSEGTTLSG 836
Cdd:cd07954   161 ALVWRIKRIPVGGKEQSLSAHVELGSLAHECPeeapPVSVSFEIPETTGSG 211
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 455-537 3.94e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 455 PSHAAPGPSPDSWVPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLAsSPGPWGLEALAGGDLMPAPADPTAREGLAA 534
Cdd:PRK14951  384 PEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAA-APAAAPAAAPAAVALAPAPPAQAAPETVAI 462


                  ...
gi 1858900856 535 PPR 537
Cdd:PRK14951  463 PVR 465
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
 710-842 4.80e-04

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


Pssm-ID: 271162  Cd Length: 237  Bit Score: 42.60  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 710 NVVLLRYQFSRPGPQSVPLQLSAhWQC-GATLTQVSVEYGyrpgATAVPTPLTNVQILLPV---GEPVTNvrlQPAATWN 785
Cdd:cd09254    87 PVGVLKWRLQGSDESLLPLTINC-WPSeSGGGCDVTIEYE----LNRDDLELNDVVISIPLpsgDAPVVN---SIDGNYE 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1858900856 786 LEEKR--LTWRLPDVSEAGGSGRLSASWEPlSGPSTPSPVAAQFTSEgTTLSGVDLELV 842
Cdd:cd09254   159 YDSRKnvLEWKIPVIDASNSSGSLEFSIPA-DDEDAFFPISVSFTSS-KTFCGVKVVEV 215
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 16-214 7.88e-04

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 41.66  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  16 FEVLYHSVKQGPISTKELADFIRERTFAPLwevfrvssdKLALCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVST 95
Cdd:cd07307     2 LDELEKLLKKLIKDTKKLLDSLKELPAAAE---------KLSEALQELGKELPDLSNTDLGEALEKFGKIQKELEEFRDQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  96 LDaVQVLSGVSQLLpksrENYLN---RCMDQERLRRESTSQkEMDKAETKTKKAAESLRRSV------EKYNSARADFEQ 166
Cdd:cd07307    73 LE-QKLENKVIEPL----KEYLKkdlKEIKKRRKKLDKARL-DYDAAREKLKKLRKKKKDSSklaeaeEELQEAKEKYEE 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1858900856 167 KMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQN 214
Cdd:cd07307   147 LREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 13-216 8.21e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 41.87  E-value: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  13 NHGFEVLYHSVKQGPISTKELADFIRERTFA----------------------PLWEVF---RVSSDKLALCHLELTRKL 67
Cdd:cd07671     4 NTGYEILLQRLLDGRKMCKDVEELLKQRAQAeerygkelvqiarkaggqteinTLKASFdqlKQQIENIGNSHIQLAGML 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  68 QDLIKDVLRYGEEQLKTHKKCKeevvSTLDAVQVlSGVSqLLPK---SRENYLNRCMD----QERLRRESTS--QKEMDK 138
Cdd:cd07671    84 REELKSLEEFRERQKEQRKKYE----AVMERVQK-SKVS-LYKKtmeSKKTYEQRCREadeaEQTFERSSSTgnPKQSEK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 139 AETKTKKAAES-------LRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEF 211
Cdd:cd07671   158 SQNKAKQCRDAateaervYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCNHFSMQCVKDDELYEEV 237


                  ....*
gi 1858900856 212 KQNIE 216
Cdd:cd07671   238 RTTLE 242
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 276-538 2.05e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  276 PEPPAAVDFLE--PDSGTCPEVDEEGFTVRPDVTQNSTAEPSRFSSSDSDFDDEEPRKFYVHIKPAPARAPACSPEAAAA 353
Cdd:PHA03307   167 ASSRQAALPLSspEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSG 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  354 QLRATAGSLILPPGPGGTMKRHSSRDAAGKPQRPRSAPRTSSCAERLQSEEQVSKNLFGPPLESAFDHEDFTGSSSlgft 433
Cdd:PHA03307   247 CGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR---- 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  434 sspspfSSSSPENVEDSGLDSPSHAAPGPSPDswvpRPGTPQSP-PSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLE 512
Cdd:PHA03307   323 ------ESSSSSTSSSSESSRGAAVSPGPSPS----RSPSPSRPpPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARA 392

                          250       260
                   ....*....|....*....|....*.
gi 1858900856  513 ALAGgdlMPAPADPTAREGLAAPPRR 538
Cdd:PHA03307   393 AVAG---RARRRDATGRFPAGRPRPS 415
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 459-537 2.96e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 41.27  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 459 APGPSPDSW-VPRPGTPQSPPSCRAPPPEARgirAPPLPDSPQPLASSPGPwglealaggdlmPAPADPTAREGLAAPPR 537
Cdd:PRK14965  381 APAPPSAAWgAPTPAAPAAPPPAAAPPVPPA---APARPAAARPAPAPAPP------------AAAAPPARSADPAAAAS 445
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 365-536 3.71e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 365 PPGPGGTMKRHSSRDAAGKPQRPRSAPRTSSCAErlQSEEQVSKNLFGPPLESAFDHEDFTGSSSLGFTSSPSPFSSSSP 444
Cdd:PRK07764  602 APASSGPPEEAARPAAPAAPAAPAAPAPAGAAAA--PAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA 679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856 445 ENVE--DSGLDSPSHAAPGPSPD---SWVPRPGTPQSPPSCRAPPPEARGiRAPPLPDSPQPLASSPGPWGLEALAGGDL 519
Cdd:PRK07764  680 APPPapAPAAPAAPAGAAPAQPApapAATPPAGQADDPAAQPPQAAQGAS-APSPAADDPVPLPPEPDDPPDPAGAPAQP 758

                         170
                  ....*....|....*..
gi 1858900856 520 MPAPADPTAREGLAAPP 536
Cdd:PRK07764  759 PPPPAPAPAAAPAAAPP 775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 455-592 5.06e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900856  455 PSHAAPGPSPDSWVPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAGGDLMPA-PADPTAREGLA 533
Cdd:PHA03247  2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPApPAAPAAGPPRR 2782

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1858900856  534 APPRRLRSRKVSCPLTRSNGDLSrSLSPSPLGSSAASTALERPSFLSQTGHGVSRGPSP 592
Cdd:PHA03247  2783 LTRPAVASLSESRESLPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP 2840
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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