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Conserved domains on  [gi|19071867|dbj|BAB85677.1|]
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up-regulated in liver cancer 1 [Homo sapiens]

Protein Classification

BAR_ASAP3 and PH_ASAP domain-containing protein (domain architecture ID 11576978)

protein containing domains BAR_ASAP3, PH_ASAP, ArfGap, and ANK

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_ASAP3 cd07640
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
35-243 5.56e-139

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP3 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3) is also known as ACAP4 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 4), DDEFL1 (Development and Differentiation Enhancing Factor-Like 1), or centaurin beta-6. It is an Arf6-specific GTPase activating protein (GAP) and is co-localized with Arf6 in ruffling membranes upon EGF stimulation. ASAP3 is implicated in the pathogenesis of hepatocellular carcinoma and plays a role in regulating cell migration and invasion. ASAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


:

Pssm-ID: 153324  Cd Length: 213  Bit Score: 416.32  E-value: 5.56e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  35 RGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFK 114
Cdd:cd07640   1 RSTAAALEESLEGDQASLQRIKKIVKAIHNSGLNHVENEEQYTEALENLGNSHLSQNNHELSTGFLNLAVFTREVTALFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 115 NLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGI----PGEVAQDMQRERRIFQ 190
Cdd:cd07640  81 NLVQNLNNIVSFPLDSLLKGQLRDGRLESKKQMEKAWKDYEAKIGKLEKERREKQKQHGLirldMTDTAEDMQRERRNFQ 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 19071867 191 LHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKL 243
Cdd:cd07640 161 LHMCEYLLKAQESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQNLGPFIEKL 213
PH_ASAP cd13251
ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs ...
294-400 4.01e-56

ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs (ASAP1, ASAP2, and ASAP3) function as an Arf-specific GAPs, participates in rhodopsin trafficking, is associated with tumor cell metastasis, modulates phagocytosis, promotes cell proliferation, facilitates vesicle budding, Golgi exocytosis, and regulates vesicle coat assembly via a Bin/Amphiphysin/Rvs domain. ASAPs contain an NH2-terminal BAR domain, a tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 (SH3) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270071  Cd Length: 108  Bit Score: 189.88  E-value: 4.01e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 294 QHQGNKQFGTEKVGFLYKKSDG-IRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEKKCFDLVTHNRTY 372
Cdd:cd13251   1 QQQGNKSHGTEKSGYLLKKSEGkIRKVWQKRRCSIKDGFLTISHADENKPPAKLNLLTCQVKLVPEDKKCFDLISHNRTY 80
                        90       100
                ....*....|....*....|....*...
gi 19071867 373 HFQAEDEHECEAWVSVLQNSKDEALSSA 400
Cdd:cd13251  81 HFQAEDENDANAWMSVLKNSKEQALNKA 108
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
428-543 5.05e-41

Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs.


:

Pssm-ID: 307528  Cd Length: 117  Bit Score: 148.55  E-value: 5.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   428 LIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVME 507
Cdd:pfam01412   3 VLRELRKLPGNKVCADCGAPNPTWASLNLGIFICIRCSGVHRSLGVHISKVRSLTLDTWTPEQLEFMKAGGNDRANEYWE 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19071867   508 AQLPShgGPKPSAESDMGTRRDYIMAKYVEHRFARR 543
Cdd:pfam01412  83 ANLPK--PLPPPPSSDQEKRESFIRAKYVEKKFAEP 116
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
590-674 3.55e-18

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


:

Pssm-ID: 238125  Cd Length: 126  Bit Score: 83.59  E-value: 3.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 590 LHLAVKVANqasLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKE 669
Cdd:cd00204  44 LHLAAKNGH---LEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLDVVKLLLKHGADVNARDKDGRTPLHLAAKNGHLE 120

                ....*
gi 19071867 670 CEELL 674
Cdd:cd00204 121 VVKLL 125
Herpes_ICP4_C super family cl28033
Herpesvirus ICP4-like protein C-terminal region; The immediate-early protein ICP4 ...
723-897 7.40e-03

Herpesvirus ICP4-like protein C-terminal region; The immediate-early protein ICP4 (infected-cell polypeptide 4) is required for efficient transcription of early and late viral genes and is thus essential for productive infection. ICP4 is a large phosphoprotein that binds DNA in a sequence specific manner as a homodimer. ICP4 represses transcription from LAT, ICP4 and ORF-P that have high-affinity a ICP4 binding site that spans the transcription initiation site. ICP4 proteins have two highly conserved regions, this family contains the C-terminal region that probably acts as an enhancer for the N-terminal region.


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 332854  Cd Length: 1352  Bit Score: 40.15  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   723 SGRLDISNKTYETVASLGAATPQGESEDCPPPLPVKNSSRTLVQGCARHASGDR--SEVSSLSSEAPETPESLGSPasss 800
Cdd:PHA03307  227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSrpGPASSSSSPRERSPSPSPSS---- 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   801 slmsplePGDPSQAPPNSEEGLREPPGTSRPSLTSGTTPSEMYLPVRFSSESTRSyrrgARSPEDGPSARQPLPRRNVPV 880
Cdd:PHA03307  303 -------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS----PSPSRPPPPADPSSPRKRPRP 371
                         170
                  ....*....|....*..
gi 19071867   881 GITEGDGSRTGSLPASS 897
Cdd:PHA03307  372 SRAPSSPAASAGRPTRR 388
 
Name Accession Description Interval E-value
BAR_ASAP3 cd07640
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
35-243 5.56e-139

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP3 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3) is also known as ACAP4 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 4), DDEFL1 (Development and Differentiation Enhancing Factor-Like 1), or centaurin beta-6. It is an Arf6-specific GTPase activating protein (GAP) and is co-localized with Arf6 in ruffling membranes upon EGF stimulation. ASAP3 is implicated in the pathogenesis of hepatocellular carcinoma and plays a role in regulating cell migration and invasion. ASAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153324  Cd Length: 213  Bit Score: 416.32  E-value: 5.56e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  35 RGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFK 114
Cdd:cd07640   1 RSTAAALEESLEGDQASLQRIKKIVKAIHNSGLNHVENEEQYTEALENLGNSHLSQNNHELSTGFLNLAVFTREVTALFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 115 NLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGI----PGEVAQDMQRERRIFQ 190
Cdd:cd07640  81 NLVQNLNNIVSFPLDSLLKGQLRDGRLESKKQMEKAWKDYEAKIGKLEKERREKQKQHGLirldMTDTAEDMQRERRNFQ 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 19071867 191 LHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKL 243
Cdd:cd07640 161 LHMCEYLLKAQESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQNLGPFIEKL 213
PH_ASAP cd13251
ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs ...
294-400 4.01e-56

ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs (ASAP1, ASAP2, and ASAP3) function as an Arf-specific GAPs, participates in rhodopsin trafficking, is associated with tumor cell metastasis, modulates phagocytosis, promotes cell proliferation, facilitates vesicle budding, Golgi exocytosis, and regulates vesicle coat assembly via a Bin/Amphiphysin/Rvs domain. ASAPs contain an NH2-terminal BAR domain, a tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 (SH3) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270071  Cd Length: 108  Bit Score: 189.88  E-value: 4.01e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 294 QHQGNKQFGTEKVGFLYKKSDG-IRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEKKCFDLVTHNRTY 372
Cdd:cd13251   1 QQQGNKSHGTEKSGYLLKKSEGkIRKVWQKRRCSIKDGFLTISHADENKPPAKLNLLTCQVKLVPEDKKCFDLISHNRTY 80
                        90       100
                ....*....|....*....|....*...
gi 19071867 373 HFQAEDEHECEAWVSVLQNSKDEALSSA 400
Cdd:cd13251  81 HFQAEDENDANAWMSVLKNSKEQALNKA 108
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
428-543 5.05e-41

Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs.


Pssm-ID: 307528  Cd Length: 117  Bit Score: 148.55  E-value: 5.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   428 LIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVME 507
Cdd:pfam01412   3 VLRELRKLPGNKVCADCGAPNPTWASLNLGIFICIRCSGVHRSLGVHISKVRSLTLDTWTPEQLEFMKAGGNDRANEYWE 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19071867   508 AQLPShgGPKPSAESDMGTRRDYIMAKYVEHRFARR 543
Cdd:pfam01412  83 ANLPK--PLPPPPSSDQEKRESFIRAKYVEKKFAEP 116
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
429-540 1.67e-29

Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs.


Pssm-ID: 214518  Cd Length: 119  Bit Score: 115.90  E-value: 1.67e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867    429 IAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEA 508
Cdd:smart00105   1 LKLLRSIPGNKKCFDCGAPNPTWASVNLGVFLCIECSGIHRSLGVHISKVRSLTLDTWTEEELRLLQKGGNENANSIWES 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 19071867    509 QLpsHGGPKPSAESDMGTRRD-YIMAKYVEHRF 540
Cdd:smart00105  81 NL--DDFSLKPPDDDDQQKYEsFIAAKYEEKLF 111
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
422-540 6.24e-25

GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ARF-mediated vesicular transport [Intracellular trafficking and secretion];


Pssm-ID: 227651  Cd Length: 319  Bit Score: 107.56  E-value: 6.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 422 HDLTKLLIAeVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTS 501
Cdd:COG5347   5 SEDRKLLKL-LKSDSSNKKCADCGAPNPTWASVNLGVFLCIDCAGVHRSLGVHISKVKSLTLDNWTEEELRRMEVGGNSN 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19071867 502 FNEVMEAQLPSHGGPKPSAESDMGTRRDYIMAKYVEHRF 540
Cdd:COG5347  84 ANRFYEKNLLDQLLLPIKAKYDSSVAKKYIRKKYELKKF 122
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
590-674 3.55e-18

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 83.59  E-value: 3.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 590 LHLAVKVANqasLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKE 669
Cdd:cd00204  44 LHLAAKNGH---LEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLDVVKLLLKHGADVNARDKDGRTPLHLAAKNGHLE 120

                ....*
gi 19071867 670 CEELL 674
Cdd:cd00204 121 VVKLL 125
BAR_3 pfam16746
BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or ...
81-261 7.25e-13

BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or adaptor protein containing PH domain, PTB domain, and leucine zipper motif proteins in higher eukaryotes. This BAR domain contains four helices whereas the other classical BAR domains contain only three helices. The first three helices form an antiparallel coiled-coil, while the fourth helix, is unique to APPL1. BAR domains take part in many varied biological processes such as fission of synaptic vesicles, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, apoptosis, secretory vesicle fusion, and tissue differentiation.


Pssm-ID: 318867  Cd Length: 235  Bit Score: 69.12  E-value: 7.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867    81 ESLGNSHLSQNSHELSTGFlnlavftREVAALFKNLIQNLNNIVSFPLDSLMKGQLRdGRQDSKKQLEKAWKDYEAKMAK 160
Cdd:pfam16746  65 QFIGDEETDESLKKFSQLL-------QEMEDFHTILLDQAQRTIIKPLEKFRKEDIG-EVKETKKKFDKASEKLDAALEK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   161 ---LEKERDRARVTggipgEVAQDMQRERRIFQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLF 237
Cdd:pfam16746 137 naqLSRKKKPSELE-----EADNELDATRKCFHHTALDYVLQINELQERKKFEILEPLLSFMHAQFTFFHQGHELFKDLE 211
                         170       180
                  ....*....|....*....|....
gi 19071867   238 PFIEKLAASVHALHQAQEDELQKL 261
Cdd:pfam16746 212 PYMKDLQAQLQNTREETAEEKEEL 235
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
303-390 2.55e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 65.65  E-value: 2.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867    303 TEKVGFLYKKSDGIRRVWQKRKCGVKYGCLTISHS----TINRPPVKLTLLTCQVRPNPE-----EKKCFDLVTHNR-TY 372
Cdd:smart00233   1 VIKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSkkdkKSYKPKGSIDLSGCTVREAPDpdsskKPHCFEIKTSDRkTL 80
                           90
                   ....*....|....*...
gi 19071867    373 HFQAEDEHECEAWVSVLQ 390
Cdd:smart00233  81 LLQAESEEEREKWVEALR 98
Ank_2 pfam12796
Ankyrin repeats (3 copies);
590-675 2.79e-12

Ankyrin repeats (3 copies);


Pssm-ID: 315466  Cd Length: 92  Bit Score: 65.52  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   590 LHLAVKvanQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKgRALVGTVNEAGETALDIARKKHHKE 669
Cdd:pfam12796   1 LHLAAK---NGDLELVKLLLEEGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDKNGRTALHYAARSGHLE 76

                  ....*..
gi 19071867   670 C-EELLE 675
Cdd:pfam12796  77 IvKLLLE 83
PLN03114 PLN03114
ADP-ribosylation factor GTPase-activating protein AGD10; Provisional
431-499 2.36e-11

ADP-ribosylation factor GTPase-activating protein AGD10; Provisional


Pssm-ID: 178661  Cd Length: 395  Bit Score: 66.42  E-value: 2.36e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19071867  431 EVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGN 499
Cdd:PLN03114  15 KLKAKSDNKICFDCNAKNPTWASVTYGIFLCIDCSAVHRSLGVHISFVRSTNLDSWSSEQLKMMIYGGN 83
PH pfam00169
PH domain; PH stands for pleckstrin homology.
307-390 7.51e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 306640  Cd Length: 105  Bit Score: 58.35  E-value: 7.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   307 GFLYKKSDGIRRVWQKRKCGVKYGCLTISHSTI----NRPPVKLTLLTCQVR-----PNPEEKKCFDLVTHN----RTYH 373
Cdd:pfam00169   5 GWLLKKGGGKKKSWKKRYFVLFDGSLLYYKDDKsgksKEPKGSISLSGCEVVevvapDSPKRKFCFELRTGErtggRTYL 84
                          90
                  ....*....|....*..
gi 19071867   374 FQAEDEHECEAWVSVLQ 390
Cdd:pfam00169  85 LQAESEEERKDWIKAIQ 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
590-681 1.08e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 59.45  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 590 LHLAVKVANQA--SLPLVDFIIQNGGHLDAKAA---DGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARK 664
Cdd:COG0666 110 LHLAALNGNPPegNIEVAKLLLEAGADLDVNNLrdeDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAK 189
                        90
                ....*....|....*..
gi 19071867 665 KHHKECEELLEQAQAGT 681
Cdd:COG0666 190 NGRIELVKLLLDKGLHL 206
PHA03100 PHA03100
ankyrin repeat protein; Provisional
590-674 5.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984  Cd Length: 422  Bit Score: 56.21  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  590 LHLAVKVaNQASLPLVDFIIQNGGHLDAK--------------AAD--GNTALHYAALYNQPDCLKLLLKGRALVGTVNE 653
Cdd:PHA03100 145 LHLYLES-NKIDLKILKLLIDKGVDINAKnrvnyllsygvpinIKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
                         90       100
                 ....*....|....*....|.
gi 19071867  654 AGETALDIARKKHHKECEELL 674
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLL 244
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
621-643 1.01e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603  Cd Length: 30  Bit Score: 39.11  E-value: 1.01e-03
                           10        20
                   ....*....|....*....|...
gi 19071867    621 DGNTALHYAALYNQPDCLKLLLK 643
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
723-897 7.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039  Cd Length: 1352  Bit Score: 40.15  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   723 SGRLDISNKTYETVASLGAATPQGESEDCPPPLPVKNSSRTLVQGCARHASGDR--SEVSSLSSEAPETPESLGSPasss 800
Cdd:PHA03307  227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSrpGPASSSSSPRERSPSPSPSS---- 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   801 slmsplePGDPSQAPPNSEEGLREPPGTSRPSLTSGTTPSEMYLPVRFSSESTRSyrrgARSPEDGPSARQPLPRRNVPV 880
Cdd:PHA03307  303 -------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS----PSPSRPPPPADPSSPRKRPRP 371
                         170
                  ....*....|....*..
gi 19071867   881 GITEGDGSRTGSLPASS 897
Cdd:PHA03307  372 SRAPSSPAASAGRPTRR 388
 
Name Accession Description Interval E-value
BAR_ASAP3 cd07640
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
35-243 5.56e-139

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP3 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3) is also known as ACAP4 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 4), DDEFL1 (Development and Differentiation Enhancing Factor-Like 1), or centaurin beta-6. It is an Arf6-specific GTPase activating protein (GAP) and is co-localized with Arf6 in ruffling membranes upon EGF stimulation. ASAP3 is implicated in the pathogenesis of hepatocellular carcinoma and plays a role in regulating cell migration and invasion. ASAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153324  Cd Length: 213  Bit Score: 416.32  E-value: 5.56e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  35 RGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFK 114
Cdd:cd07640   1 RSTAAALEESLEGDQASLQRIKKIVKAIHNSGLNHVENEEQYTEALENLGNSHLSQNNHELSTGFLNLAVFTREVTALFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 115 NLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGI----PGEVAQDMQRERRIFQ 190
Cdd:cd07640  81 NLVQNLNNIVSFPLDSLLKGQLRDGRLESKKQMEKAWKDYEAKIGKLEKERREKQKQHGLirldMTDTAEDMQRERRNFQ 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 19071867 191 LHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKL 243
Cdd:cd07640 161 LHMCEYLLKAQESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQNLGPFIEKL 213
BAR_ASAPs cd07604
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
35-243 3.42e-104

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of ASAPs (ArfGAP with SH3 domain, ANK repeat and PH domain containing proteins), which are Arf GTPase activating proteins (GAPs) with similarity to ACAPs (ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins) in that they contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and ankyrin (ANK) repeats. However, ASAPs contain an additional C-terminal SH3 domain. ASAPs function in regulating cell growth, migration, and invasion. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3. ASAP1 and ASAP2 shows GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but is able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153288  Cd Length: 215  Bit Score: 325.52  E-value: 3.42e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  35 RGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFK 114
Cdd:cd07604   1 RNTVGALEESLEGDRVGLQKLKKAVKAIHNSGLAHVENELQFAEALEKLGSKALSREEEDLGAAFLKFSVFTKELAALFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 115 NLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKER-----DRARVTGGIPG-EVAQDMQRERRI 188
Cdd:cd07604  81 NLMQNLNNIIMFPLDSLLKGDLKGSKGDLKKPFDKAWKDYETKASKIEKEKkqlakEAGMIRTEITGaEIAEEMEKERRM 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19071867 189 FQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKL 243
Cdd:cd07604 161 FQLQMCEYLIKVNEIKTKKGVDLLQHLVEYYHAQNSYFQDGLKVIEHFRPYIEKL 215
BAR_ASAP2 cd07642
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
35-243 5.99e-79

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP2 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 2) is also known as DDEF2 (Development and Differentiation Enhancing Factor 2), AMAP2, centaurin beta-3, or PAG3. ASAP2 mediates the functions of Arf GTPases vial dual mechanisms: it exhibits GTPase activating protein (GAP) activity towards class I (Arf1) and II (Arf5) Arfs; and binds class III Arfs (GTP-Arf6) stably without GAP activity. It binds paxillin and is implicated in Fcgamma receptor-mediated phagocytosis in macrophages and in cell migration. ASAP2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153326  Cd Length: 215  Bit Score: 257.65  E-value: 5.99e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  35 RGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFK 114
Cdd:cd07642   1 RNTVVAIEEALDVDRTVLYKMKKSVKAIHTSGLAHVENEEQYTQALEKFGSNCVCRDDPDLGSAFLKFSVFTKELTALFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 115 NLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKE-RDRARVTGGIP-----GEVAQDMQRERRI 188
Cdd:cd07642  81 NLVQNMNNIITFPLDSLLKGDLKGVKGDLKKPFDKAWKDYETKVTKIEKEkKEHAKMHGMIRteisgAEIAEEMEKERRF 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19071867 189 FQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKL 243
Cdd:cd07642 161 FQLQMCEYLLKVNEIKIKKGVDLLQNLIKYFHAQCNFFQDGLKAVETLKPSIEKL 215
BAR_ASAP1 cd07641
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
42-243 9.64e-60

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 1) is also known as DDEF1 (Development and Differentiation Enhancing Factor 1), AMAP1, centaurin beta-4, or PAG2. ASAP1 is an Arf GTPase activating protein (GAP) with activity towards Arf1 and Arf5 but not Arf6 However, it has been shown to bind GTP-Arf6 stably without GAP activity. It has been implicated in cell growth, migration, and survival, as well as in tumor invasion and malignancy. It binds paxillin and cortactin, two components of invadopodia which are essential for tumor invasiveness. It also binds focal adhesion kinase (FAK) and the SH2/SH3 adaptor CrkL. ASAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153325  Cd Length: 215  Bit Score: 204.14  E-value: 9.64e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  42 EEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFKNLIQNLN 121
Cdd:cd07641   8 EEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQALDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 122 NIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKE-RDRARVTGGI-----PGEVAQDMQRERRIFQLHMCE 195
Cdd:cd07641  88 HNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEkREHAKQHGMIrteitGAEIAEEMEKERRLFQLQMCE 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19071867 196 YLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKL 243
Cdd:cd07641 168 YLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKL 215
PH_ASAP cd13251
ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs ...
294-400 4.01e-56

ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs (ASAP1, ASAP2, and ASAP3) function as an Arf-specific GAPs, participates in rhodopsin trafficking, is associated with tumor cell metastasis, modulates phagocytosis, promotes cell proliferation, facilitates vesicle budding, Golgi exocytosis, and regulates vesicle coat assembly via a Bin/Amphiphysin/Rvs domain. ASAPs contain an NH2-terminal BAR domain, a tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 (SH3) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270071  Cd Length: 108  Bit Score: 189.88  E-value: 4.01e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 294 QHQGNKQFGTEKVGFLYKKSDG-IRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEKKCFDLVTHNRTY 372
Cdd:cd13251   1 QQQGNKSHGTEKSGYLLKKSEGkIRKVWQKRRCSIKDGFLTISHADENKPPAKLNLLTCQVKLVPEDKKCFDLISHNRTY 80
                        90       100
                ....*....|....*....|....*...
gi 19071867 373 HFQAEDEHECEAWVSVLQNSKDEALSSA 400
Cdd:cd13251  81 HFQAEDENDANAWMSVLKNSKEQALNKA 108
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
428-543 5.05e-41

Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs.


Pssm-ID: 307528  Cd Length: 117  Bit Score: 148.55  E-value: 5.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   428 LIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVME 507
Cdd:pfam01412   3 VLRELRKLPGNKVCADCGAPNPTWASLNLGIFICIRCSGVHRSLGVHISKVRSLTLDTWTPEQLEFMKAGGNDRANEYWE 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19071867   508 AQLPShgGPKPSAESDMGTRRDYIMAKYVEHRFARR 543
Cdd:pfam01412  83 ANLPK--PLPPPPSSDQEKRESFIRAKYVEKKFAEP 116
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
429-540 1.67e-29

Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs.


Pssm-ID: 214518  Cd Length: 119  Bit Score: 115.90  E-value: 1.67e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867    429 IAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEA 508
Cdd:smart00105   1 LKLLRSIPGNKKCFDCGAPNPTWASVNLGVFLCIECSGIHRSLGVHISKVRSLTLDTWTEEELRLLQKGGNENANSIWES 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 19071867    509 QLpsHGGPKPSAESDMGTRRD-YIMAKYVEHRF 540
Cdd:smart00105  81 NL--DDFSLKPPDDDDQQKYEsFIAAKYEEKLF 111
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
422-540 6.24e-25

GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ARF-mediated vesicular transport [Intracellular trafficking and secretion];


Pssm-ID: 227651  Cd Length: 319  Bit Score: 107.56  E-value: 6.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 422 HDLTKLLIAeVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTS 501
Cdd:COG5347   5 SEDRKLLKL-LKSDSSNKKCADCGAPNPTWASVNLGVFLCIDCAGVHRSLGVHISKVKSLTLDNWTEEELRRMEVGGNSN 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19071867 502 FNEVMEAQLPSHGGPKPSAESDMGTRRDYIMAKYVEHRF 540
Cdd:COG5347  84 ANRFYEKNLLDQLLLPIKAKYDSSVAKKYIRKKYELKKF 122
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
45-238 3.64e-21

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  Cd Length: 194  Bit Score: 94.05  E-value: 3.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  45 LEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFKNLIQNLNNIV 124
Cdd:cd07307   2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 125 SFPLDSLMKGQLRDgRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGIPgEVAQDMQRERRIFQLHMCEYLLKAGESQ 204
Cdd:cd07307  82 IEPLKEYLKKDLKE-IKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLA-EAEEELQEAKEKYEELREELIEDLNKLE 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 19071867 205 MKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFP 238
Cdd:cd07307 160 EKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLP 193
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
590-674 3.55e-18

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 83.59  E-value: 3.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 590 LHLAVKVANqasLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKE 669
Cdd:cd00204  44 LHLAAKNGH---LEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLDVVKLLLKHGADVNARDKDGRTPLHLAAKNGHLE 120

                ....*
gi 19071867 670 CEELL 674
Cdd:cd00204 121 VVKLL 125
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
590-688 4.95e-16

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 77.04  E-value: 4.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 590 LHLAVKVANqasLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKE 669
Cdd:cd00204  11 LHLAASNGH---LEVVKLLLENGADVNAKDNDGRTPLHLAAKNGHLEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLD 87
                        90       100
                ....*....|....*....|....*
gi 19071867 670 CEELLEQAQAGTFAF------PLHV 688
Cdd:cd00204  88 VVKLLLKHGADVNARdkdgrtPLHL 112
BAR_3 pfam16746
BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or ...
81-261 7.25e-13

BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or adaptor protein containing PH domain, PTB domain, and leucine zipper motif proteins in higher eukaryotes. This BAR domain contains four helices whereas the other classical BAR domains contain only three helices. The first three helices form an antiparallel coiled-coil, while the fourth helix, is unique to APPL1. BAR domains take part in many varied biological processes such as fission of synaptic vesicles, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, apoptosis, secretory vesicle fusion, and tissue differentiation.


Pssm-ID: 318867  Cd Length: 235  Bit Score: 69.12  E-value: 7.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867    81 ESLGNSHLSQNSHELSTGFlnlavftREVAALFKNLIQNLNNIVSFPLDSLMKGQLRdGRQDSKKQLEKAWKDYEAKMAK 160
Cdd:pfam16746  65 QFIGDEETDESLKKFSQLL-------QEMEDFHTILLDQAQRTIIKPLEKFRKEDIG-EVKETKKKFDKASEKLDAALEK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   161 ---LEKERDRARVTggipgEVAQDMQRERRIFQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLF 237
Cdd:pfam16746 137 naqLSRKKKPSELE-----EADNELDATRKCFHHTALDYVLQINELQERKKFEILEPLLSFMHAQFTFFHQGHELFKDLE 211
                         170       180
                  ....*....|....*....|....
gi 19071867   238 PFIEKLAASVHALHQAQEDELQKL 261
Cdd:pfam16746 212 PYMKDLQAQLQNTREETAEEKEEL 235
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
305-389 1.76e-12

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388  Cd Length: 92  Bit Score: 66.03  E-value: 1.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKSDGIRRVWQKRKCGVKYGCLTIS---HSTINRPPVKLTL-LTCQVRPNPEEKK--CFDLVT-HNRTYHFQAE 377
Cdd:cd00821   1 KEGYLLKRGGGGLKSWKKRWFVLFEGVLLYYkskKDSSYKPKGSIPLsGILEVEEVSPKERphCFELVTpDGRTYYLQAD 80
                        90
                ....*....|..
gi 19071867 378 DEHECEAWVSVL 389
Cdd:cd00821  81 SEEERQEWLKAL 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
303-390 2.55e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 65.65  E-value: 2.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867    303 TEKVGFLYKKSDGIRRVWQKRKCGVKYGCLTISHS----TINRPPVKLTLLTCQVRPNPE-----EKKCFDLVTHNR-TY 372
Cdd:smart00233   1 VIKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSkkdkKSYKPKGSIDLSGCTVREAPDpdsskKPHCFEIKTSDRkTL 80
                           90
                   ....*....|....*...
gi 19071867    373 HFQAEDEHECEAWVSVLQ 390
Cdd:smart00233  81 LLQAESEEEREKWVEALR 98
Ank_2 pfam12796
Ankyrin repeats (3 copies);
590-675 2.79e-12

Ankyrin repeats (3 copies);


Pssm-ID: 315466  Cd Length: 92  Bit Score: 65.52  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   590 LHLAVKvanQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKgRALVGTVNEAGETALDIARKKHHKE 669
Cdd:pfam12796   1 LHLAAK---NGDLELVKLLLEEGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDKNGRTALHYAARSGHLE 76

                  ....*..
gi 19071867   670 C-EELLE 675
Cdd:pfam12796  77 IvKLLLE 83
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
307-398 1.69e-11

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270070  Cd Length: 98  Bit Score: 63.39  E-value: 1.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 307 GFLYKKSDGIRRVWQKRKCGVKYGCLTISHSTINRPPVKLT--LLTCQVRP--NPEEKKCFDLVTHNRTYHFQAEDEHEC 382
Cdd:cd13250   3 GYLFKRSSNAFKTWKRRWFSLQNGQLYYQKRDKKDEPTVMVedLRLCTVKPteDSDRRFCFEVISPTKSYMLQAESEEDR 82
                        90
                ....*....|....*.
gi 19071867 383 EAWVSVLQNSKDEALS 398
Cdd:cd13250  83 QAWIQAIQSAIASALN 98
PLN03114 PLN03114
ADP-ribosylation factor GTPase-activating protein AGD10; Provisional
431-499 2.36e-11

ADP-ribosylation factor GTPase-activating protein AGD10; Provisional


Pssm-ID: 178661  Cd Length: 395  Bit Score: 66.42  E-value: 2.36e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19071867  431 EVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGN 499
Cdd:PLN03114  15 KLKAKSDNKICFDCNAKNPTWASVTYGIFLCIDCSAVHRSLGVHISFVRSTNLDSWSSEQLKMMIYGGN 83
BAR_GAP10-like cd07634
The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like; BAR domains are ...
114-239 7.71e-11

The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This group is composed of uncharacterized proteins called Rho GTPase activating protein (GAP) 10-like. GAP10-like may be a GAP with activity towards RhoA and Cdc42. Similar to GRAF and GRAF2, it contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domains of the related proteins GRAF and OPHN1, directly interact with their Rho GAP domains and inhibit theiractivity. The autoinhibited proteins are capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153318  Cd Length: 207  Bit Score: 62.74  E-value: 7.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 114 KNLIQNLNNIVSFPLDSLMKGQL---RDGRQDSKKQLEKAWKDYEaKMAKLEKERDRARVTggipgEVAQDMQRERRIFQ 190
Cdd:cd07634  84 RRLIQNANDVLIAPLEKFRKEQIgaaKDGKKKFDKESEKYYSILE-KHLNLSAKKKESHLQ-----RADTQIDREHQNFY 157
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19071867 191 LHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPF 239
Cdd:cd07634 158 EASLEYVFKIQEVQEKKKFEFVEPLLAFLQGLFTFYHEGYELAQEFAPY 206
PH_SIP3 cd13280
Snf1p-interacting protein 3 Pleckstrin homology (PH) domain; SIP3 interacts with SNF1 protein ...
304-398 1.92e-10

Snf1p-interacting protein 3 Pleckstrin homology (PH) domain; SIP3 interacts with SNF1 protein kinase and activates transcription when anchored to DNA. It may function in the SNF1 pathway. SIP3 contain an N-terminal Bin/Amphiphysin/Rvs (BAR) domain followed by a PH domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270098  Cd Length: 105  Bit Score: 60.35  E-value: 1.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 304 EKVGFLY---KKSDGIRRVWQKRKCGVK---YGCLTISHSTINrppV----KLTLLTCQVRPNPEE--KKCFDLVTHNR- 370
Cdd:cd13280   1 EKSGWLYmktSVGKPNRTIWVRRWCFVKngvFGMLSLSPSKTY---VeetdKFGVLLCSVRYAPEEdrRFCFEVKIFKDi 77
                        90       100
                ....*....|....*....|....*...
gi 19071867 371 TYHFQAEDEHECEAWVSVLQNSKDEALS 398
Cdd:cd13280  78 SIILQAETLKELKSWLTVFENAKRYALQ 105
PH pfam00169
PH domain; PH stands for pleckstrin homology.
307-390 7.51e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 306640  Cd Length: 105  Bit Score: 58.35  E-value: 7.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   307 GFLYKKSDGIRRVWQKRKCGVKYGCLTISHSTI----NRPPVKLTLLTCQVR-----PNPEEKKCFDLVTHN----RTYH 373
Cdd:pfam00169   5 GWLLKKGGGKKKSWKKRYFVLFDGSLLYYKDDKsgksKEPKGSISLSGCEVVevvapDSPKRKFCFELRTGErtggRTYL 84
                          90
                  ....*....|....*..
gi 19071867   374 FQAEDEHECEAWVSVLQ 390
Cdd:pfam00169  85 LQAESEEERKDWIKAIQ 101
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
616-674 9.21e-10

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 58.55  E-value: 9.21e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19071867 616 DAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKECEELL 674
Cdd:cd00204   1 NARDEDGRTPLHLAASNGHLEVVKLLLENGADVNAKDNDGRTPLHLAAKNGHLEIVKLL 59
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
590-681 1.08e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 59.45  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 590 LHLAVKVANQA--SLPLVDFIIQNGGHLDAKAA---DGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARK 664
Cdd:COG0666 110 LHLAALNGNPPegNIEVAKLLLEAGADLDVNNLrdeDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAK 189
                        90
                ....*....|....*..
gi 19071867 665 KHHKECEELLEQAQAGT 681
Cdd:COG0666 190 NGRIELVKLLLDKGLHL 206
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
301-389 3.99e-08

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270110  Cd Length: 106  Bit Score: 53.40  E-value: 3.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 301 FGTEKV---GFLYKKSDGiRRVWQK-----RKCGVKY------GCLTISHSTINrppvkltLLTCQVRPNPEEKKCFDLV 366
Cdd:cd13298   1 FEFDRVlksGYLLKRSRK-TKNWKKrwvvlRPCQLSYykdekeYKLRRVINLSE-------LLAVAPLKDKKRKNVFGIY 72
                        90       100
                ....*....|....*....|...
gi 19071867 367 THNRTYHFQAEDEHECEAWVSVL 389
Cdd:cd13298  73 TPSKNLHFRATSEKDANEWVEAL 95
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
590-642 4.17e-08

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 53.54  E-value: 4.17e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19071867 590 LHLAVKVANqasLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLL 642
Cdd:cd00204  77 LHLAARNGN---LDVVKLLLKHGADVNARDKDGRTPLHLAAKNGHLEVVKLLL 126
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
304-391 5.17e-08

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270073  Cd Length: 94  Bit Score: 52.77  E-value: 5.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 304 EKVGFLYKKS-DGIRRVWQKRkcGVKYGCLTISHSTINRPPVKLTL--LTC--QVRPNPEEKkcFDLVTHNRTYHFQAED 378
Cdd:cd13253   1 IKSGYLDKQGgQGNNKGFQKR--WVVFDGLSLRYFDSEKDAYSKRIipLSAisTVRAVGDNK--FELVTTNRTFVFRAES 76
                        90
                ....*....|...
gi 19071867 379 EHECEAWVSVLQN 391
Cdd:cd13253  77 DDERNLWCSTLQA 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
590-674 5.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984  Cd Length: 422  Bit Score: 56.21  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  590 LHLAVKVaNQASLPLVDFIIQNGGHLDAK--------------AAD--GNTALHYAALYNQPDCLKLLLKGRALVGTVNE 653
Cdd:PHA03100 145 LHLYLES-NKIDLKILKLLIDKGVDINAKnrvnyllsygvpinIKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
                         90       100
                 ....*....|....*....|.
gi 19071867  654 AGETALDIARKKHHKECEELL 674
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLL 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
608-662 7.98e-08

Ankyrin repeats (many copies);


Pssm-ID: 316380  Cd Length: 56  Bit Score: 51.60  E-value: 7.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19071867   608 IIQNGG-HLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIA 662
Cdd:pfam13857   1 LLENGPaDLNRLDGEGYTPLHLAAKYGALEIVRLLLKRGADLNLKDFRGLTALDLA 56
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
305-390 2.81e-07

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275402  Cd Length: 116  Bit Score: 50.70  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKSDgIRRVWQKRKCGVKYGCLTISHSTINR--P----PVKLTLLTCQVRPNPEEKKCFDLVTHNRTYHFQAED 378
Cdd:cd13215  23 KSGYLSKRSK-RTLRYTRYWFVLKGDTLSWYNSSTDLyfPagtiDLRYATSIELSKSNGEATTSFKIVTNSRTYKFKADS 101
                        90
                ....*....|..
gi 19071867 379 EHECEAWVSVLQ 390
Cdd:cd13215 102 ETSADEWVKALK 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
589-642 3.57e-07

Ankyrin repeats (many copies);


Pssm-ID: 316185  Cd Length: 54  Bit Score: 49.59  E-value: 3.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19071867   589 VLHLAvkvANQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLL 642
Cdd:pfam13637   4 ALHAA---AASGHLELLRLLLENGADINAVDGNGETALHFAASNGNVEVLKLLL 54
BAR_ACAP3 cd07637
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ...
49-240 8.40e-07

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3), also called centaurin beta-5, is presumed to be an Arf GTPase activating protein (GAP) based on its similarity to the Arf6-specific GAPs ACAP1 and ACAP2. The specific function of ACAP3 is still unknown. ACAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153321  Cd Length: 200  Bit Score: 50.38  E-value: 8.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  49 QAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLgnSHLSQNSHELSTGFLNLAVFTREVAALFKNLIQNLNNIVSFPL 128
Cdd:cd07637  15 EAKLDKLVKLCSGMIEAGKAYATTNKLFVSGIRDL--SQQCKKDEMISECLDKFGDSLQEMVNYHMILFDQAQRSVRQQL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 129 DSLMKGQLRDGRQdSKKQLEKAWKDYEAKMAKlekerdRARVTGGIPGEVAQ---DMQRERRIFQLHMCEYLLKAGESQM 205
Cdd:cd07637  93 HSFVKEDVRKFKE-TKKQFDKVREDLEIALVK------NAQAPRHKPHEVEEatsTLTITRKCFRHLALDYVLQINVLQA 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19071867 206 KQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFI 240
Cdd:cd07637 166 KKKFEILDSMLSFMHAQYTFFQQGYSLLHELDPYM 200
PLN03131 PLN03131
hypothetical protein; Provisional
436-541 2.24e-06

hypothetical protein; Provisional


Pssm-ID: 178677  Cd Length: 705  Bit Score: 51.32  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  436 PGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGvrfSRMQSLTLDLLGPSELLLALNMGNTSFNEV-------MEA 508
Cdd:PLN03131  21 PPNRRCINCNSLGPQFVCTNFWTFICMTCSGIHREFT---HRVKSVSMSKFTSQDVEALQNGGNQRAREIylkdwdqQRQ 97
                         90       100       110
                 ....*....|....*....|....*....|...
gi 19071867  509 QLPSHggpkpsaeSDMGTRRDYIMAKYVEHRFA 541
Cdd:PLN03131  98 RLPDN--------SKVDKIREFIKDIYVDKKYA 122
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
303-392 3.30e-06

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270105  Cd Length: 120  Bit Score: 47.62  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 303 TEKVGFLYKKSDgIRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLT-CQVRPNPEEKK-CFDLVTH---NRTYHFQAE 377
Cdd:cd13288   8 VDKEGYLWKKGE-RNTSYQKRWFVLKGNLLFYFEKKGDREPLGVIVLEgCTVELAEDAEPyAFAIRFDgpgARSYVLAAE 86
                        90
                ....*....|....*
gi 19071867 378 DEHECEAWVSVLQNS 392
Cdd:cd13288  87 NQEDMESWMKALSRA 101
Ank_4 pfam13637
Ankyrin repeats (many copies);
622-674 6.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 316185  Cd Length: 54  Bit Score: 45.74  E-value: 6.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 19071867   622 GNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKECEELL 674
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLENGADINAVDGNGETALHFAASNGNVEVLKLL 53
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
305-391 7.00e-06

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 46.52  E-value: 7.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKSdGIRRVWQKRKCGVKYGCLTI---SHSTINRPPVKLTLLT-CQVRPNpEEKKCFDLVTHNRTYHFQAEDEH 380
Cdd:cd13282   1 KAGYLTKLG-GKVKTWKRRWFVLKNGELFYyksPNDVIRKPQGQIALDGsCEIARA-EGAQTFEIVTEKRTYYLTADSEN 78
                        90
                ....*....|.
gi 19071867 381 ECEAWVSVLQN 391
Cdd:cd13282  79 DLDEWIRVIQN 89
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
302-396 7.54e-06

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270118  Cd Length: 113  Bit Score: 46.63  E-value: 7.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 302 GTEKVGFLYKK--SDGIRRVWQKRKCGVKYGCLTISHSTINRPP---VKLTLLTCQVRPNPEEKKCF-----DLVTHNRT 371
Cdd:cd13308   8 DVIHSGTLTKKggSQKTLQNWQLRYVIIHQGCVYYYKNDQSAKPkgvFSLNGYNRRAAEERTSKLKFvfkiiHLSPDHRT 87
                        90       100
                ....*....|....*....|....*
gi 19071867 372 YHFQAEDEHECEAWVSVLQNSKDEA 396
Cdd:cd13308  88 WYFAAKSEDEMSEWMEYIRREIDHY 112
PH2_MyoX cd13296
Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular ...
305-392 1.69e-05

Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270108  Cd Length: 103  Bit Score: 45.15  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKSDGI----RRVWQKRKCGVKYGCLTISHstiNRPPVKLTLLTCQVRPNPE------EKKCFDLVTHNRTYHF 374
Cdd:cd13296   1 KSGWLTKKGGGSstlsRRNWKSRWFVLRDTVLKYYE---NDQEGEKLLGTIDIRSAKEivdndpKENRLSITTEERTYHL 77
                        90
                ....*....|....*...
gi 19071867 375 QAEDEHECEAWVSVLQNS 392
Cdd:cd13296  78 VAESPEDASQWVNVLTRV 95
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
305-400 1.86e-05

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270075  Cd Length: 110  Bit Score: 45.10  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKsdGIRR-VWQKRKCGVKYGCLTISHSTINRPPVKL-------TLLTCQVRPNPEekkCFDLVTHNRTYHFQA 376
Cdd:cd13255   8 KAGYLEKK--GERRkTWKKRWFVLRPTKLAYYKNDKEYRLLRLidltdihTCTEVQLKKHDN---TFGIVTPARTFYVQA 82
                        90       100
                ....*....|....*....|....
gi 19071867 377 EDEHECEAWVSVLQNSKDEALSSA 400
Cdd:cd13255  83 DSKAEMESWISAINLARQALRATI 106
PLN03119 PLN03119
putative ADP-ribosylation factor GTPase-activating protein AGD14; Provisional
436-541 2.80e-05

putative ADP-ribosylation factor GTPase-activating protein AGD14; Provisional


Pssm-ID: 178666  Cd Length: 648  Bit Score: 47.53  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  436 PGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGvrfSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEAQLpSHGG 515
Cdd:PLN03119  21 PPNRRCINCNSLGPQYVCTTFWTFVCMACSGIHREFT---HRVKSVSMSKFTSKEVEVLQNGGNQRAREIYLKNW-DHQR 96
                         90       100
                 ....*....|....*....|....*.
gi 19071867  516 PKPSAESDMGTRRDYIMAKYVEHRFA 541
Cdd:PLN03119  97 QRLPENSNAERVREFIKNVYVQKKYA 122
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
621-653 4.89e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 306522  Cd Length: 33  Bit Score: 43.01  E-value: 4.89e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 19071867   621 DGNTALHYAALYNQPDCLKLLLKGRALVGTVNE 653
Cdd:pfam00023   1 DGNTPLHLAAREGNLEIVKLLLSKGADVNARDK 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
588-675 5.34e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 45.59  E-value: 5.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 588 LVLHLAVKVANQASlplVDFIIQNGGHLDAKAADGNTALHYAALYNQP-----DCLKLLLKGRA---LVGTVNEAGETAL 659
Cdd:COG0666  75 LPLHSAASKGDDKI---VKLLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGAdldVNNLRDEDGNTPL 151
                        90
                ....*....|....*..
gi 19071867 660 DIA-RKKHHKECEELLE 675
Cdd:COG0666 152 HWAaLNGDADIVELLLE 168
BAR_SFC_plant cd07606
The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC); BAR domains are ...
45-239 5.48e-05

The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC); 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. The plant protein SCARFACE (SFC), also called VAscular Network 3 (VAN3), is a plant ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein), an Arf GTPase Activating Protein (GAP) that plays a role in the trafficking of auxin efflux regulators from the plasma membrane to the endosome. It is required for the normal vein patterning in leaves. SCF contains an N-terminal BAR domain, followed by a Pleckstrin Homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153290  Cd Length: 202  Bit Score: 45.17  E-value: 5.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  45 LEGDQAIL----QRIKKAVRAiHSSGLGHV-ENEEQYREAVESLGNSHLSqnshELSTGFLNLAV--FT---REVAALFK 114
Cdd:cd07606   6 LEGSADELrdrsLKLYKGCRK-YRDALGEAyDGDSAFAESLEEFGGGHDD----PISVAVGGPVMtkFTsalREIGSYKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 115 NLIQNLNNIVSFPLDSLMKGQLRDGRqDSKKQLEKAWKDYEAKMAKLEKERDRARvtGGIPGEVAQDMQRERRIFQ---L 191
Cdd:cd07606  81 VLRSQVEHMLNDRLAQFADTDLQEVK-DARRRFDKASLDYEQARSKFLSLTKDAK--PEILAAAEEDLGTTRSAFEtarF 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19071867 192 HMCEYLLKAgESQMKQGpdFLQSLIKFFHAQHNFFQDGWKAAQSLFPF 239
Cdd:cd07606 158 DLMNRLHAA-DARKRVE--FLERLSGSMDAHLAFFKSGYELLRQLEPY 202
BAR_GRAF cd07636
The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; ...
107-239 6.22e-05

The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase (GRAF), also called Rho GTPase activating protein 26 (ARHGAP26), is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153320  Cd Length: 207  Bit Score: 45.05  E-value: 6.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 107 REVAALFKNL-------IQNLNNIVSFPLDSLMKGQLRDGRqDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGIPGEVA 179
Cdd:cd07636  70 QEFAAVLRNLedertrmIENASEVLITPLEKFRKEQIGAAK-EAKKKYDKETEKYCAVLEKHLNLSSKKKESQLHEADSQ 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 180 QDMQRERrIFQLHMcEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPF 239
Cdd:cd07636 149 VDLVRQH-FYEVSL-EYVFKVQEVQERKMFEFVEPLLAFLQGLFTFYHHGYELAKDFSDF 206
PH_Skap_family cd13266
Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain; Skap adaptor ...
305-386 1.24e-04

Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain; Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270086  Cd Length: 106  Bit Score: 42.51  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKS-DG--IRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLT-CQVRPNPEEKK------CFDLVTHN-RTYH 373
Cdd:cd13266   3 KAGYLEKRRkDHsfFGSEWQKRWCAISKNVFYYYGSDKDKQQKGEFAINgYDVRMNPTLRKdgkkdcCFELVCPDkRTYQ 82
                        90
                ....*....|...
gi 19071867 374 FQAEDEHECEAWV 386
Cdd:cd13266  83 FTAASPEDAEDWV 95
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
343-390 2.43e-04

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269977  Cd Length: 96  Bit Score: 41.54  E-value: 2.43e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19071867 343 PVK-LTLLTC---QVRPNPEEKKCFDLVTHNRTYHFQAEDEHECEAWVSVLQ 390
Cdd:cd10573  42 PIRvLDLRECssvQRDYSQGKVNCFCLVFPERTFYMYANTEEEADEWVKLLK 93
BAR_ACAP1 cd07639
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ...
43-236 8.67e-04

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 1), also called centaurin beta-1, is an Arf6-specific GTPase activating protein (GAP) which mediates Arf6 signaling. Arf6 is involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration. ACAP1 also participates in the cargo sorting and recycling of the transferrin receptor and integrin beta1. It may also play a role in innate immune responses. ACAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153323  Cd Length: 200  Bit Score: 41.44  E-value: 8.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  43 EILEGDQAILQ-RIKKAVRAIHS---SGLGHVENEEQYREAVESLGnsHLSQNSHELSTGFLNLAVFTREVAALFKNLIQ 118
Cdd:cd07639   5 EEVEAEVSELEtRLEKLVKLGSGmleGGRHYCAASRAFVDGLCDLA--HHGPKDPMMAECLEKFSDGLNHILDSHAELLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 119 NLNNIVSFPLDSLMKGQLRdGRQDSKKQLEKAWKDYEAKMAK-LEKERDRARVTGgipgEVAQDMQRERRIFQLHMCEYL 197
Cdd:cd07639  83 ATQFSFKQQLQLLVKEDLR-GFRDARKEFERGAESLEAALQHnAETPRRKAQEVE----EAAAALLGARATFRDRALDYA 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19071867 198 LKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSL 236
Cdd:cd07639 158 LQINVIEDKKKFDILEFMLQLMEAQASFFQQGHEALSAL 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
621-643 1.01e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603  Cd Length: 30  Bit Score: 39.11  E-value: 1.01e-03
                           10        20
                   ....*....|....*....|...
gi 19071867    621 DGNTALHYAALYNQPDCLKLLLK 643
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
621-646 3.00e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 316158  Cd Length: 30  Bit Score: 37.65  E-value: 3.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 19071867   621 DGNTALHYAALYNQPDCLKLLLKGRA 646
Cdd:pfam13606   1 DGNTPLHLAARNGRLEVVKLLLELGA 26
PHA03095 PHA03095
ankyrin-like protein; Provisional
598-661 3.65e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980  Cd Length: 471  Bit Score: 40.78  E-value: 3.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19071867  598 NQASLPLVDFIIQNGGHLDAKAADGNTALH-YAALYN-QPDCLKLLLKGRALVGTVNEAGETALDI 661
Cdd:PHA03095  93 NATTLDVIKLLIKAGADVNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA03095 PHA03095
ankyrin-like protein; Provisional
590-661 3.84e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980  Cd Length: 471  Bit Score: 40.39  E-value: 3.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19071867  590 LHLAVKVANQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQ-PDCLKLLLKGRALVGTVNEAGETALDI 661
Cdd:PHA03095  51 LHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHV 123
PH2_ARAP cd13254
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
359-390 4.26e-03

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 2; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the second PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270074  Cd Length: 90  Bit Score: 37.78  E-value: 4.26e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 19071867 359 EKKCFDLVTHNRTYHFQAEDEHECEAWVSVLQ 390
Cdd:cd13254  59 DRRSFDLTTPYRSFSFTAESEHEKQEWIEAVQ 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
551-642 6.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205  Cd Length: 434  Bit Score: 39.56  E-value: 6.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  551 LWTAICNRDLLSVLEAFANGQDFGqpLPGPDAQAPeelvLHLAVKvanQASLPLVDFIIQNGGHLDAKAADGNTALHYAA 630
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYP----IHIAIK---HNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         90
                 ....*....|..
gi 19071867  631 LYNQPDCLKLLL 642
Cdd:PHA02874 199 EYGDYACIKLLI 210
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
723-897 7.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039  Cd Length: 1352  Bit Score: 40.15  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   723 SGRLDISNKTYETVASLGAATPQGESEDCPPPLPVKNSSRTLVQGCARHASGDR--SEVSSLSSEAPETPESLGSPasss 800
Cdd:PHA03307  227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSrpGPASSSSSPRERSPSPSPSS---- 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867   801 slmsplePGDPSQAPPNSEEGLREPPGTSRPSLTSGTTPSEMYLPVRFSSESTRSyrrgARSPEDGPSARQPLPRRNVPV 880
Cdd:PHA03307  303 -------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS----PSPSRPPPPADPSSPRKRPRP 371
                         170
                  ....*....|....*..
gi 19071867   881 GITEGDGSRTGSLPASS 897
Cdd:PHA03307  372 SRAPSSPAASAGRPTRR 388
PHA02878 PHA02878
ankyrin repeat protein; Provisional
590-668 7.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939  Cd Length: 477  Bit Score: 39.48  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867  590 LHLAVKVANQaslPLVDFIIQNGGHLDAKAADGNTALHYAALY-NQPDCLKLLLKGRALVGTVNEA-GETALDIARKKHH 667
Cdd:PHA02878 205 LHHAVKHYNK---PIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER 281

                 .
gi 19071867  668 K 668
Cdd:PHA02878 282 K 282
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
305-387 7.87e-03

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 36.91  E-value: 7.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071867 305 KVGFLYKKSDGIRrVWQKR----KCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEK----KCFDLVTHNRTYHFQA 376
Cdd:cd13276   1 KAGWLEKQGEFIK-TWRRRwfvlKQGKLFWFKEPDVTPYSKPRGVIDLSKCLTVKSAEDAtnkeNAFELSTPEETFYFIA 79
                        90
                ....*....|.
gi 19071867 377 EDEHECEAWVS 387
Cdd:cd13276  80 DNEKEKEEWIG 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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